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Information on EC 3.4.11.18 - methionyl aminopeptidase
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EC Tree
3.4.11.18 methionyl aminopeptidaseSpecify your search results
Word Map
- 3.4.11.18
-
microtubule-associated
- microtubule
- dendritic
- hippocampus
- tubulin
- protein-2
- tau
- cerebral
- aminopeptidases
- fumagillin
- nestin
-
neurite
- cortical
- cytoskeletal
- neurofilament
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neuroprotective
- ischemia
-
fibrillary
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synaptophysin
-
outgrowth
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neurotrophic
-
neuron-specific
- beta-tubulin
-
neurogenesis
- map2
- synapsin
-
antiangiogenic
-
deformylase
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microtubule-binding
- calbindin
- synthesis
-
dinuclear
-
microsporidian
- drug development
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
map-2, metap2, metap, methionine aminopeptidase, metap-2, metap1, methionine aminopeptidase 2, methionine aminopeptidase-2, metap-1, methionyl aminopeptidase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aminopeptidase, methionine
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CoCoEcMetAP
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dicobalt form of the methionine aminopeptidase from Escherichia coli
initiation factor 2 associated 67 kDa glycoprotein
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L-methionine aminopeptidase
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LdBPK_210960
MAP
MAP-2
MAP11
mAPA
MapB
MetAP
MetAP-1
MetAP-2
MetAP-I
MetAP1
MetAP1a
MetAP1c
MetAP2
methionine amino peptidase type 2
methionine aminopeptidase
methionine aminopeptidase 1
methionine aminopeptidase 1b
methionine aminopeptidase 2
methionine aminopeptidase AbMetAPx
methionine aminopeptidase AbMetAPy
methionine aminopeptidase type 2
methionine aminopeptidase type II
methionine aminopeptidase type-2
methionine aminopeptidase-1
methionine aminopeptidase-2
p67
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p67eIF2
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peptidase M
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PVX_094985
type I MetAP
type I methionine aminopeptidase
additional information
MAP
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MetAP
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MetAP-1
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MetAP-2
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MetAP1
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MetAP2
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MetAP2
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methionine aminopeptidase
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methionine aminopeptidase
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methionine aminopeptidase
nuclear localization signal at C-terminal end
additional information
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MetAP belongs to the family of dinuclear metallohydrolases
additional information
MetAP is one of the dinuclear metallohydrolases
additional information
MetAP is one of the dinuclear metallohydrolases
-
additional information
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eukaryotes contain both the type I and the type II MetAPs, whereas prokaryotes possess only the type I enzyme
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
peptide + H2O = N-terminal amino acid + peptide, preferentially methionine, further reaction: arylamide + H2O = aromatic hydrocarbon + amine
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-
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release of N-terminal amino acids, preferentially methionine, from peptides and arylamides
reaction mechanism of monometalated enzyme. Charge-charge interactions involving D97 and D108 position and bind substrate. E204 acts as general base
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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PATHWAY SOURCE
PATHWAYS
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,
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CAS REGISTRY NUMBER
COMMENTARY
61229-81-0
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
14-3-3gamma protein + H2O
?
14-3-3gamma is a shared substrate between isoform MetAP1 and MetAP2 in HUVEC cells
-
-
?
L-alanine-4-methylcoumarin-7-amide + H2O
L-alanine + 7-amino-4-methylcoumarin
-
-
-
?
L-leucine-4-methylcoumarin-7-amide + H2O
L-leucine + 7-amino-4-methylcoumarin
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-
-
?
L-Met-L-Ala-L-Ser
L-Met + L-Ala-L-Ser
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isoform MAP, 77% of the activity with L-Met-Gly-L-Met-L-Met, isoform YflG, 18% of the activity with L-Met-Gly-L-Met-L-Met
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-
?
L-Met-L-Gln-L-Asp-onconase + H2O
L-Met + L-Gln-L-Asp-onconase
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wild-type, no substrate, mutant M206G/Q233G, 96% of Met removal, mutant M206T/Q233G, 91% of removal, mutant M206T/Q233T, 93% of removal
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-
?
L-Met-L-Pro-4-nitroanilide + H2O
L-Met + L-Pro-4-nitroaniline
-
-
-
?
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp + H2O
L-Met + L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp
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-
-
-
?
L-methionyl-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
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-
-
-
?
Leu-Gly-Gly + H2O
?
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34% of the activity with Met-Ala-Ser
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-
?
Leu-Leu-Tyr + H2O
?
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32% of the activity with Leu-Gly-Gly
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-
?
Leu-Ser-Phe + H2O
?
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30% of the activity with Met-Ala-Ser
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-
?
MAPLDLDRWGRPVGRRRRPVRVYP-OH + H2O
L-methionine + APLDLDRWGRPVGRRRRPVRVYP-OH
sequence corresponds to the N-terminus of the human serine/threonine-protein phosphatase 6 catalytic subunit protein
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-
?
Met-Ala-His-Thr-Leu-Pro-Glu-Glu-Leu + H2O
Met + Ala-His-Thr-Leu-Pro-Glu-Glu-Leu
-
-
-
-
?
Met-Ala-Pro-Thr-Ser-Ser-Ser-Thr-Lys-Lys-Thr-Gln-Leu + H2O
Met + Ala-Pro-Thr-Ser-Ser-Ser-Thr-Lys-Lys-Thr-Gln-Leu
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-
-
-
?
Met-Ala-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Ala-Ser-His-Arg-Trp-Asp-Trp
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-
-
-
?
Met-Arg-Phe + H2O
Met + Arg-Phe
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substrate of isozymes c1MetAP-Ia and c3MetAP-Ib, no activity with isozyme c2MetAP-Ia
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-
?
Met-Asp-Gly + H2O
Met + Asp-Gly
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substrate of isozyme c3MetAP-Ib, no activity with the other two isozymes
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-
?
Met-Gly-Ala-Gln-Phe-Ser-Lys-Thr + H2O
Met + Gly-Ala-Gln-Phe-Ser-Lys-Thr
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-
-
?
Met-Gly-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Gly-Ser-His-Arg-Trp-Asp-Trp
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-
-
-
?
Met-Leu-Gly + H2O
Met + Leu-Gly
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substrate of isozymes c1MetAP-Ia and c3MetAP-Ib, no activity with isozyme c2MetAP-Ia
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-
?
Met-Met-Ala + H2O
Met + Met-Ala
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substrate of isozymes c1MetAP-Ia and c3MetAP-Ib, no activity with isozyme c2MetAP-Ia
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-
?
Met-Pro-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Pro-Ser-His-Arg-Trp-Asp-Trp
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?
Met-Pro-Thr-Ser-Ser-Ser-Thr-Lys-Lys-Thr-Gln-Leu-Cys + H2O
Met + Pro-Thr-Ser-Ser-Ser-Thr-Lys-Lys-Thr-Gln-Leu-Cys
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-
-
-
?
Met-Ser-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Ser-Ser-His-Arg-Trp-Asp-Trp
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-
-
?
Met-Thr-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Thr-Ser-His-Arg-Trp-Asp-Trp
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-
-
-
?
Met-Val-His-Thr-Leu-Pro-Glu-Glu-Leu + H2O
Met + Val-His-Thr-Leu-Pro-Glu-Glu-Leu
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-
-
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?
Met-Val-Ser-His-Arg-Trp-Asp-Trp + H2O
Met + Val-Ser-His-Arg-Trp-Asp-Trp
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?
Met-[2-mercapto-ethanoyl]-Phe + H2O
[2-mercapto-ethanoyl]-Phe + Met
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?
MGKVKVGV + H2O
L-Met + GKVKVGV
N-terminal peptide of glyceraldehyde 3-phosphate dehydrogenase
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?
MGNLKSVA + H2O
L-Met + GNLKSVA
N-terminal peptide of endothelial nitric oxide synthase
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?
MTNKSSLKNN-OH + H2O
L-methionine + TNKSSLKNN-OH
sequence corresponds to the N-terminus of the yeast VHS3 protein
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?
Nle-Gly-Met-Phe + H2O
Gly-Met-Phe + norleucine
KT943909
zinc-activated einzyme shows 159% of the activity with substrate Nle-Gly-Met-Phe
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?
glutathione-S-transferase + H2O
?
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removal of Met(init) from glutathione-S-transferase. Processing of glutathione-S-transferase in yeast relies almost entirely on MetAP1 function
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?
glyceraldehye 3-phosphate dehydrogenase + H2O
?
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MetAP2-specific substrate
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?
glyceraldehye 3-phosphate dehydrogenase + H2O
?
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MetAP2-specific substrate
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?
L-Met 4-nitroanilide + H2O
L-Met + 4-nitroaniline
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?
L-Met 4-nitroanilide + H2O
L-Met + 4-nitroaniline
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?
L-Met 4-nitroanilide + H2O
L-Met + 4-nitroaniline
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?
L-Met 4-nitroanilide + H2O
L-Met + 4-nitroaniline
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?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
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?
L-Met-7-amido-4-methylcoumarin + H2O
L-Met + 7-amino-4-methylcoumarin
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?
L-Met-Gly-L-Met-L-Met + H2O
L-Met + Gly-L-Met-L-Met
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?
L-Met-L-Pro-p-nitroanilide + H2O
L-Met + L-Pro-p-nitroanilide
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?
L-Met-p-nitroanilide + H2O
L-Met + p-nitroaniline
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
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?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
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?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
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?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
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?
L-methionine 4-methylcoumaryl-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
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?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
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?
L-methionine 4-nitroanilide + H2O
L-methionine + 4-nitroaniline
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?
L-methionine-4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
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?
L-methionine-4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
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fluorogenic substrate
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?
L-methionine-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
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?
L-methionine-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
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?
L-methionine-7-amido-4-methylcoumarin + H2O
L-methionine + 7-amino-4-methylcoumarin
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?
L-methionyl 4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
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fluorogenic substrate
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?
L-methionyl 4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
fluorogenic substrate
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?
L-methionyl 4-methylcoumarin-7-amide + H2O
L-methionine + 7-amino-4-methylcoumarin
fluorogenic substrate
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?
Met-4-methylcoumaryl-7-amide + H2O
Met + 7-amino-4-methylcoumarin
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?
Met-4-methylcoumaryl-7-amide + H2O
Met + 7-amino-4-methylcoumarin
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?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
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?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
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?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
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?
Met-7-amido-4-methylcoumarin + H2O
Met + 7-amino-4-methylcoumarin
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?
Met-Ala-Ser + H2O
Met + Ala-Ser
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also cleaves methionine from other tripeptides with a relatively small and/or uncharged penultimate amino acid residue (Pro, Gly, Val, Thr, or Ser) but not if bulky and/or charged (Arg, His, Leu, Met, or Tyr)
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-
?
Met-Lys-bradykinin + H2O
Met + Lys-bradykinin
-
i.e. Met-Lys-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
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-
?
Met-peptide + H2O
Met + peptide
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the enzyme removes the N-terminal Met from polypeptides, and thus plays a key role in protein synthesis, modification and transport
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-
?
Met-peptide + H2O
Met + peptide
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the enzyme catalyzes the removal of an amino-terminal methionine from a newly synthesized polypeptide
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?
Met-peptide + H2O
Met + peptide
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the enzyme is directly involved in the regulation of growth factor-stimulated endothelial cell proliferation
-
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?
Met-peptide + H2O
Met + peptide
-
the biological function is removing the terminal methionine from nascent peptides
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-
?
Met-peptide + H2O
Met + peptide
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the biological function is removing the terminal methionine from nascent peptides during protein synthesis
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-
?
Met-peptide + H2O
Met + peptide
-
the enzyme is responsible for hydrolysis of the initiator methionine residue from the majority of newly synthesized proteins. Potentially important role in the production of recombinant proteins, since failure to correctly remove initiator methionine residues can result in a product that is inactive or immunogenic
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-
?
SH3 binding glutamic acid rich-like protein + H2O
?
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MetAP2-specific substrate
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?
SH3 binding glutamic acid rich-like protein + H2O
?
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MetAP2-specific substrate
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-
?
additional information
?
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active site structure and substrate binding, overview
-
-
?
additional information
?
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-
no substrates: Gly 4-nitroanilide , Ala 4-nitroanilide, Ser 7-amido-4-methyl-coumarin, Leu 4-nitroanilide, Glu 4-nitroanilide, Lys 4-nitroanilide and Arg 4-nitroanilide
-
-
?
additional information
?
-
active site structure and substrate binding, overview
-
-
?
additional information
?
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-
active site structure and substrate binding, overview
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-
?
additional information
?
-
active site structure and substrate binding, overview
-
-
?
additional information
?
-
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residues adjacent to the initiation methionine can significantly influence the methionine cleavage process
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?
additional information
?
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detailed analysis of mutants specificity on oligo- and protein substrates
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?
additional information
?
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enzyme hydrolyzes N-terminal L-methionine when the next amino acid is L-alanine, L-proline, or L-serine with substrate preference in decreasing order: proloine, alanine, serine. enzyme hydrolyzes the Xaa-Po peptide bond when the first amino acid is L-alanine, L-asparagine, or L-methionine
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?
additional information
?
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peptides with Val or Thr at P1' are much less efficiently cleaved than those with Ala, Cys, Gly, Pro, or Ser in this position
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?
additional information
?
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substrate specificity is systematically profiled by screening against a combinatorial peptide library and kinetic analysis of individually synthesized peptide substrates
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?
additional information
?
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while the nature of the P1' residue of peptide substrates dictates the substrate specificity in the active site of metAP2 the P2' residue appears to play a key role in the kinetics of peptidolysis. The catalytic efficiency of dipeptide substrates is at least 250fold lower than those of the tripeptides. When the P1' amino acid of the peptide substrate is sterically large such as with L-Leu, MetAP2 exhibits no detectable activity. L-Nle is the only amino acid residue other than L-Met that can be accomodated at the N-terminus of a substrate
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-
?
additional information
?
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together with N-myristoyltransferase, enzyme plays a major role in the process of myristoylation of oncoproteins including the c-src family
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-
?
additional information
?
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no activity when using Glu-Ala-Ser and Leu-Ala-Ser peptides as substrates
-
-
?
additional information
?
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active site strutcure and substrate binding, overview
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-
?
additional information
?
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substrate specificity is systematically profiled by screening against a combinatorial peptide library and kinetic analysis of individually synthesized peptide substrates
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-
?
additional information
?
-
among the 4-methylcoumarin-7-amides tested, activity is highest with L-alanine 4-methylcoumarin-7-amide
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-
?
additional information
?
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among the 4-methylcoumarin-7-amides tested, activity is highest with L-alanine 4-methylcoumarin-7-amide
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-
?
additional information
?
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isozyme substrate specificity, overview
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-
?
additional information
?
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MetAP carries out the cotranslational N-terminal methionine excision
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-
?
additional information
?
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the enzyme hydrolyzes NH2-terminal methionine from methionyl peptides longer than tetrapeptides and from shorter methionyl peptides with blocked carboxy ends
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-
?
additional information
?
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the isozymes act on peptides in the cytosol, that are N-terminal fragments from digestion of hemoglobin in the digestive vacuole. The hemoglobin-derived peptides show leucine and alanine as most abundant amino acids
-
-
?
additional information
?
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the enzyme shows preference for synthetic peptides containing leucine and alanine
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-
?
additional information
?
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removes methionine from hemoglobin nascent peptides
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?
additional information
?
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specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of glutamic acid
-
-
?
additional information
?
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specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of threonine
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of lysine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of valine
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of asparagine
-
-
?
additional information
?
-
-
no activity with methionine 4-nitroanilide
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of aspartic acid
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of proline
-
-
?
additional information
?
-
-
the mutant enzyme prefers substrates, having Ser or Pro at P1', over substrates that contain glycine and alanine at that position. The wild-type enzyme prefers substrates that have Ala, Gly, Ser or Pro at P1'. Amino-terminal Met cannot be removed by either the mutant or wild-type enzyme from substrates having large and charged amino acids at P1' position
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of leucine
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of isoleucine
-
-
?
additional information
?
-
-
removal of the initiator methionine if the penultimate residue has a small radius of gyration (Gly, Ala, Ser, Thr, Pro, Val and Cys)
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of arginine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of serine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of glycine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of alanine
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of glutamine
-
-
?
additional information
?
-
no substrates: 4-nitroanilides of Val, Arg, Leu, Glu, Gly, Lys, Phe, Pro,Tyr, Ile
-
-
?
additional information
?
-
-
no substrates: 4-nitroanilides of Val, Arg, Leu, Glu, Gly, Lys, Phe, Pro,Tyr, Ile
-
-
?
additional information
?
-
no substrates: 4-nitroanilides of Val, Arg, Leu, Glu, Gly, Lys, Phe, Pro,Tyr, Ile
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of lysine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of valine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of proline
-
-
?
additional information
?
-
-
specificity: the enzyme does not cleave amino-terminal methionine when it precedes residues of leucine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of serine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of glycine
-
-
?
additional information
?
-
-
specificity: the enzyme cleaves amino-terminal methionine when it precedes residues of alanine
-
-
?
additional information
?
-
-
substrate specificities of recombinant isozymes, overview, no activity towards tripeptides in which the N-terminal amino acid is not Met, no activity with Pro-Met and X-Gly-Gly peptides
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glutathione-S-transferase + H2O
?
-
removal of Met(init) from glutathione-S-transferase. Processing of glutathione-S-transferase in yeast relies almost entirely on MetAP1 function
-
-
?
Met-peptide + H2O
Met + peptide
-
the enzyme removes the N-terminal Met from polypeptides, and thus plays a key role in protein synthesis, modification and transport
-
-
?
Met-peptide + H2O
Met + peptide
-
the enzyme catalyzes the removal of an amino-terminal methionine from a newly synthesized polypeptide
-
-
?
Met-peptide + H2O
Met + peptide
-
the enzyme is directly involved in the regulation of growth factor-stimulated endothelial cell proliferation
-
-
?
Met-peptide + H2O
Met + peptide
-
the biological function is removing the terminal methionine from nascent peptides
-
-
?
Met-peptide + H2O
Met + peptide
-
the biological function is removing the terminal methionine from nascent peptides during protein synthesis
-
-
?
Met-peptide + H2O
Met + peptide
-
the enzyme is responsible for hydrolysis of the initiator methionine residue from the majority of newly synthesized proteins. Potentially important role in the production of recombinant proteins, since failure to correctly remove initiator methionine residues can result in a product that is inactive or immunogenic
-
-
?
additional information
?
-
-
together with N-myristoyltransferase, enzyme plays a major role in the process of myristoylation of oncoproteins including the c-src family
-
-
?
additional information
?
-
-
the isozymes act on peptides in the cytosol, that are N-terminal fragments from digestion of hemoglobin in the digestive vacuole. The hemoglobin-derived peptides show leucine and alanine as most abundant amino acids
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
Mg2+
Mn2+
Ni2+
Zinc
Zn2+
additional information
Co2+
-
required, both isoform MAP and YflG. YflG shows strong preference for Co2+
Co2+
-
absolutely required, maximal enzyme activity is observed at 3.0 molar equivalents
Co2+
-
in mutant enzymes D97A and E204V cobalt content is not detectable, in mutant enzyme H171L and 235V the cobalt content is 3% of that of the wild-type enzyme, in mutant enzyme D108A the cobalt content is 6% of that of the wild-type enzyme
Co2+
-
maximal activity is observed after addition of only 1 equivalent of divalent metal ion, the metal binding constant for the first binding event is 0.0003 mM for Co(II)-substituted enzyme. The metal ion resides in a pentacoordinate geometry
Co2+
-
the active site contains two Co2+, ligated by the side chains of Asp97, Asp108, Glu204, Glu235, and His171 with approximate octahedral coordination
Co2+
enzyme binds up to 1.1 equivalents of Co2+ in the metal concentration range found in vivo. Dissociation constant is about 0.0025-0.004 mM
Co2+
-
the dicobalt form of the methionine aminopeptidase has an active site with one 5-coordinate Co2+ and a more weakly bound 6-coordinate Co2+
Co2+
-
the kcat value increases as a function of Co2+ ion concentration and exhibits a maximum after the addition of one equivalent of Co2+
Co2+
-
activates, two metal ions are coordinated by five conserved amino acid residues D97, D108, H171, E204 and E235, activation kinetics, overview
Co2+
-
stimulates activity of MetAP2 with Met-Ala-Ser or Met-Gly-Ala-Gln-Phe-Ser-Lys-Thr 10-20fold, maximal stimulation at 0.01 mM. In presence of 5 mM glutathione 30-40fold stimulation
Co2+
-
at low concentrations, 0.01 mM, Co2+ plays a key role in the stimulation of enzyme activity. It is still questionable that Co(II) is the physically relevant divalent cation
Co2+
significant activation at 0.01 mM, at least two Co2+ ions, which may act cooperatively, are needed to promote catalysis
Co2+
-
determination of metal affinity to the active site of the metalloenzyme by onlinear curve fitting of metal titration curves using the multiple independent binding sites, MIBS, model, overview
Co2+
and Ni2+, best activators. Highest activity at 0.1 mM
Co2+
may substitute for Ni2+. Highest activity at 0.04 mM
Co2+
-
the mutant enzyme contains 0.43 mol of Co2+ per mol. The wild-type enzyme contains 0.75 mol of Co2+ per mol of enzyme
Co2+
-
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
Co2+
-
loosely associated with the enzyme protein
Fe2+
activator after removal of divalent metal ions with Chelex-100
Fe2+
activator after removal of divalent metal ions with EDTA
Fe2+
-
maximal activity is observed after addition of only 1 equivalent of divalent metal ion, the metal binding constant for the first binding event is 0.0002 mM for Fe(II)-substituted enzyme. The metal ion resides in a pentacoordinate geometry
Fe2+
Fe2+ is the likely metal cofactor used by MetAP in the cellular environment
Mn2+
-
stimulates activity of MetAP2 with Met-Ala-Ser or Met-Gly-Ala-Gln-Phe-Ser-Lys-Thr 10-20fold, maximal stimulation at 0.001 mM. In presence of 5 mM glutathione 30-40fold stimulation
Mn2+
may substitute for Co2+ or Ni2+, highest activity at 0.4 mM
Mn2+
enzyme contains 2 Mn-ions residing in a distorted trigonal bipyramidal geometry. A bridging water molecule is displaced by L-methionine
Ni2+
activator after removal of divalent metal ions with Chelex-100
Ni2+
activator after removal of divalent metal ions with EDTA, less efficient than Fe2+
Ni2+
-
may substitute for Co2+, maximal enzyme activity is observed at 10.0 molar equivalents
Ni2+
-
activates apoenzyme with Met-7-amido-4-methylcoumarin as substrate, very poor activity in presence of Met-S-Gly-Phe as substrate
Ni2+
and Co2+, best activators. Highest activity at 0.1 mM
Ni2+
-
enzyme is active at concentrations below 0.002 mM, inhibition at higher concentrations
Zinc
-
methionine aminopeptidase type 1 requires its N-terminal zinc finger domain for normal function in vivo
Zinc
-
1 mol of wild-type enzyme contains 2 mol of Zn2+, zinc fingers are essential for normal MAP function
Zn2+
-
may substitute for Co2+, maximal enzyme activity is observed at 10.0 molar equivalents. Activity with Zn2+ is not dependent on pH
Zn2+
-
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mol of cobalt ion
additional information
-
MetAP belongs to the dinuclear metallohydrolases, mathematical model and detailed analysis of the stoichiometric activation of MetAP by metal cofactors, overview
additional information
-
MetAP can be activated in vitro by a number of divalent metals
additional information
-
MetAp requires divalent metal ions for catalytic activity
additional information
Zn(II)-activated MAP2 shows negligible amidolytic activity
additional information
-
Zn(II)-activated MAP2 shows negligible amidolytic activity
additional information
MetAP is one of the dinuclear metallohydrolases. MetAP1c requires divalent cations for activity. Co2+ and Fe2+ show the tightest binding, while Ni2+ is the most efficient cofactor for the catalysis. Metal binding kinetics, overview
additional information
-
MetAP is one of the dinuclear metallohydrolases. MetAP1c requires divalent cations for activity. Co2+ and Fe2+ show the tightest binding, while Ni2+ is the most efficient cofactor for the catalysis. Metal binding kinetics, overview
additional information
-
not activating: Ni2+, Mg2+, Ca2+, Cd2+, Cu2+
additional information
-
the purified preparations do not contain significant amounts of any metal. Enzymatically important metal is loosely associated and lost during enzyme purification
additional information
-
activating potencies of divalent metal ions with the three isozymes, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E,4E,6E,8E)-10-((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-10-oxodeca-2,4,6,8-tetraenoic acid
-
-
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[(1-isobutyrylpiperidin-3-yl)-methyl]-2-methoxy-8,8-dimethylnon-6-enamide
-
-
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[2-(mesityloxy)ethyl]-2-methoxy-8,8-dimethylnon-6-enamide
-
-
(2R,3R,4S,5R,E)-N-(2,3-dihydro-1H-inden-2-yl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
-
-
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
-
-
(2R,3R,4S,5R,E)-N-[3-(4-fluorophenyl)-3-(furan-2-yl)propyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
-
-
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
-
-
(2R,3R,4S,5R,E)-N-[[1-(cyclopropanecarbonyl)piperidin-3-yl]methyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
-
-
(3E)-3-(furan-2-ylmethylidene)-5-(hydroxymethyl)-1-methoxy-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]bicyclo[3.1.0]hexan-2-one
no activity at 0.1 mM
(3R)-amino-(2S)-hydroxypentanoic acid
-
IC50: 0.0123 mM for the Co2+-substituted enzyme, 0.0115 mM for the Mn2+-substituted enzyme, 0.0093 mM for the Zn2+-substituted enzyme, 0.0223 for the Ni2+-substituted enzyme
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-ol
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (2R)-3-methyl-1-(2-(1-methylpyrrolidin-2-yl)ethylamino)-1-oxobutan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-1-amino-3-methyl-1-oxobutan-2-yl carbamate
-
i.e. PPI-2458, advanced into phase I clinical studies in non-Hodgkin's lymphoma and solid cancers, overview
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-1-amino-3-methyl-1-oxobutan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-1-hydroxy-3-methylbutan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-3-methyl-1-(morpholinoamino)-1-oxobutan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-3-methyl-1-oxo-1-(2-(pyrrolidin-1-yl)ethylamino)butan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 1-amino-2-methyl-1-oxopropan-2-ylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 1-carbamoylcyclopentylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 2-(1-methylpyrrolidin-2-yl)ethylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 2-(pyrrolidin-1-yl)ethylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl isopropylcarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl morpholinocarbamate
-
-
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl tert-butylcarbamate
-
-
(3R,5S,6R)-5-methoxy-4-[(3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]oct-6-yl (chloroacetyl)carbamate
-
-
(5,5-Dimethyl-4,5-dihydro-thiazol-2-yl)-(3-methyl-pyridin-2-yl)-amine
-
IC50 for Co-EcMetAP1: 0.00021 mM
(8S)-2-[[(4-fluorophenyl)sulfonyl]amino]-8-methyl-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
-
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-2-phenylacetate
-
-
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-3-methylbutanoate
-
-
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-4-methylpentanoate
-
-
(S)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)-3-methylbutanoate
-
-
1-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonyl)-piperidine-4-carboxylic acid
-
-
1-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)-2-(2-sulfanylmorpholin-4-yl)ethanone
-
-
1-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)-2-(2-sulfanylphenyl)ethanone
-
-
1-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)-2-(4-fluoro-2-sulfanylphenyl)ethanone
-
-
1-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)-2-(4-methoxy-2-sulfanylphenyl)ethanone
-
-
1-(5-chloro-6-methyl-2-pyridin-2-ylpyrimidin-4-yl)-4-(2,4-dichlorobenzyl)-1,4-diazepane
-
1-benzyl-2-pyridin-2-yl-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00099 mM
1-methoxy-5-(methoxymethyl)-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]bicyclo[3.1.0]hexan-2-one
no activity at 0.1 mM
1-[2-pyridin-2-yl-6-(trifluoromethyl)-3,4-dihydropyrimidin-4-yl]propane-2-thiol
-
-
2,2'-bipyridine
-
maximum inhibition is observed in the presence of CoCl2 rather than other metal ions
2-((1,3-thiazol-2-ylamino)carbonyl)pyridin-3-yl phenylacetate
-
Co(II)-form of enzyme, 50% inhibition at 0.00046 mM
2-((1H-1,2,4-triazol-5-ylthio)methyl)benzonitrile
-
Co(II)-form of enzyme, 50% inhibition at 0.00066 mM
2-(1,3-thiazol-4-yl)-1H-imidazo(4,5-c)pyridine
Co(II)-form of enzyme, 50% inhibition at 0.00172 mM
2-(1H-benzimidazol-2-ylamino)pyridin-3-ol
Co(II)-form of enzyme, 50% inhibition at 0.00078 mM
2-(2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)ethyl)-1,1-dimethylpyrrolidinium iodide
-
-
2-(2-aminoethoxy)-3-ethyl-6-[[(2-propylphenyl)sulfonyl]amino]benzoic acid
-
2-(2-aminoethoxy)-3-ethyl-6-[[(4-fluorophenyl)sulfonyl]amino]benzoic acid
-
2-(2-aminoethoxy)-6-[([2-[3-(diethylamino)propyl]-4-fluorophenyl]sulfonyl)amino]-3-ethylbenzoic acid
-
2-(3H-pyrrol-5-yl)-1H-imidazo(4,5-b)pyridine
Co(II)-form of enzyme, 50% inhibition at 0.000078 mM
2-(5-methoxy-6-[2-methyl-3-((3-methylbut-2-en-1-yl)oxiran-2-yl]-4-oxobicyclo[3.1.0]hex-1-yl)methyl)-1H-isoindole-1,3(2H)-dione
no activity at 0.1 mM
2-(carboxymethoxy)-3-ethyl-6-[[(4-fluorophenyl)sulfonyl]amino]benzoic acid
-
2-({3-[3,5-bis[4-nitrobenzylidene]-4-oxopiperidin-1-yl]-3-oxopropylsulfanyl) ethanesulfonic acid
-
inhibitor of MetAP2
2-amino-4-(methylthio)-1-(1,3-thiazol-2-yl)butan-1-one
50% inhibition at 0.019 mM, formation of uncleavable tetrahedral intermediate upon binding
2-amino-4-(methylthio)-1-pyridin-2-ylbutan-1-one
50% inhibition at 0.016 mM, formation of uncleavable tetrahedral intermediate upon binding
2-hydroxy-1-naphthaldehyde isonicotinoyl hydrazone
-
inhibitor of HIV-1 replication and transcription, and potent and selective inhibitor of isoforms MetAP1a and MetAP1c. The inhibitor is active against replicating and aged non-growing Micobacterium tuberculosis at low micromolar concentrations
2-hydroxyethyl disulfide
inhibition is through covalent modifiction of residue C105
2-pyridin-2-yl-1H-benzimidazol-5-amine
Co(II)-form of enzyme, 50% inhibition at 0.0097 mM
2-pyridin-2-yl-1H-benzimidazole-5-carbonitrile
Co(II)-form of enzyme, 50% inhibition at 0.00043 mM
2-pyridin-2-yl-1H-imidazo(4,5-b)pyrazine
Co(II)-form of enzyme, 50% inhibition at 0.00024 mM
2-pyridin-2-yl-1H-imidazo(4,5-b)pyridine
Co(II)-form of enzyme, 50% inhibition at 0.00011 mM
2-pyridin-2-yl-1H-imidazo(4,5-c)pyridine
Co(II)-form of enzyme, 50% inhibition at 0.00055 mM
2-pyridin-2-yl-4-(trifluoromethyl)-6-[2-(trifluoromethyl)benzyl]-1,6-dihydropyrimidine
-
-
2-[(phenylsulfonyl)amino]-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
potent inhibitor but lacks cellular activity and is highly protein bound
2-[([4-[(E)-(5-amino-3-imino-3H-pyrazol-4-yl)diazenyl]phenyl]sulfinyl)oxy]hydrazinecarboximidamide
-
-
2-[2-(2-amino-4-methylsulfanyl-butyrylsulfanyl)-3-phenyl-propionylamino]-3-hydroxy-propionic acid
-
IC50 for Co-EcMetAP1: 0.0296 mM, IC50 for Mn-EcMetAPa: 0.0441 mM, IC50 for Zn-EcMetAP1: 0.0365 mM
2-[2-(2-Amino-4-methylsulfanyl-butyrylsulfanyl)-5-methyl-hexanoylamino]-3-hydroxy-propionic acid
-
IC50 for Co-EcMetAP1: 0.0286 mM, IC50 for Mn-EcMetAPa: 0.0443 mM, IC50 for Zn-EcMetAP1: 0.0498 mM, IC50 for Ni-EcMetAP1: 0.0357 mM
2-[2-(3-Amino-2-hydroxy-heptanoylamino)-propionylamino]-4-methyl-pentanoic acid methyl ester
-
IC50 for Co-EcMetAP1: 0.0229 mM, IC50 for Mn-EcMetAPa: 0.0252 mM, IC50 for Zn-EcMetAP1: 0.0167 mM, IC50 for Ni-EcMetAP1: 0.0125 mM
2-[4-(2-Cyano-2-ethoxycarbonyl-1-methyl-vinyl)-phenyl]-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carboxylic acid
-
IC50 for Co-EcMetAP1: 0.037 mM
2-[[(4-fluorophenyl)sulfonyl]amino]-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
-
2-[[(4-fluorophenyl)sulfonyl]amino]-8-methyl-5,6-dihydronaphthalene-1-carboxylic acid
-
3-(((2-(((1'-methyl-1,4'-bipiperidin-4-yl)methyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000055 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00037 mM
3-(((2-(((1-(1-methylethyl)piperidin-4-yl)methyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000046 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00095 mM
3-(((2-(((1-methylpiperidin-4-yl)methyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00013 mM
3-(((2-(((2-(diethylamino)ethyl)carbamoyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00037 mM
3-(((2-((1E)-3-((2-hydroxyethyl)(methyl)amino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000024 mM
3-(((2-((1E)-3-(4-methylpiperazin-1-yl)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000018 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000042 mM
3-(((2-((1E)-3-(diethylamino)but-1-en-1-yl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000016 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00007 mM
3-(((2-((1E)-3-(diethylamino)but-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000019 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00026 mM
3-(((2-((1E)-3-(diethylamino)prop-1-en-1-yl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000011 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000006 mM
3-(((2-((1E)-3-(diethylamino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000012 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000019 mM; 50% inhibition of enzyme at 0.000027 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00029 mM
3-(((2-((1E)-3-(dimethylamino)prop-1-en-1-yl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000019 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000036 mM
3-(((2-((1E)-3-(dimethylamino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000081 mM
3-(((2-((1E)-3-(ethyl(2-hydroxyethyl)amino)but-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000038 mM
3-(((2-((1E)-3-(ethyl(methyl)amino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000009 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000023 mM
3-(((2-((1E)-3-(methyl(1-methylethyl)amino)prop-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000012 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000027 mM
3-(((2-((1E)-4-(diethylamino)but-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000016 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000049 mM; 50% inhibition of enzyme at 0.000025 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00017 mM
3-(((2-((1E)-5-(diethylamino)pent-1-en-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000020 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00012 mM; 50% inhibition of enzyme at 0.000028 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000033 mM
3-(((2-((2-(1-(1-methylethyl)pyrrolidin-2-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000062 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00035 mM
3-(((2-((2-(1-(1-methylpiperidin-4-yl)pyrrolidin-2-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000070 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0005 mM
3-(((2-((2-(1-(cyclohexylmethyl)pyrrolidin-2-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0015 mM
3-(((2-((2-(1-piperidin-4-ylpyrrolidin-2-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000069 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0013 mM
3-(((2-((2-(1H-imidazol-1-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000010 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0029 mM
3-(((2-((2-(2-oxopyrrolidin-1-yl)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000040 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0014 mM
3-(((2-((2-(bis(1-methylethyl)amino)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000031 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00064 mM
3-(((2-((2-(diethylamino)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000031 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00054 mM
3-(((2-((2-(diethylamino)ethyl)carbamoyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000031 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00052 mM
3-(((2-((2-(dimethylamino)ethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000048 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0013 mM
3-(((2-((2-(dimethylamino)ethyl)sulfanyl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000030 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0007 mM
3-(((2-((2-pyridin-2-ylethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000053 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0020 mM
3-(((2-((2-pyridin-4-ylethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000016 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0085 mM
3-(((2-((2-pyrrolidin-1-ylethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000069 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0022 mM
3-(((2-((2-pyrrolidin-2-ylethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000022 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00014 mM
3-(((2-((3-((2-hydroxyethyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00028 mM
3-(((2-((3-((2-tert-butoxy-2-oxoethyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00011 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0043 mM
3-(((2-((3-((tert-butoxycarbonyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000077 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0049 mM
3-(((2-((3-(1,4'-bipiperidin-1'-yl)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000058 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0011 mM
3-(((2-((3-(1-methylpyrrolidin-2-yl)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000096 mM
3-(((2-((3-(4-methylpiperazin-1-yl)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000026 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00041 mM
3-(((2-((3-(bis(1-methylethyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000052 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00029 mM
3-(((2-((3-(bis(2-hydroxyethyl)amino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000026 mM, 50% inhibition of proliferation of HT-1080 cells at 0.001 mM
3-(((2-((3-(diethylamino)-1-methylpropyl)carbamoyl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000067 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00012 mM
3-(((2-((3-(diethylamino)-1-methylpropyl)carbamoyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0026 mM
3-(((2-((3-(diethylamino)propyl)amino)-4-methylphenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0021 mM
3-(((2-((3-(diethylamino)propyl)amino)-5-(trifluoromethyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00069 mM, 50% inhibition of proliferation of HT-1080 cells at 0.100 mM
3-(((2-((3-(diethylamino)propyl)amino)-5-methylphenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000066 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00066 mM
3-(((2-((3-(diethylamino)propyl)amino)-6-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000019 mM, 50% inhibition of proliferation of HT-1080 cells at 0.014 mM; 50% inhibition of enzyme at 0.00018 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0083 mM
3-(((2-((3-(diethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000025 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0014 mM
3-(((2-((3-(diethylamino)propyl)carbamoyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000025 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00055 mM
3-(((2-((3-(dimethylamino)-2,2-dimethylpropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000018 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00061 mM
3-(((2-((3-(dimethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000014 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00019 mM
3-(((2-((3-(ethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000012 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00011 mM
3-(((2-((3-aminopropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000013 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00016 mM
3-(((2-((3-morpholin-4-ylpropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000022 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00032 mM
3-(((2-((3-piperazin-1-ylpropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000020 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00051 mM
3-(((2-((3-pyrrolidin-1-ylpropyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000085 mM
3-(((2-((4-(diethylamino)-1-methylbutyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00013 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00021 mM
3-(((2-((4-(dimethylamino)butyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000012 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00046 mM
3-(((2-((piperidin-3-ylmethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000035 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00029 mM
3-(((2-((piperidin-4-ylmethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00046 mM
3-(((2-((pyridin-4-ylmethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000035 mM, 50% inhibition of proliferation of HT-1080 cells at 0.017 mM
3-(((2-((pyrrolidin-3-ylmethyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000034 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00038 mM
3-(((2-(3,3,4,5,5-pentamethylpiperazin-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000091 mM, 50% inhibition of proliferation of HT-1080 cells at 0.015 mM
3-(((2-(3-(diethylamino)propoxy)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000018 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0062 mM
3-(((2-(3-(diethylamino)propyl)-4-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000017 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000024 mM
3-(((2-(3-(diethylamino)propyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000009 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000073 mM
3-(((2-(3-(dimethylamino)propyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000010 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000035 mM
3-(((2-(4-(diethylamino)butyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000019 mM, 50% inhibition of proliferation of HT-1080 cells at 0.000068 mM
3-(((2-(4-benzylpiperazin-1-yl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000020 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0016 mM
3-(((2-(5-(diethylamino)pentyl)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000045 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00035mM
3-(((2-aminophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000013 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0062 mM
3-(((3-chloro-2-((3-(diethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000015 mM, 50% inhibition of proliferation of HT-1080 cells at 0.00037 mM
3-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-N,N,N-trimethylpropan-1-aminium iodide
-
-
3-(((4-chloro-2-((3-(diethylamino)propyl)amino)-5-fluorophenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00079 mM, 50% inhibition of proliferation of HT-1080 cells at 0.013 mM
3-(((4-chloro-2-((3-(diethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.00011 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0031 mM
3-(((5-chloro-2-((3-(diethylamino)propyl)amino)phenyl)sulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000056 mM, 50% inhibition of proliferation of HT-1080 cells at 0.010 mM
3-((4-methylpent-3-enoyl)amino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0149 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.00068 mM
3-((5-methylhex-4-enoyl)amino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0074 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0010 mM
3-((cyclopent-1-en-1-ylcarbonyl)amino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition above 100 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition above 100 mM
3-((phenylsulfonyl)amino)-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
50% inhibition of enzyme at 0.000010 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0024 mM
3-((R)-2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)-3-methylbutanamido)benzoic acid
-
-
3-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-{[(2-nitrophenyl)methyl]sulfanyl}-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-fluorobenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-methylbenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-nitrobenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(3-methoxybenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(4-fluorobenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(4-nitrobenzylthio)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,4-difluorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2,6-difluorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(2-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(3-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(3-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(4-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(4-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(benzoylamino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition above 100 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0074 mM
3-(benzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
-
-
3-(hexanoylamino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0867 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0020 mM
3-(pent-4-enoylamino)-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition above 0.1 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.00079 mM
3-amino-1-(cyclopropylamino)heptan-2 -one
50% inhibition at 0.007 mM, formation of uncleavable tetrahedral intermediate upon binding
3-But-3-enoylamino-pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50 for Co-EcMetAP1: 0.0001 mM, IC50 for Mn-EcMetAPa: 0.0233 mM, IC50 for Zn-EcMetAP1: 0.0224 mM, IC50 for Ni-EcMetAP1: 0.00076 mM
3-ethyl-2-methoxy-6-[[(2-[[2-(1-methylpyrrolidin-2-yl)ethyl]amino]phenyl)sulfonyl]amino]benzoic acid
-
3-ethyl-2-methoxy-6-[[(2-[[3-(2-methylpiperidin-1-yl)propyl]amino]phenyl)sulfonyl]amino]benzoic acid
-
3-hydroxy-N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0081 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0035 mM
3-[(phenylsulfonyl)amino]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
-
4-((((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)methyl)benzoic acid
-
-
4-(((3-((2-methoxyphenoxy)methyl)-1H-1,2,4-triazol-5-yl)sulfanyl)acetyl)-1,5-dimethyl-2-phenyl-1,2-dihydro-3H-pyrazol-3-one
-
Co(II)-form of enzyme, 50% inhibition at 0.00099 mM
4-(1-benzyl-1H-1,2,3-triazol-4-yl)benzene-1,2-diol
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
4-(1-methyl-1H-imidazol-2-yl)benzene-1,2-diol
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
4-(2-aminothiazol-4-yl)benzene-1,2-diol
specific inhibition of Fe2+-loaded MetAP
4-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)morpholine
-
-
4-(5-fluoropyrimidin-2-yl)benzene-1,2-diol
-
does only inhibit Fe2+- or Co2+-activated MetAP enzymes, but not Mn2+-activated MetAP enzyme
4-(5-methoxy-1,3-oxazol-2-yl)benzene-1,2-diol
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
4-methyl-2-(1H-1,2,3-triazol-5-yl)pyridine
-
Co(II)-form, Ki,app-value 8 nM, Mn(II)-form, 0.014 mM, 50% reduction of viability of human umbilical vein endothelial cell above 0.03 mM
4-pyridin-2-ylbenzene-1,2-diol
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
4-pyrimidin-2-ylbenzene-1,2-diol
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
4-[4-(4-methoxyphenyl)piperazin-1-yl]-2-(pyridin-2-yl)quinazoline
EC50 value in presence of Co(II) is 0.0001 mM, superior inhibitory potency and selectivity for isoform MetAP1
5,5'-dithiobis(2-nitrobenzoic acid)
inhibition is through covalent modifiction of residue C105
5,6-dimethyl-2-pyridin-2-yl-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00243 mM
5-((R)-1-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl-pyrrolidin-2-ylmethoxy)-isoquinoline
-
5-(1-benzofuran-2-yl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 15 nM, Mn(II)-form, 26% inhibition at 0.02 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.006 mM
5-(2-(trifluoromethyl)phenyl)-2-furoic acid
-
Co(II)-form of enzyme, 50% inhibition at 0.073 mM, Mn(II)-form, 50% inhibition at 0.000063 mM, Ni-(II)form, 50% inhibition above 200 mM, Fe-(II)form, 50% inhibition at 0.195 mM
5-(2-chloro-3-methylphenyl)-2-furoic acid
-
Co(II)-form of enzyme, 50% inhibition at 0.069 mM, Mn(II)-form, 50% inhibition at 0.00096 mM, Ni-(II)form, 50% inhibition above 200 mM, Fe-(II)form, 50% inhibition above 200 mM
5-(2-chlorophenyl)-2-furoic acid
-
Co(II)-form of enzyme, 50% inhibition at 0.154 mM, Mn(II)-form, 50% inhibition at 0.0024 mM, Ni-(II)form, 50% inhibition above 200 mM, Fe-(II)form, 50% inhibition at 0.186 mM
5-(2-fluorophenyl)-2-furoic acid
-
Co(II)-form of enzyme, 50% inhibition at 0.198 mM, Mn(II)-form, 50% inhibition at 0.014 mM, Ni-(II)form, 50% inhibition above 200 mM, Fe-(II)form, 50% inhibition above 200 mM
5-(3,4-dibromophenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 1 nM, Mn(II)-form, 0.016 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.002 mM
5-(3,4-dihydroxyphenyl)-2-methyl-N-(propan-2-yl)-1,3-thiazole-4-carboxamide
-
-
5-(3,4-dihydroxyphenyl)-N-isopropyl-2-methylthiazole-4-carboxamide
specific inhibition of Fe2+-loaded MetAP
5-(3-chlorophenyl)-2-furoic acid
-
Co(II)-form of enzyme, 50% inhibition at 0.193 mM, Mn(II)-form, 50% inhibition at 0.019 mM, Ni-(II)form, 50% inhibition above 200 mM, Fe-(II)form, 50% inhibition above 200 mM
5-(4-bromophenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 3 nM, Mn(II)-form, 0.011 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.006 mM
5-(4-chlorophenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 6 nM, Mn(II)-form, 0.011 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.005 mM
5-(4-iodophenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 1 nM, Mn(II)-form, not inhibitory at 0.02 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.02 mM
5-(4-methylphenyl)-1H-1,2,3-triazole
-
Co(II)-form, Ki,app-value 15 nM, Mn(II)-form, 4400 nM, 50% reduction of viability of human umbilical vein endothelial cell at 0.03 mM
5-(hydroxymethyl)-1-methoxy-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]bicyclo[3.1.0]hexan-2-ol
no activity at 0.1 mM
5-chloro-2-(5-chloropyridin-2-yl)-6-methyl-N-((R)-2-phenyl-2-(4-phenylbutylamino)ethyl)pyrimidin-4-amine
compound shows 500fold specificity for isoform AP1 over isoform AP2
5-chloro-2-(5-chloropyridin-2-yl)-N-(2,4-diphenylbutyl)-6-methylpyrimidin-4-amine
compound shows 3175fold specificity for isoform AP1 over isoform AP2
5-chloro-2-pyridin-2-yl-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00169 mM
5-chloro-4-methyl-2-pyridin-2-yl-6-pyrrolidin-1-yl-1,6-dihydropyrimidine
-
-
5-chloro-4-methyl-6-(4-methylbenzyl)-2-pyridin-2-yl-1,6-dihydropyrimidine
-
-
5-chloro-6-(2-ethylphenyl)-4-methyl-2-pyridin-2-yl-1,6-dihydropyrimidine
-
highly selective inhibitor
5-chloro-6-methyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
-
5-chloro-N,6-dimethyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
-
5-fluoro-2-pyridin-2-yl-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00151 mM
5-methoxy-6-[(4-methoxyphenyl)sulfanyl]-2-pyridin-2-yl-1,6-dihydropyrimidine
-
-
5-methoxy-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-4-oxobicyclo[3.1.0]hexane-1-carbaldehyde
-
5-methyl-2-((phenylsulfonyl)amino)benzoic acid
50% inhibition of enzyme at 0.0014 mM, 50% inhibition of proliferation of HT-1080 cells at 0.0072 mM
5-methyl-2-(1H-1,2,3-triazol-5-yl)pyridine
-
Co(II)-form, Ki,app-value 3 nM, Mn(II)-form, 0.015 mM, 50% reduction of viability of human umbilical vein endothelial cell at 0.002 mM
5-methyl-2-pyridin-2-yl-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00209 mM
5-nitro-2-pyridin-2-yl-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00016 mM
5-tert-butyl-2-pyridin-2-yl-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00260 mM
5-[(2E)-hepta-2,6-dien-4-yn-1-ylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
-
5-[(3-methylbut-2-en-1-yl)sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[(cyclohexylmethyl)sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[(cyclohexylmethyl)sulfanyl]-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[(cyclohexylmethyl)sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[(cyclohexylmethyl)sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[(2-methyl-2,5-dihydro-1,3-thiazol-4-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[(4-chlorophenyl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
most potent compound in the host-cell viability assay
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
-
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
-
6-(1,5-dimethylhex-4-en-1-yl)-5-(hydroxymethyl)-1-methoxybicyclo[3.1.0]hexan-2-one
-
6-(1H-benzimidazol-2-ylamino)pyridin-2-ol
Co(II)-form of enzyme, 50% inhibition at 0.00134 mM
6-(2-chlorobenzyl)-2-pyridin-2-yl-4-(trifluoromethyl)-1,6-dihydropyrimidine
-
-
6-(benzylsulfanyl)-5-chloro-4-methyl-2-pyridin-2-yl-1,6-dihydropyrimidine
-
-
6-(phenylsulfanyl)-2-pyridin-2-yl-4-(trifluoromethyl)-1,6-dihydropyrimidine
-
-
6-[(1E)-1,5-dimethylhexa-1,4-dien-1-yl]-5-(hydroxymethyl)-1-methoxybicyclo[3.1.0]hexan-2-one
-
6-[(2,4-dichlorophenyl)sulfanyl]-5-methoxy-2-pyridin-2-yl-1,6-dihydropyrimidine
-
-
6-[(4-methoxyphenyl)sulfanyl]-2-pyridin-2-yl-4-(trifluoromethyl)-1,6-dihydropyrimidine
-
-
6-[([2-[(1E)-3-(diethylamino)prop-1-en-1-yl]-4-fluorophenyl]sulfonyl)amino]-3-ethyl-2-methoxybenzoic acid
-
6-[[(2-bromo-4-fluorophenyl)sulfonyl]amino]-2-(1H-imidazol-4-yl)-3-methoxybenzoic acid
-
6-[[(2-bromo-4-fluorophenyl)sulfonyl]amino]-2-furan-2-yl-3-methoxybenzoic acid
-
6-[[(2-bromo-4-fluorophenyl)sulfonyl]amino]-2-furan-3-yl-3-methoxybenzoic acid
-
6-[[(2-[(1E)-3-(diethylamino)prop-1-en-1-yl]-4-fluorophenyl]sulfonyl)amino]-3-furan-3-yl-2-methoxybenzoic acid
-
6-[[(2-[[3-(dimethylamino)propyl]amino]-4-fluorophenyl)sulfonyl]amino]-3-furan-3-yl-2-methoxybenzoic acid
-
6-[[(2-[[4-(dimethylamino)butyl]amino]phenyl)sulfonyl]amino]-3-ethyl-2-methoxybenzoic acid
-
6-[[(4-fluorophenyl)sulfonyl]amino]-2-(1-hydroxyethyl)-3-methylbenzoic acid
-
6-[[(4-fluorophenyl)sulfonyl]amino]-2-(hydroxymethyl)-3-methylbenzoic acid
-
6-[[(4-fluorophenyl)sulfonyl]amino]-2-methoxy-3-(1H-pyrazol-4-yl)benzoic acid
-
8-pyridin-2-yl-7H-purine
Co(II)-form of enzyme, 50% inhibition at 0.00038 mM
A-310840
-
IC50: 0.000031 mM for enzyme with Zn2+, 0.000043 mM for enzyme with Ni2+, 0.000069 mM for enzyme with Co2+, 0.000026 for enzyme with Fe2+, 0.0578 mM for enzyme with Mn2+
A-311263
-
IC50: 0.000121 mM for enzyme with Zn2+, 0.000107 mM for enzyme with Ni2+, 0.000149 mM for enzyme with Co2+, 0.00011 mM for enzyme with Fe2+, 0.000055 mM for enzyme with Mn2+
bengamide B
nonselective inhibitor for both MetAP1 and MetAP2; nonselective inhibitor for both MetAP1 and MetAP2
bengamide G
nonselective inhibitor for both MetAP1 and MetAP2; nonselective inhibitor for both MetAP1 and MetAP2
bengamide L
nonselective inhibitor for both MetAP1 and MetAP2; nonselective inhibitor for both MetAP1 and MetAP2
bengamide M
nonselective inhibitor for both MetAP1 and MetAP2; nonselective inhibitor for both MetAP1 and MetAP2
bengamide N
nonselective inhibitor for both MetAP1 and MetAP2; nonselective inhibitor for both MetAP1 and MetAP2
bengamide O
nonselective inhibitor for both MetAP1 and MetAP2; nonselective inhibitor for both MetAP1 and MetAP2
cyclopropyl 5-(3,4-dihydroxyphenyl)-2-methyl-1,3-thiazole-4-carboxylate
-
DTNB
-
the enzyme is fully reactivated when incubated with tris(2-carboxyethyl)-phosphine hydrochloride
ethyl (6E)-8-[(2R,3R)-3-[(1S,5S)-5-(hydroxymethyl)-1-methoxy-2-oxobicyclo[3.1.0]hex-6-yl]-3-methyloxiran-2-yl]oct-6-enoate
no activity at 0.1 mM
ethyl 5-(3,4-dihydroxyphenyl)-1,3-oxazole-4-carboxylate
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
fumagillol
-
i.e. (3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-ol
isobutyl (2-((1,3-thiazol-2-ylamino)carbonyl)pyridin-3-yl)carbamate
-
wild-type, 50% inhibition above 100 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition above 100 mM
LAF 389
nonselective inhibitor for both MetAP1 and MetAP2; nonselective inhibitor for both MetAP1 and MetAP2
MCB2379
-
IC50: 599 nM in presence of Co2+, 1455 nM in presence of Zn2+
MCB2813
-
IC50: 43.7 nM in presence of Co2+, 300 nM in presence of Zn2+
methionine
feedback inhibition. 70% inhibition at 0.1 mM
methyl 4-([5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
-
methyl 4-([5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
-
methyl 4-([5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
-
methyl 4-([5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
-
methyl 4-[(5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl 4-[(5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
-
methyl N-[(2S,3R)-3-amino-2-hydroxy-3-(4-methylphenyl)propanoyl]-L-alanylleucinate
-
-
methyl N-[(2S,3R)-3-amino-2-hydroxy-3-[4-(1-methylethyl)phenyl]propanoyl]-L-alanylleucinate
-
-
methyl [[(2S)-2-([(2S,3R)-3-amino-2-hydroxy-3-[4-(trifluoromethyl)phenyl]propanoyl]amino)propanoyl]amino]acetate
-
-
N-((R)-2-(5-chloro-2-(5-chloropyridin-2-yl)-6-methylpyrimidin-4-ylamino)-1-phenylethyl)-3-phenylpropanamide
compound shows 323fold specificity for isoform AP1 over isoform AP2
N-(1,3-thiazol-2-yl)-3-[(N-[2-[2-(2-[2-[(1H-triaziren-1-ylacetyl)amino]ethoxy]ethoxy)ethoxy]-4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzoyl]glycyl)amino]pyridine-2-carboxamide
-
-
N-(2-aminoethyl)-N'-[5-chloro-6-methyl-2-pyridin-2-yl-4-[5-(trifluoromethyl)pyridin-2-yl]-3,4-dihydropyrimidin-4-yl]ethane-1,2-diamine
-
-
N-(2-aminoethyl)-N'-[5-chloro-6-methyl-2-pyridin-3-yl-4-[5-(trifluoromethyl)pyridin-2-yl]-3,4-dihydropyrimidin-4-yl]ethane-1,2-diamine
-
-
N-(2-aminoethyl)-N'-[5-chloro-6-methyl-2-pyridin-4-yl-4-[5-(trifluoromethyl)pyridin-2-yl]-3,4-dihydropyrimidin-4-yl]ethane-1,2-diamine
-
-
N-(2-methylphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(2-methylphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(2-methylphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(3,4-dimethoxyphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[(2,2-dimethylpropanoyl)amino]pyridine-2-carboxamide
-
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[(3-phenylpropanoyl)amino]pyridine-2-carboxamide
-
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[[(1E)-2-methylpropylidene]amino]pyridine-2-carboxamide
-
N-(4-chlorophenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfany]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-chlorophenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methoxyphenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[(thiophen-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(4-methylphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-(5-chloroquinolin-8-yl)benzenesulfonamide
Co(II)-form of enzyme, 50% inhibition at 0.00169 mM, Mn(II)-form, 50% inhibition at 0.0185 mM, Fe(II)-form, at 0.0138 mM, Ni(II)-form, at 0.00742 mM, Zn(II)-form, at 0.0113 mM
N-(5-chloroquinolin-8-yl)methanesulfonamide
Co(II)-form of enzyme, 50% inhibition at 0.000154 mM, Mn(II)-form, 50% inhibition at 0.00164 mM, Fe(II)-form, at 0.00393 mM, Ni(II)-form, at 0.000171 mM, Zn(II)-form, at 0.000806 mM; inhibits the Co(II)- and Ni(II)-forms of MetAP potently
N-(5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)pyridin-3-amine
-
N-(5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)pyridin-3-amine
-
N-1,3-thiazol-2-yl-1H-benzimidazol-2-amine
Co(II)-form of enzyme, 50% inhibition at 0.00054 mM
N-1,3-thiazol-2-yl-3-(N-[(2-2-[(1H-triaziren-1-ylacetyl)amino]ethoxy]-4-[[3-(trifluoromethyl)-[3H-diaziren-3-yl]phenyl)carbonyl]glycyl]amino)pyridine-2-carboxamide
-
-
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
N-biphenyl-2-yl-5-[(3,4-difluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-biphenyl-2-yl-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-biphenyl-2-yl-5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-biphenyl-2-yl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-biphenyl-2-yl-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-but-3-en-1-yl-5-(3,4-dihydroxyphenyl)-1,3-oxazole-4-carboxamide
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
N-cyclopentyl-5-(3,4-dihydroxyphenyl)-1,3-oxazole-4-carboxamide
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
N-cyclopentyl-N-(thiazol-2-yl)oxalamide
potent and selective inhibitor
N-cyclopropyl-5-(3,4-dihydroxyphenyl)-2-methyl-1,3-thiazole-4-carboxamide
-
-
N-cyclopropyl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
N-ethylmaleimide
1 mM, 90% inhibition. Inhibition is through covalent modifiction of residue C105
N-isobutyl-N'-1,3-thiazol-2-ylethanediamide
-
Co(II)-form of enzyme, 50% inhibition at 0.00028 mM, Mn(II)-form, 50% inhibition at 0.108 mM, Ni-(II)form, 50% inhibition at 0.0034 mM, Fe-(II)form, 50% inhibition at 0.118 mM
N-pyrazin-2-yl-1H-benzimidazol-2-amine
Co(II)-form of enzyme, 50% inhibition at 0.0046 mM
N-pyridin-2-yl-1H-benzimidazol-2-amine
Co(II)-form of enzyme, 50% inhibition at 0.00057 mM
N-quinolin-8-ylmethanesulfonamide
Co(II)-form of enzyme, 50% inhibition at 0.000137 mM, Mn(II)-form, 50% inhibition at 0.00214 mM, Fe(II)-form, at 0.00374 mM, Ni(II)-form, at 0.000184 mM, Zn(II)-form, at 0.00111 mM
N-[4-(chloromethyl)phenyl]-5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
-
N-[5-[(3,4-difluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
-
N-[5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
-
N-[5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
-
N-[5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
-
phenyl(2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-yl)methanone
Co(II)-form of enzyme, 50% inhibition at 0.00240 mM
phenyl(2-pyridin-2-yl-1H-benzimidazol-5-yl)methanone
Co(II)-form of enzyme, 50% inhibition at 0.00040 mM
tert-butyl [2-(4,5-dihydro-1,3-thiazol-2-ylcarbamoyl)pyridin-3-yl]carbamate
-
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methyl-but-2-enyl)-oxiranyl]-1-oxa-spiro [2.5] oct-6-yl ester
-
PPI-2458, potent irreversible inhibitor
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methyl-but-2-enyl)-oxiranyl]-1-oxa-spiro[2.5]oct-6-yl ester
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiranyl]-1-oxaspiro(2,5)oct-6-yl ester
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
-
A-311263, the inhibitor has little or no preference for the type of divalent metal ion that occupies the active site of MetAP
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
-
A-311263, the inhibitor has little or no preference for the type of divalent metal ion that occupies the active site of MetAP
(3R)-amino-(2S)-hydroxyheptanoyl-Ala-Leu methyl ester
-
IC50: 0.095 mM
1-(1H-benzimidazol-2-yl)thiourea
Co(II)-form of enzyme, 50% inhibition at 0.0089 mM
1-benzyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00046 mM
1-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00050 mM
2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-amine
Co(II)-form of enzyme, 50% inhibition at 0.00339 mM
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
-
A-310840, the inhibitor binds to the Co2+-loaded enzyme well but is approximately 23fold less potent for Mn2+-loaded MetAP
3-(2,2,2-trifluoroacetylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.000034 mM
3-(2,2,2-trifluoroacetylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00492
3-(2,2-dimethylpropionylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00034 mM; IC50: 0.00054 mM
3-(2,2-dimethylpropionylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
-
3-(2,2-dimethylpropionyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00068 mM
3-(2,2-dimethylpropionyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00078 mM
3-(2-acetyloxybenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0016 mM
3-(2-acetyloxybenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
0.015 mM
3-(2-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00028 mM
3-(2-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50 above 0.1 mM
3-(2-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00083 mM
3-(2-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.016 mM
3-(2-iodobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0013 mM
3-(2-iodobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00089 mM
3-(2-methoxybenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0017 mM
3-(2-methoxybenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00055 mM
3-(2-methylbut-2-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00028 mM
3-(2-methylbut-2-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0109 mM
3-(2-methylbut-2-enoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0044 mM
3-(2-methylbut-2-enoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00039 mM
3-(2-nitrobenzoyloxy)pyridine-2-carboxylic acid thiatol-2-ylamide
-
IC50: 0.0021 mM; IC50 above 0.1 mM
3-(2-nitrobenzoyloxy)pyridine-2-carboxylic acid thiatol-2-ylamide
-
-
3-(3-bromo-4-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0025 mM
3-(3-bromo-4-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0034 mM
3-(3-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00071 mM
3-(3-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50 above 0.1 mM
3-(3-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.000095 mM
3-(3-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50 above 0.1 mM
3-(3-methoxy-2-nitrobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0017 mM
3-(3-methoxy-2-nitrobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00302 mM
3-(3-methylbut-2-enoylamino)pyridien-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00022 mM
3-(3-methylbut-2-enoylamino)pyridien-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00077 mM
3-(3-methylbut-2-enoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0026 mM
3-(3-methylbut-2-enoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00049 mM
3-(3-methylbut-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00015 mM
3-(3-methylbut-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00467
3-(3-nitrobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0006 mM
3-(3-nitrobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50 above 0.1 mM
3-(4-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00136 mM
3-(4-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50 above 0.1 mM
3-(4-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0011 mM
3-(4-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.062 mM
3-(4-methylpent-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00024 mM
3-(4-methylpent-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00014 mM
3-(5-methylhex-4-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.000671 mM
3-(5-methylhex-4-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00031 mM
3-(but-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00013 mM
3-(but-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00038 mM
3-(cyclohexanecarbonylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00087 mM
3-(cyclohexanecarbonylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50 above 0.1 mM
3-(cyclohexanecarbonyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00239 mM
3-(cyclohexanecarbonyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00032 mM
3-aminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 1.7 mM, IC50: 0.0328 mM
3-benzoylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00089 mM
3-benzoylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC5ß0 above 0.1 mM
3-benzoyloxypyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00103 mM
3-formylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00033 mM
3-formylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00032
3-hexanoylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.000038 mM
3-hexanoylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00062 mM
3-hexanoyloxypyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00102 mM
3-hexanoyloxypyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.000174 mM
3-hydroxypyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00486 mM
3-iso-butoxycarbonylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00192 mM
3-iso-butoxycarbonylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0537
3-phenylacetylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00004 mM
3-phenylacetylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00082 mM
3-phenylacetyloxypyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.000054 mM
3-phenylacetyloxypyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0002 mM
3-propionylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00026 mM
3-propionylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00035 mM
3-propionyloxypyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0054 mM
3-propionyloxypyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00038 mM
3-tert-butoxycarbonylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00018 mM
3-tert-butoxycarbonylaminopyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.00335 mM
3-[3-(2-methoxyphenyl)acryloyloxy]pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0021 mM
3-[3-(2-methoxyphenyl)acryloyloxy]pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50: 0.0099 mM
4-(1,3-thiazol-2-yl)benzene-1,2-diol
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
4-(2,5-dimethylthiophen-3-yl)benzene-1,2-diol
specific inhibition of Fe2+-loaded MetAP
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
4-(3-methylthiophen-2-yl)benzene-1,2-diol
-
does only inhibit Fe2+-activated MetAP enzyme, but not Mn2+- or Co2+-activated MetAP enzymes
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
potent and selective inhibitor
5-chloro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00515 mM
5-fluoro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00431 mM
5-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00716 mM
5-nitro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00122 mM
5-tert-butyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Co(II)-form of enzyme, 50% inhibition at 0.00391 mM
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
-
5-[2-(trifluoromethyl)phenyl]furan-2-carboxylic acid
potent and selective inhibitor
actinonin
0.01 mM, 40% loss of activity; 0.01 mM, 70% loss of activity
bengamide A
nonselective inhibitor for both MetAP1 and MetAP2; nonselective inhibitor for both MetAP1 and MetAP2
bengamide A
nonspecific, reversible inhibitor of MetAP-1 and MetAP-2; nonspecific, reversible inhibitor of MetAP-1 and MetAP-2
bestatin
0.01 mM, 25% loss of activity; 0.01 mM, 50% loss of activity
Co2+
-
in excess, a third Co2+ ion binds to the active site regions and results in inhibition
EDTA
-
33.7% relative activity at 100 mM, the enzyme activity inhibited by 1 mM EDTA is restored in presence of 5 mM Mg2+
EDTA
1 mM, about 10% residual activity. The aminopeptidase activity of the EDTA-inactivated enzyme is successfully restored by Mn2+
fumagillin
binding structure, overview. Fumagillin and its analogues show inhibitory activity in vitro and in animal models of microsporidiosis and human infections due to Enterocytozoon bieneusi
fumagillin
-
fumagillin covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase
fumagillin
a covalent bond is formed between a reactive epoxide of fumagillin and histidine-231 in the active site of Met-AP2. Fumagillin-based drugs inhibit MetAP-2 but not MetAP-1
fumagillin
higher affinity to MetAP2 than to MetAP1; lower affinity to MetAP1 than to MetAP2
fumagillin
-
binding structure, specificity determinants lie in the S1 hydrophobic methionine binding subsite, overview
N-(pyridin-2-ylmethyl)-N'-1,3-thiazol-2-ylethanediamide
-
Co(II)-form of enzyme, 50% inhibition at 0.000073 mM, Mn(II)-form, 50% inhibition at 0.043 mM, Ni-(II)form, 50% inhibition at 0.002 mM, Fe-(II)form, 50% inhibition at 0.065 mM
N-(quinolin-8-yl)methanesulfonamide
inhibits the Co(II)- and Ni(II)-forms of MetAP potently
N-(quinolin-8-yl)methanesulfonamide
-
a trimetalated enzyme, forms a complex with the enzyme, cuases bacterial growth inhibition of strains AS19, D22 and SM101 by targeting MetAP by recruitment of a third auxiliary metal, binding structure, overview
N-1,3-thiazol-2-ylpyridine-2-carboxamide
Co(II)-form of enzyme, 50% inhibition at 0.000063 mM, binds to an additional Co2+ ion at the entrance of the active site
N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
wild-type, 50% inhibition at 0.0104 mM, mutant lacking N-terminal 66 amino acids, 50% inhibition at 0.0049 mM
N-1,3-thiazol-2-ylpyridine-2-carboxamide
-
Co(II)-form of enzyme, 50% inhibition at 0.0071 mM
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
-
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
-
-
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
-
-
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
-
-
N-cyclopentyl-N'-1,3-thiazol-2-ylethanediamide
-
Co(II)-form of enzyme, 50% inhibition at 0.000067 mM, Mn(II)-form, 50% inhibition at 0.053 mM, Ni-(II)form, 50% inhibition at 0.001 mM, Fe-(II)form, 50% inhibition at 0.046 mM
N-cyclopropyl-2-(3,4-dihydroxyphenyl)thiophene-3-carboxamide
specific inhibition of Fe2+-loaded MetAP
ovalicin
-
covalently modifies a conserved active-site histidine in the Escherichia coli methionine aminopeptidase
ovalicin
higher affinity to MetAP2 than to MetAP1; lower affinity to MetAP1 than to MetAP2
Pyridine-2-carboxylic acid thiazol-2-ylamide
-
IC50 for Co-EcMetAP1: 0.0013 mM
thiabendazole
Co(II)-form of enzyme, 50% inhibition at 0.00047 mM, binds to an additional Co2+ ion at the entrance of the active site
TNP-470
is likely to inhibit the enzyme by occupying the active site in the same fashion as fumagillin
TNP-470
-
binding structure, specificity determinants lie in the S1 hydrophobic methionine binding subsite, overview
TNP-470
treatment inhibits programmed cell death in miltefosine-treated promastigotes. It inhibits the biochemical features of metazoan apoptosis, including caspase3/7 protease like activity, oligonucleosomal DNA fragmentation, collapse of mitochondrial transmembrane potential, and increase in cytosolic pool of calcium ions but does not prevent the cell death and phosphatidyl serine externalization
TNP-470
-
a fumagillin derivative, targets MetAP2, no binding to MetAP1 isozymes
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methyl-but-2-enyl)-oxiranyl]-1-oxa-spiro[2.5]oct-6-yl ester
PPI-2458
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methyl-but-2-enyl)-oxiranyl]-1-oxa-spiro[2.5]oct-6-yl ester
PPI-2458, 5 mg/kg
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiranyl]-1-oxaspiro(2,5)oct-6-yl ester
-
PPI-2458, potent inhibitor
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiranyl]-1-oxaspiro(2,5)oct-6-yl ester
-
PPI-2458, potent inhibitor
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiranyl]-1-oxaspiro(2,5)oct-6-yl ester
-
PPI-2458, potent inhibitor
[amino(cyclohexyl)methyl]phosphonic acid
compound selectively inhibits the Streptococcus pneumoniae MetAP in low micromolar range but not the human enzyme. Residue F309 in the human enzyme and M205 in the Streptococcus pneumoniae MetAP at the analogous position render them with different susceptibilities against the inhibitor
[amino(cyclohexyl)methyl]phosphonic acid
compound selectively inhibits the Streptococcus pneumoniae MetAP in low micromolar range but not the human enzyme. Residue F309 in the human enzyme and M205 in the Streptococcus pneumoniae MetAP at the analogous position render them with different susceptibilities against the inhibitor
additional information
one of the protomeric states of the enzyme is relevant for inhibitor binding, whereas the other is relevant for substrate hydrolysis
-
additional information
thiabendazole and its derivatives are potent inhibitors in vitro, but fail to inhibit in vivo because they bind as Co2+-complexes to H79, thus blocking the active site of enzyme. In the in vitro assay the metal ion concentration is considerably higher than under in vivo conditions
-
additional information
-
thiabendazole and its derivatives are potent inhibitors in vitro, but fail to inhibit in vivo because they bind as Co2+-complexes to H79, thus blocking the active site of enzyme. In the in vitro assay the metal ion concentration is considerably higher than under in vivo conditions
-
additional information
-
inhibitor synthesis, pharmacokinetics, and molecular modelling
-
additional information
identification of inhibitors for human methionine aminopeptidases MetAP1 and MetAP2. 5-chloro-6-methyl-2-pyridin-2-ylpyrimidine is the minimum element for the inhibition of MetAP1, 5'-chloro is the favored substituent on the pyridine ring for the enhanced potency against MetAP1, and long C4 side chains are the essentials for higher Met AP1-selectivity
-
additional information
-
identification of inhibitors for human methionine aminopeptidases MetAP1 and MetAP2. 5-chloro-6-methyl-2-pyridin-2-ylpyrimidine is the minimum element for the inhibition of MetAP1, 5'-chloro is the favored substituent on the pyridine ring for the enhanced potency against MetAP1, and long C4 side chains are the essentials for higher Met AP1-selectivity
-
additional information
-
a set of inhibitors displayed completely different inhibitory profiles on the two mycobacterial MetAPs in both potency and metalloform selectivity
-
additional information
identification of inhibitors with high selectivity toward the Fe(II)-form, the Mn(II)-form, or the Co(II) and Ni(II) forms of the enzyme, respectively, overview. Binding structure of inhibitors in the active site of isozyme MetAP1c, overview
-
additional information
-
identification of inhibitors with high selectivity toward the Fe(II)-form, the Mn(II)-form, or the Co(II) and Ni(II) forms of the enzyme, respectively, overview. Binding structure of inhibitors in the active site of isozyme MetAP1c, overview
-
additional information
-
identification of pyridinyl-pyrimidine inhibitors with selectivity to isozyme MetAP1b before MetAP1a and MetAP1c
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0143
L-methionine 4-methylcoumaryl-7-amide
pH 7.5, temperature not specified in the publication
0.125
L-alanine-4-methylcoumarin-7-amide
presence of Ca2+, pH 8.0, 37°C
0.154
L-alanine-4-methylcoumarin-7-amide
presence of Co2+, pH 8.0, 37°C
0.167
L-alanine-4-methylcoumarin-7-amide
presence of Mn2+, pH 8.0, 37°C
0.172
L-alanine-4-methylcoumarin-7-amide
presence of Cu2+, pH 8.0, 37°C
0.179
L-alanine-4-methylcoumarin-7-amide
presence of Mg2+, pH 8.0, 37°C
0.284
L-alanine-4-methylcoumarin-7-amide
presence of Ni2+, pH 8.0, 37°C
0.154
L-Met 4-nitroanilide
presence of Ni2+, pH 8.0, 22°C
0.193
L-Met 4-nitroanilide
presence of Co2+, pH 8.0, 22°C
0.466
L-Met 4-nitroanilide
presence of Ni2+, pH 8.0, 22°C
0.52
L-Met 4-nitroanilide
presence of Co2+, pH 8.0, 22°C
0.6
L-Met-Gly-L-Met-L-Met
mutant enzyme D97N, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5
1.1
L-Met-Gly-L-Met-L-Met
mutant enzyme D97A, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5
1.3
L-Met-Gly-L-Met-L-Met
-
wild type enzyme, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Mn2+
1.5
L-Met-Gly-L-Met-L-Met
-
mutant enzyme H79A, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+
1.8
L-Met-Gly-L-Met-L-Met
mutant enzyme D97E, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5
1.8
L-Met-Gly-L-Met-L-Met
-
mutant enzyme H79A, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+
3
L-Met-Gly-L-Met-L-Met
wild type enzyme, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5
3
L-Met-Gly-L-Met-L-Met
-
wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
3.1
L-Met-Gly-L-Met-L-Met
-
mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
3.2
L-Met-Gly-L-Met-L-Met
-
wild type enzyme, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+
12
L-Met-L-Ala-L-Ser
-
wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
15
L-Met-L-Ala-L-Ser
-
mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
1.8
L-Met-L-Pro-4-nitroanilide
-
truncated mutant lacking N-terminal 89 amino acids, pH 7.5, 22°C
1
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp
-
mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
1
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp
-
wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
0.59
L-Met-p-nitroanilide
-
in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
3
L-Met-p-nitroanilide
-
in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
1.24
L-Met-PSI[C(O)S]Gly-L-Phe
-
Co(II)-form of enzyme, 22°C, pH 7.0
1.28
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
6.75
L-Met-PSI[C(O)S]Gly-L-Phe
-
Zn(II)-form of enzyme, 22°C, pH 7.0
8.81
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
0.386
L-methionine 4-nitroanilide
wild-type, pH not specified in the publication, temperature not specified in the publication
0.4019
L-methionine 4-nitroanilide
mutant F309M, pH not specified in the publication, temperature not specified in the publication
0.543
L-methionine 4-nitroanilide
pH not specified in the publication, temperature not specified in the publication
0.011
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Ni2+
0.082
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Co2+
0.161
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Fe2+
0.17
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Mn2+
0.111
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.115
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.13
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.144
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.154
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.155
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.161
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.168
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication
2
Met-Gly-Met-Met
-
wild-type enzyme and mutant enzyme H178A, Fe(II) loaded, pH 7.5
3.2
Met-Gly-Met-Met
-
wild-type enzyme and mutant enzyme H178A, Co(II) loaded, pH 7.5
5.1
Met-Gly-Met-Met
-
in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
18.3
Met-Gly-Met-Met
-
in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
0.18
Met-Pro-p-nitroanilide
-
in 40 mM HEPES, pH 8.0, and 100 mM NaCl, at 23°C
0.576
Met-Pro-p-nitroanilide
in 40 mM HEPES, pH 8.0, and 100 mM NaCl, at 23°C
additional information
additional information
metal binding kinetics, overview
-
additional information
additional information
-
metal binding kinetics, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.43
L-alanine-4-methylcoumarin-7-amide
presence of Cu2+, pH 8.0, 37°C
1.47
L-alanine-4-methylcoumarin-7-amide
presence of Ni2+, pH 8.0, 37°C
1.5
L-alanine-4-methylcoumarin-7-amide
presence of Ca2+, pH 8.0, 37°C
1.66
L-alanine-4-methylcoumarin-7-amide
presence of Mn2+, pH 8.0, 37°C
1.82
L-alanine-4-methylcoumarin-7-amide
presence of Mg2+, pH 8.0, 37°C
2.13
L-alanine-4-methylcoumarin-7-amide
presence of Co2+, pH 8.0, 37°C
0.078
L-Met 4-nitroanilide
presence of Co2+, pH 8.0, 22°C
0.08
L-Met 4-nitroanilide
presence of Co2+, pH 8.0, 22°C
0.08
L-Met 4-nitroanilide
presence of Ni2+, pH 8.0, 22°C
0.133
L-Met 4-nitroanilide
presence of Ni2+, pH 8.0, 22°C
0.001
L-Met-Gly-L-Met-L-Met
mutant enzyme D97N, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5
0.002
L-Met-Gly-L-Met-L-Met
mutant enzyme D97E, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5
0.003
L-Met-Gly-L-Met-L-Met
mutant enzyme D97A, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5
0.003
L-Met-Gly-L-Met-L-Met
-
mutant enzyme H79A, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+
1.8
L-Met-Gly-L-Met-L-Met
-
mutant enzyme H79A, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+
4.6
L-Met-Gly-L-Met-L-Met
-
wild type enzyme, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Mn2+
4.8
L-Met-Gly-L-Met-L-Met
-
mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
18.3
L-Met-Gly-L-Met-L-Met
wild type enzyme, Co2+-loaded, in 25 mM HEPES buffer, at 30°C and pH 7.5
18.3
L-Met-Gly-L-Met-L-Met
-
wild type enzyme, in 25 mM HEPES buffer (pH 7.5) containing 150 mM KCl, in the presence of 3 equivalents of Co2+
18.3
L-Met-Gly-L-Met-L-Met
-
wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
3
L-Met-L-Ala-L-Ser
-
mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
11
L-Met-L-Ala-L-Ser
-
wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
0.425
L-Met-L-Pro-4-nitroanilide
-
truncated mutant lacking N-terminal 89 amino acids, pH 7.5, 22°C
70
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp
-
mutant enzyme H63A, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
84
L-Met-L-Ser-L-Ser-L-His-L-Arg-L-Trp-L-Asp-L-Trp
-
wild type enzyme, in 25 mM HEPES buffer, pH 7.5, and 150 mM KCl, at 30°C
0.006
L-Met-p-nitroanilide
-
in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
0.057
L-Met-p-nitroanilide
-
in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
0.97
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
7.31
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
12.8
L-Met-PSI[C(O)S]Gly-L-Phe
-
Zn(II)-form of enzyme, 22°C, pH 7.0
15.8
L-Met-PSI[C(O)S]Gly-L-Phe
-
Mn(II)-form of enzyme, 22°C, pH 7.0
16.61
L-Met-PSI[C(O)S]Gly-L-Phe
-
N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
0.0033
L-methionine 4-nitroanilide
mutant F309M, pH not specified in the publication, temperature not specified in the publication
0.005
L-methionine 4-nitroanilide
pH not specified in the publication, temperature not specified in the publication
0.0483
L-methionine 4-nitroanilide
wild-type, pH not specified in the publication, temperature not specified in the publication
0.014
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Fe2+
0.045
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Ni2+
0.07
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Mn2+
0.36
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Co2+
0.0000508
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.000055
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.000137
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.000159
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.000263
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.000305
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.000312
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.000449
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.0633
Met-7-amido-4-methylcoumarin
-
pH 7.5, 30°C, in presence of 0.01 mM CoCl2
11.7
Met-Ala-Ser
-
calculated with 29.5 kDa as molecular mass, pH 7.5, 30°C
1516
Met-Ala-Ser
-
calculated with 33.1 kDa as molecular mass, pH 7.5, 30°C
9.63
Met-Gly-Met-Met
-
calculated with 29.5 kDa as molecular mass, pH 7.5, 30°C
18.3
Met-Gly-Met-Met
-
in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
188
Met-Gly-Met-Met
-
in 25 mM HEPES buffer at 30°C (pH 7.5) with 150 mM KCl
0.0065
Met-Pro-p-nitroanilide
in 40 mM HEPES, pH 8.0, and 100 mM NaCl, at 23°C
1.82
Met-Pro-p-nitroanilide
-
in 40 mM HEPES, pH 8.0, and 100 mM NaCl, at 23°C
additional information
additional information
-
turnover-numbers of truncated enzyme
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.5
L-alanine-4-methylcoumarin-7-amide
presence of Cu2+, pH 8.0, 37°C
5.17
L-alanine-4-methylcoumarin-7-amide
presence of Ni2+, pH 8.0, 37°C
9.8
L-alanine-4-methylcoumarin-7-amide
presence of Mn2+, pH 8.0, 37°C
10
L-alanine-4-methylcoumarin-7-amide
presence of Mg2+, pH 8.0, 37°C
12
L-alanine-4-methylcoumarin-7-amide
presence of Ca2+, pH 8.0, 37°C
13.83
L-alanine-4-methylcoumarin-7-amide
presence of Co2+, pH 8.0, 37°C
153
L-Met 4-nitroanilide
presence of Co2+, pH 8.0, 22°C
171
L-Met 4-nitroanilide
presence of Ni2+, pH 8.0, 22°C
404
L-Met 4-nitroanilide
presence of Co2+, pH 8.0, 22°C
867
L-Met 4-nitroanilide
presence of Ni2+, pH 8.0, 22°C
10
L-methionine 4-nitroanilide
pH not specified in the publication, temperature not specified in the publication
10
L-methionine 4-nitroanilide
mutant F309M, pH not specified in the publication, temperature not specified in the publication
128
L-methionine 4-nitroanilide
wild-type, pH not specified in the publication, temperature not specified in the publication
0.41
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Mn2+
0.87
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Fe2+
4.39
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Co2+
40.91
L-methionine-4-methylcoumarin-7-amide
-
recombinant isozyme MetAP1a in presence of Ni2+
0.00033
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.000479
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.000948
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.00105
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.0017
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.00217
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.020 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.00275
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.00278
Met-4-methylcoumaryl-7-amide
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.002 - 0.02
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
0.000001
3-(anilino)-5-(3-methyl-2-butenylthio)-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.000015
3-(N-methyl-anilino)-5-benzylthio-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.000066
3-anilino-5-(3-methyl-butylthio)-methylthio-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.0000005
3-anilino-5-benzylthio-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.01
3-anilino-5-benzylthio-1-methyl-1,2,4-triazole
IC50 above 0.01 mM, in 50 mM HEPES-Na+ (pH 7.5), with 100 mM NaCl
0.0013
3-anilino-5-benzylthio-2-methyl-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.001
3-anilino-5-methylthio-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.000003
3-[2-(isopropyl)-anilino]-5-(furan-2-ylmethylthio)-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.000024
3-[2-(isopropyl)-anilino]-5-(furan-3-ylmethylthio)-1,2,4-triazole
in 50 mM HEPES (pH 7.5), with 100 mM NaCl
0.00000004
5-(benzylsulfanyl)-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000017
5-(benzylsulfanyl)-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000043
5-(benzylsulfanyl)-N-(4-chlorophenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000005
5-(benzylsulfanyl)-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000007
5-(benzylsulfanyl)-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00074
5-(benzylsulfanyl)-N-biphenyl-2-yl-4H-1,2,4-triazol-3-amine
apparent value
0.162
5-[(2E)-hepta-2,6-dien-4-yn-1-ylidene]pyrimidine-2,4,6(1H,3H,5H)-trione
-
0.00000015
5-[(3-methylbut-2-en-1-yl)sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000033
5-[(cyclohexylmethyl)sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000083
5-[(cyclohexylmethyl)sulfanyl]-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000031
5-[(cyclohexylmethyl)sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0001
5-[(cyclohexylmethyl)sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000012
5-[[(2-methyl-2,5-dihydro-1,3-thiazol-4-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000036
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000035 - 0.0000078
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
0.00000023
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000013
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.00000065
5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.000061
5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.01
5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
Ki above 0.01 mM, apparent value
0.0000024
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(2-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.000004
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(3,4-dimethoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000021
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(4-methoxyphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000033
5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000005
methyl 4-([5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
apparent value
0.0000027
methyl 4-([5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
apparent value
0.0000009
methyl 4-([5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
apparent value
0.0000009
methyl 4-([5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]amino)benzoate
apparent value
0.0000038
methyl 4-[(5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.0000008
methyl 4-[(5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.00000041
methyl 4-[(5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.00001
methyl 4-[(5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.000135
methyl 4-[(5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.0000013
methyl 4-[(5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-yl)amino]benzoate
apparent value
0.0000007
methyl 4-[[5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]amino]benzoate
apparent value
0.0000037
N-(2-methylphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000038
N-(2-methylphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000025
N-(2-methylphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000009
N-(3,4-dimethoxyphenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000024
N-(3,4-dimethoxyphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000096
N-(3,4-dimethoxyphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000021
N-(3,4-dimethoxyphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000007
N-(3,4-dimethoxyphenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000013
N-(3,4-dimethoxyphenyl)-5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.001
N-(3,4-dimethoxyphenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.001 mM, apparent value
0.000018
N-(3,4-dimethoxyphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00000052
N-(4-chlorophenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000052
N-(4-chlorophenyl)-5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000004
N-(4-chlorophenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000025
N-(4-chlorophenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000048
N-(4-chlorophenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000018
N-(4-chlorophenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfany]-4H-1,2,4-triazol-3-amine
apparent value
0.00000061
N-(4-chlorophenyl)-5-[[2-(2-fluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.01
N-(4-chlorophenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000023
N-(4-chlorophenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00000016
N-(4-methoxyphenyl)-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000018
N-(4-methoxyphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000061
N-(4-methoxyphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000016
N-(4-methoxyphenyl)-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.000034
N-(4-methoxyphenyl)-5-[[2-(2-methoxyphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000078
N-(4-methylphenyl)-5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000057
N-(4-methylphenyl)-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000052
N-(4-methylphenyl)-5-[(thiophen-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000078
N-(4-methylphenyl)-5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000065
N-(4-methylphenyl)-5-[[2-(2-methylphenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000091
N-(5-[[(2-methyl-1,3-thiazolidin-4-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)pyridin-3-amine
apparent value
0.0000015
N-(5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-yl)pyridin-3-amine
apparent value
0.00035
N-biphenyl-2-yl-5-[(2-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.002
N-biphenyl-2-yl-5-[(2-methoxybenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.002 mM, apparent value
0.002
N-biphenyl-2-yl-5-[(2-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.002 mM, apparent value
0.002
N-biphenyl-2-yl-5-[(3,4-difluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.002 mM, apparent value
0.00048
N-biphenyl-2-yl-5-[(3-methylbut-2-en-1-yl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00065
N-biphenyl-2-yl-5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.002
N-biphenyl-2-yl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Ki above 0.002 mM, apparent value
0.0017
N-biphenyl-2-yl-5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00000075
N-phenyl-5-[(thiophen-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.0000015
N-[4-(chloromethyl)phenyl]-5-[[2-(3,4-difluorophenyl)ethyl]sulfanyl]-4H-1,2,4-triazol-3-amine
apparent value
0.00000004
N-[5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.0000003
N-[5-[(2-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.0000017
N-[5-[(2-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.0000005
N-[5-[(3,4-difluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.000003
N-[5-[(cyclohexylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.0000057
N-[5-[(pyridin-2-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridin-3-amine
apparent value
0.000000245
[(1R)-1-carbamoyl-2-methyl-propyl]-carbamic acid-(3R,4S,5S,6R)-5-methoxy-4-[(2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiranyl]-1-oxaspiro(2,5)oct-6-yl ester
-
recombinant MetAP-2, in 50 mM Hepes, 100 mM MnCl2, 100 mM NaCl, 0.005% (w/v) bovine serum albumin, 0.006% (w/v) 3-[(3-cholamidopropyl)dimethylammonio]propanesulphonic acid, at pH 7.5
0.002
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
-
Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.003
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
-
Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.02
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
-
Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.02
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
-
Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.003
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
-
Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.008
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
-
Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.44
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
-
Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.75
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
-
Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.0000035
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000078
5-[[(5-methylisoxazol-3-yl)methyl]sulfanyl]-N-(4-methylphenyl)-4H-1,2,4-triazol-3-amine
apparent value
0.0000287
N-(5-chloroquinolin-8-yl)methanesulfonamide
Co(II)-form of enzyme
0.0079
[amino(cyclohexyl)methyl]phosphonic acid
pH not specified in the publication, temperature not specified in the publication
0.5
[amino(cyclohexyl)methyl]phosphonic acid
IC50 value above 0.5 mM, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02 - 0.034
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
0.0013 - 0.179
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[(1-isobutyrylpiperidin-3-yl)-methyl]-2-methoxy-8,8-dimethylnon-6-enamide
0.00054 - 0.075
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[2-(mesityloxy)ethyl]-2-methoxy-8,8-dimethylnon-6-enamide
0.00076 - 0.201
(2R,3R,4S,5R,E)-N-(2,3-dihydro-1H-inden-2-yl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
0.00062 - 0.12
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
0.0002 - 0.08
(2R,3R,4S,5R,E)-N-[3-(4-fluorophenyl)-3-(furan-2-yl)propyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
0.0004 - 0.15
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
0.00096 - 0.187
(2R,3R,4S,5R,E)-N-[[1-(cyclopropanecarbonyl)piperidin-3-yl]methyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
0.0123
(3R)-amino-(2S)-hydroxypentanoic acid
Escherichia coli
-
IC50: 0.0123 mM for the Co2+-substituted enzyme, 0.0115 mM for the Mn2+-substituted enzyme, 0.0093 mM for the Zn2+-substituted enzyme, 0.0223 for the Ni2+-substituted enzyme
0.0000006
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (2R)-3-methyl-1-(2-(1-methylpyrrolidin-2-yl)ethylamino)-1-oxobutan-2-ylcarbamate
Homo sapiens
-
above, in HUVEC
0.000000095
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-1-amino-3-methyl-1-oxobutan-2-ylcarbamate
Homo sapiens
-
in HUVEC
0.0000017
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-3-methyl-1-(morpholinoamino)-1-oxobutan-2-ylcarbamate
Homo sapiens
-
in HUVEC
0.0000006
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl (R)-3-methyl-1-oxo-1-(2-(pyrrolidin-1-yl)ethylamino)butan-2-ylcarbamate
Homo sapiens
-
in HUVEC
0.0000017
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 1-amino-2-methyl-1-oxopropan-2-ylcarbamate
Homo sapiens
-
in HUVEC
0.0000007
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 1-carbamoylcyclopentylcarbamate
Homo sapiens
-
in HUVEC
0.0000002
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 2-(1-methylpyrrolidin-2-yl)ethylcarbamate
Homo sapiens
-
above, in HUVEC
0.0000001
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl 2-(pyrrolidin-1-yl)ethylcarbamate
Homo sapiens
-
in HUVEC
0.00000006
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl isopropylcarbamate
Homo sapiens
-
in HUVEC
0.0000007
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl morpholinocarbamate
Homo sapiens
-
in HUVEC
0.0000011
(3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yl tert-butylcarbamate
Homo sapiens
-
in HUVEC
0.00000025
(3R,5S,6R)-5-methoxy-4-[(3R)-2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-1-oxaspiro[2.5]oct-6-yl (chloroacetyl)carbamate
Homo sapiens
-
in HUVEC
0.00021
(5,5-Dimethyl-4,5-dihydro-thiazol-2-yl)-(3-methyl-pyridin-2-yl)-amine
Escherichia coli
-
IC50 for Co-EcMetAP1: 0.00021 mM
0.000027
(8S)-2-[[(4-fluorophenyl)sulfonyl]amino]-8-methyl-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
Homo sapiens
-
0.000000036
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-2-phenylacetate
Homo sapiens
-
in HUVEC
0.00000004
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-3-methylbutanoate
Homo sapiens
-
in HUVEC
0.000000038
(R)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-4-methylpentanoate
Homo sapiens
-
in HUVEC
0.000000018
(S)-methyl 2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)-3-methylbutanoate
Homo sapiens
-
in HUVEC
0.0000013
1-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonyl)-piperidine-4-carboxylic acid
Homo sapiens
-
in HUVEC
0.00312
1-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)-2-(2-sulfanylmorpholin-4-yl)ethanone
Plasmodium falciparum
-
-
0.00154
1-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)-2-(2-sulfanylphenyl)ethanone
Plasmodium falciparum
-
-
0.00124
1-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)-2-(4-fluoro-2-sulfanylphenyl)ethanone
Plasmodium falciparum
-
-
0.00102
1-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)-2-(4-methoxy-2-sulfanylphenyl)ethanone
Plasmodium falciparum
-
-
0.0011 - 0.0081
1-(5-chloro-6-methyl-2-pyridin-2-ylpyrimidin-4-yl)-4-(2,4-dichlorobenzyl)-1,4-diazepane
0.00046
1-benzyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.00099
1-benzyl-2-(pyridin-2-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.00118
1-[2-pyridin-2-yl-6-(trifluoromethyl)-3,4-dihydropyrimidin-4-yl]propane-2-thiol
Plasmodium falciparum
-
-
0.0001
2-(2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)ethyl)-1,1-dimethylpyrrolidinium iodide
Homo sapiens
-
in HUVEC
0.000016
2-(2-aminoethoxy)-3-ethyl-6-[[(2-propylphenyl)sulfonyl]amino]benzoic acid
Mus musculus
-
0.000046
2-(2-aminoethoxy)-3-ethyl-6-[[(4-fluorophenyl)sulfonyl]amino]benzoic acid
Mus musculus
-
0.000024
2-(2-aminoethoxy)-6-[([2-[3-(diethylamino)propyl]-4-fluorophenyl]sulfonyl)amino]-3-ethylbenzoic acid
Mus musculus
-
0.0058
2-(carboxymethoxy)-3-ethyl-6-[[(4-fluorophenyl)sulfonyl]amino]benzoic acid
Mus musculus
-
0.0005
2-(prop-1-en-2-yl)-5-[2-(trifluoromethyl)phenyl]furan
Rickettsia prowazekii
pH 7.0, 30°C, Hill slope 2.1
0.0013
2-butyl-6-[[(4-fluorophenyl)sulfonyl]amino]-3-methylbenzoic acid
Mus musculus
-
0.000015
2-chloro-3-ethyl-6-[[(4-fluorophenyl)sulfonyl]amino]benzoic acid
Mus musculus
-
0.00006
2-ethenyl-6-[[(4-fluorophenyl)sulfonyl]amino]-3-methylbenzoic acid
Mus musculus
-
0.000038
2-ethoxy-3-ethyl-6-[[(4-fluorophenyl)sulfonyl]amino]benzoic acid
Mus musculus
-
0.000011
2-ethyl-6-[[(4-fluorophenyl)sulfonyl]amino]-3-methoxybenzoic acid
Mus musculus
-
0.000016
2-ethyl-6-[[(4-fluorophenyl)sulfonyl]amino]-3-methylbenzoic acid
Mus musculus
-
0.00107
2-pyridin-2-yl-4-(trifluoromethyl)-6-[2-(trifluoromethyl)benzyl]-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.0039
2-[(2,1,3-benzothiadiazol-4-ylsulfonyl)amino]-5-bromobenzoic acid
Homo sapiens
-
0.000009
2-[(phenylsulfonyl)amino]-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
Mus musculus
-
0.02
2-[([4-[(E)-(5-amino-3-imino-3H-pyrazol-4-yl)diazenyl]phenyl]sulfinyl)oxy]hydrazinecarboximidamide
Escherichia coli
-
-
0.0296 - 0.0441
2-[2-(2-amino-4-methylsulfanyl-butyrylsulfanyl)-3-phenyl-propionylamino]-3-hydroxy-propionic acid
0.0286 - 0.0498
2-[2-(2-Amino-4-methylsulfanyl-butyrylsulfanyl)-5-methyl-hexanoylamino]-3-hydroxy-propionic acid
0.0125 - 0.0252
2-[2-(3-Amino-2-hydroxy-heptanoylamino)-propionylamino]-4-methyl-pentanoic acid methyl ester
0.037
2-[4-(2-Cyano-2-ethoxycarbonyl-1-methyl-vinyl)-phenyl]-1,3-dioxo-2,3-dihydro-1H-isoindole-5-carboxylic acid
Escherichia coli
-
IC50 for Co-EcMetAP1: 0.037 mM
0.00001
2-[[(4-fluorophenyl)sulfonyl]amino]-5,6,7,8-tetrahydronaphthalene-1-carboxylic acid
Homo sapiens
-
0.00002
2-[[(4-fluorophenyl)sulfonyl]amino]-8-methyl-5,6-dihydronaphthalene-1-carboxylic acid
Homo sapiens
-
0.0001
3-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)-N,N,N-trimethylpropan-1-aminium iodide
Homo sapiens
-
in HUVEC
0.000015
3-((R)-2-(((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)-carbonylamino)-3-methylbutanamido)benzoic acid
Homo sapiens
-
in HUVEC
0.000034 - 0.00492
3-(2,2,2-trifluoroacetylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
0.00034 - 0.00054
3-(2,2-dimethylpropionylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
0.00068 - 0.00078
3-(2,2-dimethylpropionyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
0.01178
3-(2,3-dihydro-1,4-benzodioxin-6-yl)-5-{[(2-nitrophenyl)methyl]sulfanyl}-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00093
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-fluorobenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01766
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(2-methylbenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03071
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(3-methoxybenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00224
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(4-fluorobenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.01239
3-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-5-(4-nitrobenzylthio)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00395
3-(2,4-difluorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0048
3-(2,6-difluorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0016
3-(2-acetyloxybenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0016 mM
0.00537
3-(2-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00184
3-(2-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0025 - 0.0034
3-(3-bromo-4-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
0.00591
3-(3-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00192
3-(3-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0017 - 0.00302
3-(3-methoxy-2-nitrobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
0.00022 - 0.00077
3-(3-methylbut-2-enoylamino)pyridien-2-carboxylic acid thiazol-2-ylamide
0.00015 - 0.00467
3-(3-methylbut-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
0.00729
3-(4-bromobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00345
3-(4-chlorobenzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00014 - 0.00024
3-(4-methylpent-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
0.00031 - 0.000671
3-(5-methylhex-4-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
0.00601
3-(benzylthio)-5-(2,3-dihydrobenzo[b][1,4]dioxin-6-yl)-4-phenyl-4H-1,2,4-triazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0082
3-acetyloxypyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0082 mM
0.0328
3-aminopyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 1.7 mM, IC50: 0.0328 mM
0.00089
3-benzoylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00089 mM
0.000015
3-ethyl-2-methoxy-6-[[(2-[[2-(1-methylpyrrolidin-2-yl)ethyl]amino]phenyl)sulfonyl]amino]benzoic acid
Mus musculus
-
0.000018
3-ethyl-2-methoxy-6-[[(2-[[3-(2-methylpiperidin-1-yl)propyl]amino]phenyl)sulfonyl]amino]benzoic acid
Mus musculus
-
0.00025
3-imino-4-[(E)-[2-(trifluoromethyl)phenyl]diazenyl]-3H-pyrazol-5-amine
Escherichia coli
-
-
0.00025
3-imino-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-3H-pyrazol-5-amine
Escherichia coli
-
-
0.002
3-[(E)-(5-amino-3-imino-3H-pyrazol-4-yl)diazenyl]-2-hydroxybenzoic acid
Escherichia coli
-
-
0.000009
3-[(phenylsulfonyl)amino]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
Homo sapiens
-
0.0021 - 0.0099
3-[3-(2-methoxyphenyl)acryloyloxy]pyridine-2-carboxylic acid thiazol-2-ylamide
0.000015
3-[[(4-fluorophenyl)sulfonyl]amino]naphthalene-2-carboxylic acid
Homo sapiens
-
0.0000007
4-((((3R,4S,5S,6R)-5-methoxy-4-((2R,3R)-2-methyl-3-(3-methylbut-2-enyl)oxiran-2-yl)-1-oxaspiro[2.5]octan-6-yloxy)carbonylamino)methyl)benzoic acid
Homo sapiens
-
in HUVEC
0.0166
4-(1,3-thiazol-2-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.1
4-(1-methyl-1H-imidazol-2-yl)benzene-1,2-diol
Escherichia coli
-
IC50 above 0.1 mM, using Fe2+, Co2+, or Mn2+-activated MetAP enzymes
0.000152
4-(5-chloro-6-methyl-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)morpholine
Plasmodium falciparum
-
-
0.0112
4-(5-methoxy-1,3-oxazol-2-yl)benzene-1,2-diol
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.1
4-(5-methoxy-2-phenyl-3,4-dihydropyrimidin-4-yl)morpholine
Plasmodium falciparum
-
IC50 above 0.1 mM
0.00513
4-(5-methoxy-2-pyridin-2-yl-3,4-dihydropyrimidin-4-yl)morpholine
Plasmodium falciparum
-
-
0.00055
4-[(E)-(3-chloro-2-methylphenyl)diazenyl]-3-imino-3H-pyrazol-5-amine
Escherichia coli
-
-
0.000038
5-((R)-1-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl-pyrrolidin-2-ylmethoxy)-isoquinoline
Homo sapiens
pH not specified in the publication, temperature not specified in the publication
0.002
5-(2-chlorophenyl)-2-furohydrazide
Escherichia coli
-
Mn2+-activated enzyme (0.004 mM MnCl2), pH 7.5, 21°C
0.0002
5-chloro-2-(5-chloropyridin-2-yl)-6-methyl-N-((R)-2-phenyl-2-(4-phenylbutylamino)ethyl)pyrimidin-4-amine
Homo sapiens
22°C, pH not specified in the publication
0.000063
5-chloro-2-(5-chloropyridin-2-yl)-N-(2,4-diphenylbutyl)-6-methylpyrimidin-4-amine
Homo sapiens
22°C, pH not specified in the publication
0.000843
5-chloro-4,6-dimethyl-2-pyridin-2-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.000521
5-chloro-4-methyl-2-pyridin-2-yl-6-pyrrolidin-1-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.000158
5-chloro-4-methyl-6-(4-methylbenzyl)-2-pyridin-2-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.000112
5-chloro-6-(2-ethylphenyl)-4-methyl-2-pyridin-2-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.1
5-methoxy-2-phenyl-6-pyrrolidin-1-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
IC50 above 0.1 mM
0.1
5-methoxy-2-pyridin-2-yl-3,4-dihydropyrimidin-4-ol
Plasmodium falciparum
-
IC50 above 0.1 mM
0.00791
5-methoxy-2-pyridin-2-yl-6-pyrrolidin-1-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.1
5-methoxy-6-methyl-2-phenyl-1,6-dihydropyrimidine
Plasmodium falciparum
-
IC50 above 0.1 mM
0.00217
5-methoxy-6-methyl-6-phenyl-2-pyridin-2-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.00113
5-methoxy-6-[(4-methoxyphenyl)sulfanyl]-2-pyridin-2-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.0132
5-methoxy-6-[2-methyl-3-(3-methylbut-2-en-1-yl)oxiran-2-yl]-4-oxobicyclo[3.1.0]hexane-1-carbaldehyde
Homo sapiens
-
0.03
5-[[(4-chlorophenyl)methyl]sulfanyl]-4H-1,2,4-triazol-3-amine
Rickettsia prowazekii
pH 7.0, 30°C, Hill slope 1.6
0.0575
6-(1,5-dimethylhex-4-en-1-yl)-5-(hydroxymethyl)-1-methoxybicyclo[3.1.0]hexan-2-one
Homo sapiens
-
0.00106
6-(2-chlorobenzyl)-2-pyridin-2-yl-4-(trifluoromethyl)-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.000938
6-(benzylsulfanyl)-5-chloro-4-methyl-2-pyridin-2-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.00111
6-(phenylsulfanyl)-2-pyridin-2-yl-4-(trifluoromethyl)-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.00106
6-benzyl-2-pyridin-2-yl-4-(trifluoromethyl)-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.1
6-benzyl-5-chloro-4-methyl-2-pyridin-3-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
IC50 above 0.1 mM
0.0338
6-[(1E)-1,5-dimethylhexa-1,4-dien-1-yl]-5-(hydroxymethyl)-1-methoxybicyclo[3.1.0]hexan-2-one
Homo sapiens
-
0.00104
6-[(2,4-dichlorophenyl)sulfanyl]-5-methoxy-2-pyridin-2-yl-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.00123
6-[(4-methoxyphenyl)sulfanyl]-2-pyridin-2-yl-4-(trifluoromethyl)-1,6-dihydropyrimidine
Plasmodium falciparum
-
-
0.000026
6-[([2-[(1E)-3-(diethylamino)prop-1-en-1-yl]-4-fluorophenyl]sulfonyl)amino]-3-ethyl-2-methoxybenzoic acid
Mus musculus
-
0.036
6-[[(2-bromo-4-fluorophenyl)sulfonyl]amino]-2-(1H-imidazol-4-yl)-3-methoxybenzoic acid
Mus musculus
-
0.001
6-[[(2-bromo-4-fluorophenyl)sulfonyl]amino]-2-furan-2-yl-3-methoxybenzoic acid
Mus musculus
-
0.00002
6-[[(2-bromo-4-fluorophenyl)sulfonyl]amino]-2-furan-3-yl-3-methoxybenzoic acid
Mus musculus
-
0.000015
6-[[(2-[(1E)-3-(diethylamino)prop-1-en-1-yl]-4-fluorophenyl]sulfonyl)amino]-3-furan-3-yl-2-methoxybenzoic acid
Mus musculus
-
0.000017
6-[[(2-[[3-(dimethylamino)propyl]amino]-4-fluorophenyl)sulfonyl]amino]-3-furan-3-yl-2-methoxybenzoic acid
Mus musculus
-
0.00001
6-[[(2-[[4-(dimethylamino)butyl]amino]phenyl)sulfonyl]amino]-3-ethyl-2-methoxybenzoic acid
Mus musculus
-
0.0025
6-[[(4-fluorophenyl)sulfonyl]amino]-2-(1-hydroxyethyl)-3-methylbenzoic acid
Mus musculus
-
0.008
6-[[(4-fluorophenyl)sulfonyl]amino]-2-(hydroxymethyl)-3-methylbenzoic acid
Mus musculus
-
0.000008
6-[[(4-fluorophenyl)sulfonyl]amino]-2-furan-3-yl-3-methoxybenzoic acid
Mus musculus
-
0.00028
6-[[(4-fluorophenyl)sulfonyl]amino]-2-methoxy-3-(1H-pyrazol-4-yl)benzoic acid
Mus musculus
-
0.00015
6-[[(4-fluorophenyl)sulfonyl]amino]-3-methyl-2-propylbenzoic acid
Mus musculus
-
0.000031
A-310840
Homo sapiens
-
IC50: 0.000031 mM for enzyme with Zn2+, 0.000043 mM for enzyme with Ni2+, 0.000069 mM for enzyme with Co2+, 0.000026 for enzyme with Fe2+, 0.0578 mM for enzyme with Mn2+
0.000121
A-311263
Homo sapiens
-
IC50: 0.000121 mM for enzyme with Zn2+, 0.000107 mM for enzyme with Ni2+, 0.000149 mM for enzyme with Co2+, 0.00011 mM for enzyme with Fe2+, 0.000055 mM for enzyme with Mn2+
0.014
ethyl 5-(3,4-dihydroxyphenyl)-1,3-oxazole-4-carboxylate
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.000599 - 0.001455
MCB2379
Staphylococcus aureus
-
IC50: 599 nM in presence of Co2+, 1455 nM in presence of Zn2+
0.0000437 - 0.0003
MCB2813
Staphylococcus aureus
-
IC50: 43.7 nM in presence of Co2+, 300 nM in presence of Zn2+
0.025
methyl N-[(2S,3R)-3-amino-2-hydroxy-3-(4-methylphenyl)propanoyl]-L-alanylleucinate
Escherichia coli
-
-
0.0035
methyl N-[(2S,3R)-3-amino-2-hydroxy-3-[4-(1-methylethyl)phenyl]propanoyl]-L-alanylleucinate
Escherichia coli
-
-
0.0017
methyl [[(2S)-2-([(2S,3R)-3-amino-2-hydroxy-3-[4-(trifluoromethyl)phenyl]propanoyl]amino)propanoyl]amino]acetate
Escherichia coli
-
-
0.000093
N-((R)-2-(5-chloro-2-(5-chloropyridin-2-yl)-6-methylpyrimidin-4-ylamino)-1-phenylethyl)-3-phenylpropanamide
Homo sapiens
22°C, pH not specified in the publication
0.00072
N-(1,3-thiazol-2-yl)-3-[(N-[2-[2-(2-[2-[(1H-triaziren-1-ylacetyl)amino]ethoxy]ethoxy)ethoxy]-4-[3-(trifluoromethyl)-3H-diaziren-3-yl]benzoyl]glycyl)amino]pyridine-2-carboxamide
Escherichia coli
-
-
0.000199
N-(2-aminoethyl)-N'-[5-chloro-6-methyl-2-pyridin-2-yl-4-[5-(trifluoromethyl)pyridin-2-yl]-3,4-dihydropyrimidin-4-yl]ethane-1,2-diamine
Plasmodium falciparum
-
-
0.1
N-(2-aminoethyl)-N'-[5-chloro-6-methyl-2-pyridin-3-yl-4-[5-(trifluoromethyl)pyridin-2-yl]-3,4-dihydropyrimidin-4-yl]ethane-1,2-diamine
Plasmodium falciparum
-
IC50 above 0.1 mM
0.1
N-(2-aminoethyl)-N'-[5-chloro-6-methyl-2-pyridin-4-yl-4-[5-(trifluoromethyl)pyridin-2-yl]-3,4-dihydropyrimidin-4-yl]ethane-1,2-diamine
Plasmodium falciparum
-
IC50 above 0.1 mM
0.0029
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[(2,2-dimethylpropanoyl)amino]pyridine-2-carboxamide
Homo sapiens
MetAP1
0.0035
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[(3-phenylpropanoyl)amino]pyridine-2-carboxamide
Homo sapiens
MetAP1
0.0064
N-(4,5-dihydro-1,3-thiazol-2-yl)-3-[[(1E)-2-methylpropylidene]amino]pyridine-2-carboxamide
Homo sapiens
MetAP1
0.0028
N-(5-methyl-1,2-oxazol-3-yl)pyridine-2-carboxamide
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.000804
N-1,3-thiazol-2-yl-3-(N-[(2-2-[(1H-triaziren-1-ylacetyl)amino]ethoxy]-4-[[3-(trifluoromethyl)-[3H-diaziren-3-yl]phenyl)carbonyl]glycyl]amino)pyridine-2-carboxamide
Escherichia coli
-
-
0.03 - 0.2
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
0.0134
N-but-3-en-1-yl-5-(3,4-dihydroxyphenyl)-1,3-oxazole-4-carboxamide
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.011
N-cyclopentyl-5-(3,4-dihydroxyphenyl)-1,3-oxazole-4-carboxamide
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.0148
N-cyclopropyl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.016
quinolin-8-yl 4-methylbenzenesulfonate
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0015
tert-butyl [2-(4,5-dihydro-1,3-thiazol-2-ylcarbamoyl)pyridin-3-yl]carbamate
Homo sapiens
MetAP1
0.02
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
Pyrococcus furiosus
-
Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.027
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
Pyrococcus furiosus
-
Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.032
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
Escherichia coli
-
Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.034
((2RS,3R)-3-amino-2-hydroxy-5-ethylthio)pentanoyl-((S)-(-)-(1-naphthyl)ethyl)amide
Escherichia coli
-
Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.0013
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[(1-isobutyrylpiperidin-3-yl)-methyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.045
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[(1-isobutyrylpiperidin-3-yl)-methyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.067
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[(1-isobutyrylpiperidin-3-yl)-methyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.068
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[(1-isobutyrylpiperidin-3-yl)-methyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.141
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[(1-isobutyrylpiperidin-3-yl)-methyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Ni2+, pH 7.5, 22°C
0.179
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[(1-isobutyrylpiperidin-3-yl)-methyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.00054
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[2-(mesityloxy)ethyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.0042
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[2-(mesityloxy)ethyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.0045
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[2-(mesityloxy)ethyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.0069
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[2-(mesityloxy)ethyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.0079
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[2-(mesityloxy)ethyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.033
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[2-(mesityloxy)ethyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Ni2+, pH 7.5, 22°C
0.075
(2R,3R,4S,5R,E)-3,4,5-trihydroxy-N-[2-(mesityloxy)ethyl]-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.00076
(2R,3R,4S,5R,E)-N-(2,3-dihydro-1H-inden-2-yl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.011
(2R,3R,4S,5R,E)-N-(2,3-dihydro-1H-inden-2-yl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.018
(2R,3R,4S,5R,E)-N-(2,3-dihydro-1H-inden-2-yl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.031
(2R,3R,4S,5R,E)-N-(2,3-dihydro-1H-inden-2-yl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.14
(2R,3R,4S,5R,E)-N-(2,3-dihydro-1H-inden-2-yl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Ni2+, pH 7.5, 22°C
0.201
(2R,3R,4S,5R,E)-N-(2,3-dihydro-1H-inden-2-yl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.00062
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.0037
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.014
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.021
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.049
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.05
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.114
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Ni2+, pH 7.5, 22°C
0.12
(2R,3R,4S,5R,E)-N-(2-amino-2-oxoethyl)-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Ni2+, pH 7.5, 22°C
0.0002
(2R,3R,4S,5R,E)-N-[3-(4-fluorophenyl)-3-(furan-2-yl)propyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.0067
(2R,3R,4S,5R,E)-N-[3-(4-fluorophenyl)-3-(furan-2-yl)propyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.0081
(2R,3R,4S,5R,E)-N-[3-(4-fluorophenyl)-3-(furan-2-yl)propyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.012
(2R,3R,4S,5R,E)-N-[3-(4-fluorophenyl)-3-(furan-2-yl)propyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.052
(2R,3R,4S,5R,E)-N-[3-(4-fluorophenyl)-3-(furan-2-yl)propyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.068
(2R,3R,4S,5R,E)-N-[3-(4-fluorophenyl)-3-(furan-2-yl)propyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.08
(2R,3R,4S,5R,E)-N-[3-(4-fluorophenyl)-3-(furan-2-yl)propyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Ni2+, pH 7.5, 22°C
0.0004
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.0055
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.006
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.011
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.026
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Ni2+, pH 7.5, 22°C
0.039
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.061
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.15
(2R,3R,4S,5R,E)-N-[3-(furan-2-yl)-3-phenylpropyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Ni2+, pH 7.5, 22°C
0.00096
(2R,3R,4S,5R,E)-N-[[1-(cyclopropanecarbonyl)piperidin-3-yl]methyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.088
(2R,3R,4S,5R,E)-N-[[1-(cyclopropanecarbonyl)piperidin-3-yl]methyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Co2+, pH 7.5, 22°C
0.11
(2R,3R,4S,5R,E)-N-[[1-(cyclopropanecarbonyl)piperidin-3-yl]methyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Fe2+, pH 7.5, 22°C
0.187
(2R,3R,4S,5R,E)-N-[[1-(cyclopropanecarbonyl)piperidin-3-yl]methyl]-3,4,5-trihydroxy-2-methoxy-8,8-dimethylnon-6-enamide
Mycobacterium tuberculosis
-
apoenyme activated by Mn2+, pH 7.5, 22°C
0.0229
(3R)-amino-(2S)-hydroxyheptanoyl-Ala-Leu methyl ester
Escherichia coli
-
IC50: 0.0229 mM
0.095
(3R)-amino-(2S)-hydroxyheptanoyl-Ala-Leu methyl ester
Saccharomyces cerevisiae
-
IC50: 0.095 mM
0.009
1-(1H-benzimidazol-2-yl)thiourea
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0359
1-(1H-benzimidazol-2-yl)thiourea
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0011
1-(5-chloro-6-methyl-2-pyridin-2-ylpyrimidin-4-yl)-4-(2,4-dichlorobenzyl)-1,4-diazepane
Homo sapiens
MetAP1
0.0081
1-(5-chloro-6-methyl-2-pyridin-2-ylpyrimidin-4-yl)-4-(2,4-dichlorobenzyl)-1,4-diazepane
Homo sapiens
MetAP2
0.0005
1-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0243
1-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0324
1-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00008
2-(1,3-thiazol-2-yl)-1H-imidazo[4,5-b]pyridine
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0398
2-(1,3-thiazol-2-yl)-1H-imidazo[4,5-b]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0023
2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-amine
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0034
2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-amine
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0101
2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-amine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0017
2-(1,3-thiazol-4-yl)-1H-imidazo[4,5-c]pyridine
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.019
2-(1,3-thiazol-4-yl)-1H-imidazo[4,5-c]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0455
2-(1,3-thiazol-4-yl)-1H-imidazo[4,5-c]pyridine
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.00078
2-(1H-benzimidazol-2-yl)pyridin-3-ol
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0044
2-(1H-benzimidazol-2-yl)pyridin-3-ol
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0046
2-(pyrazin-2-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0329
2-(pyrazin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00097
2-(pyridin-2-yl)-1H-benzimidazol-5-amine
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0049
2-(pyridin-2-yl)-1H-benzimidazol-5-amine
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0093
2-(pyridin-2-yl)-1H-benzimidazol-5-amine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00057
2-(pyridin-2-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0133
2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0199
2-(pyridin-2-yl)-1H-benzimidazole
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0284
2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00043
2-(pyridin-2-yl)-1H-benzimidazole-5-carbonitrile
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0329
2-(pyridin-2-yl)-1H-benzimidazole-5-carbonitrile
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.033
2-(pyridin-2-yl)-1H-benzimidazole-5-carbonitrile
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0373
2-(pyridin-2-yl)-1H-benzimidazole-5-carbonitrile
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00024
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyrazine
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.022
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyrazine
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0401
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyrazine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0484
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyrazine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00011
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyridine
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0188
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyridine
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0267
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0276
2-(pyridin-2-yl)-1H-imidazo[4,5-b]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00055
2-(pyridin-2-yl)-1H-imidazo[4,5-c]pyridine
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.008
2-(pyridin-2-yl)-1H-imidazo[4,5-c]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0103
2-(pyridin-2-yl)-1H-imidazo[4,5-c]pyridine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0228
2-(pyridin-2-yl)-1H-imidazo[4,5-c]pyridine
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0296
2-[2-(2-amino-4-methylsulfanyl-butyrylsulfanyl)-3-phenyl-propionylamino]-3-hydroxy-propionic acid
Escherichia coli
-
IC50 for Co-EcMetAP1: 0.0296 mM
0.0365
2-[2-(2-amino-4-methylsulfanyl-butyrylsulfanyl)-3-phenyl-propionylamino]-3-hydroxy-propionic acid
Escherichia coli
-
IC50 for Zn-EcMetAP1: 0.0365 mM
0.0441
2-[2-(2-amino-4-methylsulfanyl-butyrylsulfanyl)-3-phenyl-propionylamino]-3-hydroxy-propionic acid
Escherichia coli
-
IC50 for Mn-EcMetAPa: 0.0441 mM
0.0286
2-[2-(2-Amino-4-methylsulfanyl-butyrylsulfanyl)-5-methyl-hexanoylamino]-3-hydroxy-propionic acid
Escherichia coli
-
IC50 for Co-EcMetAP1: 0.0286 mM
0.0357
2-[2-(2-Amino-4-methylsulfanyl-butyrylsulfanyl)-5-methyl-hexanoylamino]-3-hydroxy-propionic acid
Escherichia coli
-
IC50 for Ni-EcMetAP1: 0.0357 mM
0.0443
2-[2-(2-Amino-4-methylsulfanyl-butyrylsulfanyl)-5-methyl-hexanoylamino]-3-hydroxy-propionic acid
Escherichia coli
-
IC50 for Mn-EcMetAPa: 0.0443 mM
0.0498
2-[2-(2-Amino-4-methylsulfanyl-butyrylsulfanyl)-5-methyl-hexanoylamino]-3-hydroxy-propionic acid
Escherichia coli
-
IC50 for Zn-EcMetAP1: 0.0498 mM
0.0125
2-[2-(3-Amino-2-hydroxy-heptanoylamino)-propionylamino]-4-methyl-pentanoic acid methyl ester
Escherichia coli
-
IC50 for Ni-EcMetAP1: 0.0125 mM
0.0167
2-[2-(3-Amino-2-hydroxy-heptanoylamino)-propionylamino]-4-methyl-pentanoic acid methyl ester
Escherichia coli
-
IC50 for Zn-EcMetAP1: 0.0167 mM
0.0229
2-[2-(3-Amino-2-hydroxy-heptanoylamino)-propionylamino]-4-methyl-pentanoic acid methyl ester
Escherichia coli
-
IC50 for Co-EcMetAP1: 0.0229 mM
0.0252
2-[2-(3-Amino-2-hydroxy-heptanoylamino)-propionylamino]-4-methyl-pentanoic acid methyl ester
Escherichia coli
-
IC50 for Mn-EcMetAPa: 0.0252 mM
0.015
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
Pyrococcus furiosus
-
Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.044
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
Escherichia coli
-
Co2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
1
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
Escherichia coli
-
Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
1
3-((2-naphthylmethyl)sulfanyl)-4H-1,2,4-triazole
Pyrococcus furiosus
-
Mn2+-loaded wild type enzyme, in 25 mM HEPES buffer, pH 7.5, containing 150 mM KCl, at 30°C
0.000034
3-(2,2,2-trifluoroacetylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.000034 mM
0.00492
3-(2,2,2-trifluoroacetylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00492 mM
0.00034
3-(2,2-dimethylpropionylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00034 mM
0.00054
3-(2,2-dimethylpropionylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00054 mM
0.00068
3-(2,2-dimethylpropionyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00068 mM
0.00078
3-(2,2-dimethylpropionyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00078 mM
0.00028
3-(2-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00028 mM
0.1
3-(2-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50 above 0.1 mM
0.00083
3-(2-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00083 mM
0.016
3-(2-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.016 mM
0.00089
3-(2-iodobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00089 mM
0.0013
3-(2-iodobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0013 mM
0.00055
3-(2-methoxybenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00055 mM
0.0017
3-(2-methoxybenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0017 mM
0.00028
3-(2-methylbut-2-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00028 mM
0.0109
3-(2-methylbut-2-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.0109 mM
0.00039
3-(2-methylbut-2-enoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00039 mM
0.0044
3-(2-methylbut-2-enoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0044 mM
0.0021
3-(2-nitrobenzoyloxy)pyridine-2-carboxylic acid thiatol-2-ylamide
Escherichia coli
-
IC50: 0.0021 mM
0.1
3-(2-nitrobenzoyloxy)pyridine-2-carboxylic acid thiatol-2-ylamide
Escherichia coli
-
IC50 above 0.1 mM
0.0025
3-(3-bromo-4-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0025 mM
0.0034
3-(3-bromo-4-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.0034 mM
0.00071
3-(3-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00071 mM
0.1
3-(3-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50 above 0.1 mM
0.000095
3-(3-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.000095 mM
0.1
3-(3-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50 above 0.1 mM
0.0017
3-(3-methoxy-2-nitrobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0017 mM
0.00302
3-(3-methoxy-2-nitrobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00302 mM
0.00022
3-(3-methylbut-2-enoylamino)pyridien-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00022 mM
0.00077
3-(3-methylbut-2-enoylamino)pyridien-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00077 mM
0.00049
3-(3-methylbut-2-enoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00049 mM
0.0026
3-(3-methylbut-2-enoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0026 mM
0.00015
3-(3-methylbut-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00015 mM
0.00467
3-(3-methylbut-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00467 mM
0.0006
3-(3-nitrobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0006 mM
0.1
3-(3-nitrobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50 above 0.1 mM
0.00136
3-(4-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00136 mM
0.1
3-(4-fluorobenzoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50 above 0.1 mM
0.0011
3-(4-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0011 mM
0.062
3-(4-fluorobenzoyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.062 mM
0.00014
3-(4-methylpent-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00014 mM
0.00024
3-(4-methylpent-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00024 mM
0.00031
3-(5-methylhex-4-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00031 mM
0.000671
3-(5-methylhex-4-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.000671 mM
0.00013
3-(but-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00013 mM
0.00038
3-(but-3-enoylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00038 mM
0.00087
3-(cyclohexanecarbonylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00087 mM
0.1
3-(cyclohexanecarbonylamino)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50 above 0.1 mM
0.00032
3-(cyclohexanecarbonyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00032 mM
0.00239
3-(cyclohexanecarbonyloxy)pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00239 mM
0.00103
3-benzoyloxypyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00103 mM
0.00122
3-benzoyloxypyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00122 mM
0.0001
3-But-3-enoylamino-pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50 for Co-EcMetAP1: 0.0001 mM
0.00076
3-But-3-enoylamino-pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50 for Ni-EcMetAP1: 0.00076 mM
0.0224
3-But-3-enoylamino-pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50 for Zn-EcMetAP1: 0.0224 mM
0.0233
3-But-3-enoylamino-pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50 for Mn-EcMetAPa: 0.0233 mM
0.00032
3-formylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00032 mM
0.00033
3-formylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00033 mM
0.000038
3-hexanoylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.000038 mM
0.00062
3-hexanoylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00062 mM
0.000174
3-hexanoyloxypyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.000174 mM
0.00102
3-hexanoyloxypyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00102 mM
0.00187
3-hydroxypyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00187 mM
0.00486
3-hydroxypyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00486 mM
0.00192
3-iso-butoxycarbonylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00192 mM
0.0537
3-iso-butoxycarbonylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.0537 mM
0.00004
3-phenylacetylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00004 mM
0.00082
3-phenylacetylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00082 mM
0.000054
3-phenylacetyloxypyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.000054 mM
0.0002
3-phenylacetyloxypyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.0002 mM
0.00026
3-propionylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00026 mM
0.00035
3-propionylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00035 mM
0.00038
3-propionyloxypyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00038 mM
0.0054
3-propionyloxypyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0054 mM
0.00018
3-tert-butoxycarbonylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.00018 mM
0.00335
3-tert-butoxycarbonylaminopyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.00335 mM
0.00058
3-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazole
Mycobacterium tuberculosis
pH 7.5, 37°C, with Ni2+
0.002
3-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazole
Mycobacterium tuberculosis
pH 7.5, 37°C, with Co2+
0.25
3-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazole
Mycobacterium tuberculosis
-
above, recombinant isozyme MetAP1a in presence of different divalent metal ions, overview
0.0021
3-[3-(2-methoxyphenyl)acryloyloxy]pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50: 0.0021 mM
0.0099
3-[3-(2-methoxyphenyl)acryloyloxy]pyridine-2-carboxylic acid thiazol-2-ylamide
Saccharomyces cerevisiae
-
IC50: 0.0099 mM
0.0161
4-(1-benzyl-1H-1,2,3-triazol-4-yl)benzene-1,2-diol
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.0195
4-(1-benzyl-1H-1,2,3-triazol-4-yl)benzene-1,2-diol
Escherichia coli
-
using Co2+-activated MetAP enzyme
0.0246
4-(1-benzyl-1H-1,2,3-triazol-4-yl)benzene-1,2-diol
Escherichia coli
-
using Mn2+-activated MetAP enzyme
0.0202
4-(2,5-dichlorothiophen-3-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0486
4-(2,5-dichlorothiophen-3-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0624
4-(2,5-dichlorothiophen-3-yl)benzene-1,2-diol
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0074
4-(2,5-dimethylthiophen-3-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.1
4-(2,5-dimethylthiophen-3-yl)benzene-1,2-diol
Escherichia coli
IC50 above 0.1 mM, Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.1
4-(2,5-dimethylthiophen-3-yl)benzene-1,2-diol
Escherichia coli
IC50 above 0.1 mM, Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0066
4-(2-aminothiazol-4-yl)benzene-1,2-diol
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0066
4-(2-aminothiazol-4-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.1
4-(2-aminothiazol-4-yl)benzene-1,2-diol
Escherichia coli
IC50 above 0.1 mM, Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.000031 - 0.0007
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Mycobacterium tuberculosis
-
recombinant isozyme MetAP1a in presence of different divalent metal ions, overview
0.00095
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.013
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0131
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.024
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.032
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.034
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.039
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.056
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.072
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.079
4-(2-methyl-1,3-thiazol-4-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.0073
4-(3-(2-bromoethyl)thiophen-2-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.014
4-(3-(2-bromoethyl)thiophen-2-yl)benzene-1,2-diol
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0224
4-(3-(2-bromoethyl)thiophen-2-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0092
4-(3-butylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0482
4-(3-butylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.1
4-(3-butylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
IC50 above 0.1 mM, Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0129
4-(3-ethylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0557
4-(3-ethylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0626
4-(3-ethylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.00007 - 0.0023
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Mycobacterium tuberculosis
-
recombinant isozyme MetAP1a in presence of different divalent metal ions, overview
0.00051
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.00065
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.008
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.008
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.021
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.022
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.023
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.023
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
-
using Mn2+-activated MetAP enzyme
0.027
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.03
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.033
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.041
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
-
using Co2+-activated MetAP enzyme
0.0427
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.055
4-(3-methylthiophen-2-yl)benzene-1,2-diol
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.014
4-(3-propylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0343
4-(3-propylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.1
4-(3-propylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
IC50 above 0.1 mM, Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0021
4-(4-bromo-2,5-dimethylthiophen-3-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0024
4-(4-bromo-2,5-dimethylthiophen-3-yl)benzene-1,2-diol
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0031
4-(4-bromo-2,5-dimethylthiophen-3-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0128
4-(5-chlorothiophen-2-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0448
4-(5-chlorothiophen-2-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.1
4-(5-chlorothiophen-2-yl)benzene-1,2-diol
Escherichia coli
IC50 above 0.1 mM, Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0106
4-(5-fluoropyrimidin-2-yl)benzene-1,2-diol
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.0526
4-(5-fluoropyrimidin-2-yl)benzene-1,2-diol
Escherichia coli
-
using Co2+-activated MetAP enzyme
0.028
4-(5-methylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0327
4-(5-methylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0515
4-(5-methylthiophen-2-yl)benzene-1,2-diol
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0051
4-(thiophen-2-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0157
4-(thiophen-2-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0237
4-(thiophen-2-yl)benzene-1,2-diol
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0038
4-(thiophen-3-yl)benzene-1,2-diol
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2
0.0275
4-(thiophen-3-yl)benzene-1,2-diol
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0404
4-(thiophen-3-yl)benzene-1,2-diol
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.01
5,6-dimethyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0388
5,6-dimethyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0024
5,6-dimethyl-2-(pyridin-2-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0179
5,6-dimethyl-2-(pyridin-2-yl)-1H-benzimidazole
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0284
5,6-dimethyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0326
5,6-dimethyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0009 - 4
5-(2,3-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.03
5-(2,3-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2,3-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,3-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00275
5-(2,3-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.0359
5-(2,3-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2,3-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,3-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00053
5-(2,3-dimethylphenyl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.0264
5-(2,3-dimethylphenyl)furan-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2,3-dimethylphenyl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,3-dimethylphenyl)furan-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00338
5-(2,3-dimethylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.05
5-(2,3-dimethylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,3-dimethylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2,3-dimethylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00044
5-(2,4-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.0373
5-(2,4-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2,4-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,4-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00032
5-(2,4-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.05
5-(2,4-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,4-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2,4-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.0077
5-(2,4-dimethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.00889
5-(2,4-dimethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.0099
5-(2,4-dimethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,4-dimethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00025
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.0061
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.0071
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.0381
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.25
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Mycobacterium tuberculosis
-
above, recombinant isozyme MetAP1a in presence of different divalent metal ions, overview
0.251
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.286
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.355
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.494
5-(2,5-dichlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.00042
5-(2,5-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.0095
5-(2,5-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.0286
5-(2,5-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,5-dimethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.0046
5-(2,5-dimethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.0097
5-(2,5-dimethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2,5-dimethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,5-dimethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00118
5-(2,5-dimethylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.004
5-(2,5-dimethylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.0357
5-(2,5-dimethylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2,5-dimethylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00089
5-(2-(trifluoromethyl)phenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.05
5-(2-(trifluoromethyl)phenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2-(trifluoromethyl)phenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2-(trifluoromethyl)phenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00116
5-(2-chlorophenyl)furan-2-carbohydrazide
Escherichia coli
in the presence of 0.005 mM Mn2+
0.00578
5-(2-chlorophenyl)furan-2-carbohydrazide
Escherichia coli
in the presence of 0.01 mM Ni2+
0.00656
5-(2-chlorophenyl)furan-2-carbohydrazide
Escherichia coli
in the presence of 0.1 mM Mn2+
0.058
5-(2-chlorophenyl)furan-2-carbohydrazide
Escherichia coli
in the presence of 0.006 mM Fe2+
0.0771
5-(2-chlorophenyl)furan-2-carbohydrazide
Escherichia coli
in the presence of 0.1 mM Co2+
0.00051
5-(2-chlorophenyl)furan-2-carboxylic acid
Escherichia coli
in the presence of 0.1 mM Mn2+
0.00078
5-(2-chlorophenyl)furan-2-carboxylic acid
Escherichia coli
in the presence of 0.005 mM Mn2+
0.00092
5-(2-chlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.013
5-(2-chlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.02 - 0.25
5-(2-chlorophenyl)furan-2-carboxylic acid
Mycobacterium tuberculosis
-
recombinant isozyme MetAP1a in presence of different divalent metal ions, overview
0.116
5-(2-chlorophenyl)furan-2-carboxylic acid
Escherichia coli
in the presence of 0.006 mM Fe2+
0.138
5-(2-chlorophenyl)furan-2-carboxylic acid
Escherichia coli
in the presence of 0.1 mM Co2+
0.141
5-(2-chlorophenyl)furan-2-carboxylic acid
Escherichia coli
in the presence of 0.01 mM Ni2+
0.186
5-(2-chlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.188
5-(2-chlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.2
5-(2-chlorophenyl)furan-2-carboxylic acid
Escherichia coli
IC50 above 0.2 mM, in the presence of 0.001 mM Co2+
0.288
5-(2-chlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.358
5-(2-chlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.381
5-(2-chlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.394
5-(2-chlorophenyl)furan-2-carboxylic acid
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.00048
5-(2-ethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.0419
5-(2-ethoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.00508
5-(2-ethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.05
5-(2-ethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2-ethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2-ethoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.00055
5-(2-methoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.132
5-(2-methoxyphenyl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.00499
5-(2-methoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.0273
5-(2-methoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.0457
5-(2-methoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.0477
5-(2-methoxyphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.00151
5-(2-methylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.05
5-(2-methylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(2-methylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(2-methylphenyl)thiophene-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.0154
5-(3,4-dihydroxyphenyl)-N-isopropyl-2-methylthiazole-4-carboxamide
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.0154
5-(3,4-dihydroxyphenyl)-N-isopropyl-2-methylthiazole-4-carboxamide
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.1
5-(3,4-dihydroxyphenyl)-N-isopropyl-2-methylthiazole-4-carboxamide
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0148
5-(3,4-dihydroxyphenyl)thiophene-2-carbonitrile
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0304
5-(3,4-dihydroxyphenyl)thiophene-2-carbonitrile
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0363
5-(3,4-dihydroxyphenyl)thiophene-2-carbonitrile
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.00067
5-(4-methylnaphthalen-1-yl)furan-2-carboxylic acid
Escherichia coli
-
Mn(II)-form of the enzyme
0.05
5-(4-methylnaphthalen-1-yl)furan-2-carboxylic acid
Escherichia coli
-
Co(II)-form of the enzyme
0.05
5-(4-methylnaphthalen-1-yl)furan-2-carboxylic acid
Escherichia coli
-
Fe(II)-form of the enzyme
0.05
5-(4-methylnaphthalen-1-yl)furan-2-carboxylic acid
Escherichia coli
-
Ni(II)-form of the enzyme
0.0052
5-chloro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.028
5-chloro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.047
5-chloro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0017
5-chloro-2-(pyridin-2-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0181
5-chloro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0488
5-chloro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0004
5-chloro-4-methyl-2-pyridin-2-yl-6-pyrrolidin-1-ylpyrimidine
Homo sapiens
MetAP1
0.0008
5-chloro-4-methyl-2-pyridin-2-yl-6-pyrrolidin-1-ylpyrimidine
Homo sapiens
MetAP2
0.0006
5-chloro-6-methyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
Homo sapiens
MetAP1
0.0076
5-chloro-6-methyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
Homo sapiens
MetAP2
0.0033
5-chloro-N,6-dimethyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
Homo sapiens
MetAP1
0.0033
5-chloro-N,6-dimethyl-N-(2-phenylethyl)-2-pyridin-2-ylpyrimidin-4-amine
Homo sapiens
MetAP2
0.0043
5-fluoro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0384
5-fluoro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0458
5-fluoro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0015
5-fluoro-2-(pyridin-2-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0149
5-fluoro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0347
5-fluoro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0401
5-fluoro-2-(pyridin-2-yl)-1H-benzimidazole
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0072
5-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0355
5-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0406
5-methyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0021
5-methyl-2-(pyridin-2-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0077
5-methyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0194
5-methyl-2-(pyridin-2-yl)-1H-benzimidazole
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0326
5-methyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0012
5-nitro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0485
5-nitro-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00016
5-nitro-2-(pyridin-2-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0288
5-nitro-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0039
5-tert-butyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0417
5-tert-butyl-2-(1,3-thiazol-4-yl)-1H-benzimidazole
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0026
5-tert-butyl-2-(pyridin-2-yl)-1H-benzimidazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0389
5-tert-butyl-2-(pyridin-2-yl)-1H-benzimidazole
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0441
5-tert-butyl-2-(pyridin-2-yl)-1H-benzimidazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00024
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Mycobacterium tuberculosis
pH 7.5, 37°C, with Ni2+
0.00026
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Mycobacterium tuberculosis
pH 7.5, 37°C, with Co2+
0.00038
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.0004
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.00078
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.002
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Mycobacterium tuberculosis
pH 7.5, 37°C, with Mn2+
0.0049
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.014
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.064
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.094
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.128
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.0025 mM Fe2+, pH not specified in the publication, temperature not specified in the publication
0.205 - 0.25
5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Mycobacterium tuberculosis
-
and above, recombinant isozyme MetAP1a in presence of different divalent metal ions, overview
0.00064
5-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.00088
5-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.0013
5-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Mycobacterium tuberculosis
pH 7.5, 37°C, with Ni2+
0.0022
5-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.0025
5-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Mycobacterium tuberculosis
pH 7.5, 37°C, with Ni2+
0.023
5-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.034
5-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.25
5-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Mycobacterium tuberculosis
-
above, recombinant isozyme MetAP1a in presence of different divalent metal ions, overview
0.303
5-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.0021
5-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.0038
5-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Co2+, pH not specified in the publication, temperature not specified in the publication
0.0044
5-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.044
5-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.005 mM Ni2+, pH not specified in the publication, temperature not specified in the publication
0.103
5-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.145
5-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Acinetobacter baumannii
after removal of divalent metal ions activated with 0.02 mM Mn2+, pH not specified in the publication, temperature not specified in the publication
0.25
5-[(4-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine
Mycobacterium tuberculosis
-
above, recombinant isozyme MetAP1a in presence of different divalent metal ions, overview
0.0013
6-(1H-benzimidazol-2-yl)pyridin-2(1H)-one
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0292
6-(1H-benzimidazol-2-yl)pyridin-2(1H)-one
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.00038
8-(pyridin-2-yl)-7H-purine
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0339
8-(pyridin-2-yl)-7H-purine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0364
8-(pyridin-2-yl)-7H-purine
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00077
8-hydroxy quinoline
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0056
8-hydroxy quinoline
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0183
8-hydroxy quinoline
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0215
8-hydroxy quinoline
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0111
cyclopropyl 5-(3,4-dihydroxyphenyl)-2-methyl-1,3-thiazole-4-carboxylate
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0923
cyclopropyl 5-(3,4-dihydroxyphenyl)-2-methyl-1,3-thiazole-4-carboxylate
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.1
cyclopropyl 5-(3,4-dihydroxyphenyl)-2-methyl-1,3-thiazole-4-carboxylate
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.00064
imidazo[2,1-a]isoquinoline-2-carbohydrazide
Escherichia coli
in the presence of 0.005 mM Mn2+
0.00244
imidazo[2,1-a]isoquinoline-2-carbohydrazide
Escherichia coli
in the presence of 0.001 mM Co2+
0.00431
imidazo[2,1-a]isoquinoline-2-carbohydrazide
Escherichia coli
in the presence of 0.1 mM Mn2+
0.00615
imidazo[2,1-a]isoquinoline-2-carbohydrazide
Escherichia coli
in the presence of 0.01 mM Ni2+
0.0174
imidazo[2,1-a]isoquinoline-2-carbohydrazide
Escherichia coli
in the presence of 0.006 mM Fe2+
0.0278
imidazo[2,1-a]isoquinoline-2-carbohydrazide
Escherichia coli
in the presence of 0.1 mM Co2+
0.00054
N-(1,3-thiazol-2-yl)-1H-benzimidazol-2-amine
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0224
N-(1,3-thiazol-2-yl)-1H-benzimidazol-2-amine
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.00006
N-(1,3-thiazol-2-yl)pyridine-2-carboxamide
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0081
N-(1,3-thiazol-2-yl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0212
N-(1,3-thiazol-2-yl)pyridine-2-carboxamide
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0258
N-(1,3-thiazol-2-yl)pyridine-2-carboxamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.011
N-(quinolin-8-yl)benzenesulfonamide
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0229
N-(quinolin-8-yl)benzenesulfonamide
Staphylococcus aureus
-
pH not specified in the publication, temperature not specified in the publication
0.0398
N-(quinolin-8-yl)benzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0449
N-(quinolin-8-yl)benzenesulfonamide
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.03
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
Escherichia coli
pH not specified in the publication, temperature not specified in the publication
0.046
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
Streptococcus pneumoniae
-
pH not specified in the publication, temperature not specified in the publication
0.06
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
Haemophilus influenzae
-
pH not specified in the publication, temperature not specified in the publication
0.2
N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
Staphylococcus aureus
-
value above 0.2 mM, pH not specified in the publication, temperature not specified in the publication
0.001
N-but-3-en-1-yl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.0067
N-but-3-en-1-yl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Mn2+-activated MetAP enzyme
0.0212
N-but-3-en-1-yl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Co2+-activated MetAP enzyme
0.0012
N-cyclobutyl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.0079
N-cyclobutyl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Mn2+-activated MetAP enzyme
0.0225
N-cyclobutyl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Co2+-activated MetAP enzyme
0.0009
N-cyclopentyl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Fe2+-activated MetAP enzyme
0.0118
N-cyclopentyl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Mn2+-activated MetAP enzyme
0.0301
N-cyclopentyl-5-(3,4-dihydroxyphenyl)furan-2-carboxamide
Escherichia coli
-
using Co2+-activated MetAP enzyme
0.0078
N-cyclopropyl-2-(3,4-dihydroxyphenyl)thiophene-3-carboxamide
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.1
N-cyclopropyl-2-(3,4-dihydroxyphenyl)thiophene-3-carboxamide
Escherichia coli
IC50 above 0.1 mM, Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.1
N-cyclopropyl-2-(3,4-dihydroxyphenyl)thiophene-3-carboxamide
Escherichia coli
IC50 above 0.1 mM, Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0238
N-cyclopropyl-5-(3,4-dihydroxyphenyl)thiophene-2-carboxamide
Escherichia coli
Fe2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.05 mM FeCl2 with 0.1 mM ascorbic acid
0.0285
N-cyclopropyl-5-(3,4-dihydroxyphenyl)thiophene-2-carboxamide
Escherichia coli
Co2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.01 mM CoCl2
0.034
N-cyclopropyl-5-(3,4-dihydroxyphenyl)thiophene-2-carboxamide
Escherichia coli
Mn2+-loaded wild type enzyme, in 50 mM MOPS (pH 7.0), 0.02 mM MnCl2
0.0024
phenyl[2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-yl]methanone
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.041
phenyl[2-(1,3-thiazol-4-yl)-1H-benzimidazol-5-yl]methanone
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0013
Pyridine-2-carboxylic acid thiazol-2-ylamide
Escherichia coli
-
IC50 for Co-EcMetAP1: 0.0013 mM
0.0412
quinolin-8-yl benzenesulfonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0417
quinolin-8-yl benzenesulfonate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0348
quinolin-8-yl benzoate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0428
quinolin-8-yl benzoate
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00047
thiabendazole
Escherichia coli
-
pH not specified in the publication, temperature not specified in the publication
0.0447
thiabendazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.0478
thiabendazole
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
0.00105
TNP-470
Homo sapiens
-
pH not specified in the publication, temperature not specified in the publication
additional information
additional information
Escherichia coli
-
IC50 values for N-(quinolin-8-yl)methanesulfonamide with different metal ions, overview
-
additional information
additional information
Escherichia coli
-
inhibitor screening, assay method development, and assay validation, overview
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.3
-
substrate L-Nle-L-Ala-L-Ser, N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
100
-
substrate L-Met-L-Ala-L-Ser, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
12.1
-
substrate L-Thr-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
141
-
substrate L-Nle-L-Ala-L-Ser, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
146
-
substrate L-Met-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
18.4
-
substrate L-Met-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
201
-
substrate L-Met-L-Ala-L-Ser-L-Trp, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
22
-
substrate L-Phe-L-Ala-L-Ser-L-Trp, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
23
-
substrate L-Leu-L-Ala-L-Ser-L-Trp, N-terminally truncated mutant, lacking 66 amino acids, pH 7.0, 22°C
30
8.8
-
substrate L-Thr-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
9.4
-
substrate L-Ala-PSI[C(O)S]Gly-L-Phe, N-terminally truncated mutant lacking 135 amino acids, pH 7.0, 22°C
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
-
octapeptide substrate related to the amino-terminal portion of the beta-chain of human hemoglobin with either valine or alanine in the penultimate position
6.5
7.5
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 8
6.5 - 9.3
-
pH 6.5: about 35% of maximal activity, pH 9.3: about 75% of maximal activity
6.5 - 8
pH 6.5: about 30% of maximal activity, pH 8.0: about 25% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
-
optimum temperature for MetAP activity against the substrate L-Met p-nitroanilide
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
-
20°C: about 60% of activity maximum, 50°C: about 70% of activity maximum
50 - 100
-
50°C: about 45% of maximal activity, 100: about 20% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PCC6803, three isozymes encoded by lr0786 or map-1, slr0918 or map-2, and sll0555 or map-3
-
-
brenda
isoform YpdF, showing Xaa-Pro aminopeptidase activity and limited methionine aminopeptidase activity
-
-
brenda
strains H37Ra and H37Rv, two isozymes MtMetAP1a and MtMetAP1c encoded by genes Rv0734 and Rv2861c
-
-
brenda
synthetic construct for expression in Escherichia coli
KT943909
GenBank
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cell line derived from a patient with high-risk neuroblastoma
brenda
-
expression of isozymes MetAP1a, MetAP1b, and MetAP2, and of isozyme MetAP1c in the late trophozoite
brenda
additional information
-
colon cancer cell line, expression of enzyme is inversely correlated to cell density
brenda
additional information
-
the two MetAP isozymes, MtMetAP1a and MtMetAP1c, are expressed at different levels in growing and stationary phases
brenda
additional information
-
Plasmodium falciparum life cycle overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
translocated from the nucleus to the cytoplasm in response to low-temperature (observed in onion cells which transiently express a GFP fusion protein)
brenda
-
methionine aminopeptidase type 1 associates primarily with the 60S ribosome subunit, lower affinity or non-specific interaction with the 40S ribosome subunit
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
blockade of the isozymes can is lethal to cell proliferation
physiological function
physiological function
-
MetAP functions in the catalytic removal of N-terminal initiator methionine residues from proteins during sythesis, which is essential for the correct folding and trafficking of proteins
physiological function
-
MetAP is a ubiquitous enzyme required for cell survival and an attractive target for antibacterial and anticancer drug development. MetAP is involved in protein maturation by catalyzing the hydrolytic excision of the N-terminal methionine from nascent proteins
physiological function
-
MetAP is essential for bacterial survival
physiological function
-
MetAP plays a critical role in protein maturation by catalyzing the removal of the N-terminal initiator methionine from nascent proteins
physiological function
-
MetAP2 is a bifunctional protein that plays a critical role in the regulation of post-translational processing and protein synthesis
physiological function
-
methionine aminopeptidase plays an essential role for cell survival
physiological function
stronger freezing tolerance (transgenic Arabidopsis plants)
physiological function
inhibition of the enzymatic activity of isoform MetAP2 inhibitor fumagillin or siRNA mediated down-regulation of the protein level of MetAP2 both lead to strong signals of unprocessed 14-3-3gamma protein with intact initiator methionine in the immunoblot
physiological function
isoform mapA is dispensable for growth of bacteria. Double-deletion mutants of isoforms MapA and MapB as well as the introduction of point mutations into mapB show partial, but not full, redundancy between MapB and MapA
physiological function
isoform mapB is indispensable for growth of bacteria. Double-deletion mutants of isoforms MapA and MapB as well as the introduction of point mutations into mapB show partial, but not full, redundancy between MapB and MapA
physiological function
MAP2 is involved in the regulation of programmed cell death in the parasite
physiological function
N-terminally acetylated terminal Met residues followed by a small residue cannot be removed by MetAPs. Yeast Naa50-mediated N-terminal acetylation may act to retain the N-terminal Met residue of proteins otherwise susceptible to MetAP
physiological function
recombinant enzyme is immunogenic, eliciting a high antibody titer in mice. Recombinant MetAP1 stimulates the production of IFN-gamma and IL-12 but not IL-4 in the host
physiological function
-
MAP2 is involved in the regulation of programmed cell death in the parasite
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28812
-
x * 28812, isozyme MetAP1a, mass spectrometry, x * 32516, isozyme MetAP1c, mass spectrometry
29140
-
sedimentation equilibrium measurement
29290
-
calculation from nucleotide sequence
29333
-
1 * 29333, calculation from nucleotide sequence, gel filtration data
29630
32000
-
the calculated molecular weight from nucleotide-derived amino acid sequence is about 32000 Da
32516
-
x * 28812, isozyme MetAP1a, mass spectrometry, x * 32516, isozyme MetAP1c, mass spectrometry
34000
37000
41000
72000
-
MetAP2 overexpressed in Escherichia coli has an apparent molecular weight of 72000Da
90000
-
MetAP2 overexpressed in Saccharomyces cerevisiae is approximately 90000 Da
additional information
additional information
-
sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold
additional information
-
two-cobalt-dependent MetAP families, presently composed of the prokaryote and yeast sequence (and represented by the Escherichia coli structure) (type I), and by human MetAP, the yeast open reading frame, and the partial prokaryotic sequence (type II)
additional information
-
two-cobalt-dependent MetAP families, presently composed of the prokaryote and yeast sequence (and represented by the Escherichia coli structure) (type I), and by human MetAP, the yeast open reading frame, and the partial prokaryotic sequence (type II)
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 40867, calculated from sequence, x * 66800, recombinant GST fusion protein
?
-
x * 28812, isozyme MetAP1a, mass spectrometry, x * 32516, isozyme MetAP1c, mass spectrometry
monomer
-
1 * 29333, calculation from nucleotide sequence, gel filtration data
monomer
1 * 31000, about, recombinant detagged enzyme, sequence calculation and gel filtration
monomer
-
1 * 31000, about, recombinant detagged enzyme, sequence calculation and gel filtration
-
additional information
-
sequence comparisons, e.g. with the human enzyme structure, PDB ID 1YW9, overview
additional information
EbMetAP2 structure analysis by homology modelling using the structure of EcMetAP2 from Enterocytozoon cuniculi
additional information
-
EbMetAP2 structure analysis by homology modelling using the structure of EcMetAP2 from Enterocytozoon cuniculi
additional information
-
EbMetAP2 structure analysis by homology modelling using the structure of EcMetAP2 from Enterocytozoon cuniculi
-
additional information
-
N-terminal region contains 3 distinct PxxP motifs that may participate in binding to the ribosome
additional information
enzyme interacts with the ribosome by a complex between a PxxP motif on the protein and an SH3 domain on the ribosome, crystallization data
additional information
-
enzyme interacts with the ribosome by a complex between a PxxP motif on the protein and an SH3 domain on the ribosome, crystallization data
additional information
-
differing active site structures of isozymes MetAP1a and MetAP1c
additional information
-
enzyme interacts with the ribosome by a complex between a PxxP motif on the protein and an SH3 domain on the ribosome, crystallization data
-
additional information
-
type 2 MetAPs contain a 60 amino acid insertion near the catalytic domain, while MetAP1s do not
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
isoform MetAP2 is post-translationally regulated by an allosteric disulfide bond, which controls substrate specificity and catalytic efficiency. Isoform MetAP2 contains a single Cys228-Cys448 disulfide bond that has an -RH-staple configuration and links two beta-loop structures, which are hallmarks of allosteric disulfide bonds. The disulfide bond exists in oxidized and reduced states in the recombinant enzyme. The disulfide has a standard redox potential of -261 mV and is efficiently reduced by the protein reductant, thioredoxin, with a rate constant of 16180 per M and s. The MetAP2 disulfide bond also exists in oxidized and reduced states in glioblastoma tumor cells, and stressing the cells by oxygen or glucose deprivation results in more oxidized enzyme. Oxidized and reduced isoforms have different catalytic efficiencies for hydrolysis of MetAP2 peptide substrates
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant MetAP2 with and without the bound inhibitors fumagillin and TNP-470, sitting drop vapor diffusion at 20°C, mixing of 2 mg/ml protein, in 10 mM HEPES, 150 mM NaCl, 10% glycerol, 5 mM DTT, pH 7.5, with 30% w/v PEG 4000, 0.2 M ammonium sulfate, for inhibitor bound enzyme crystals co-cyrstallization with 0.5 mM inhibitor in 27% PEG 4000, 0.2 M ammonium sulfate, ten days, X-ray diffraction structure determination and analysis at 2.18-2.89 A resolution, molecular replacement
-
apo-form of enzyme and modeling of inhibitor 2,2'-bipyridine. One of the rings of 2,2'-bipyridine that points into the S1 pocket is surrounded by residues Tyr60, Tyr63, Trp218, and Cys68, while the other ring points towards the surface of the protein that does not make any contact with the protein, except with the metal ion
-
hanging drop vapour diffusion method with 13-18% PEG 20000, 0.1M Mes (pH 6.5), and 2 mM MnCl2 or 1.2 mM CoCl2
hanging drop vapour diffusion method, in complex with inhibitors, with 10-15% PEG 20000, 0.1 M MES (pH 6.5) and 0.2 mM MnCl2
in complex with inhibitor 4-(3-ethylthiophen-2-yl)benzene-1,2-diol, hanging drop vapour diffusion method, using 100 mM MES, pH 6.5, 2 mM MnCl2, and 17% PEG 20000
in complex with inhibitor N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide
in complex with inhibitor, hanging drop vapour diffusion method with 10-15% PEG 20 000, 0.1 M MES (pH 6.5) and 0.2 mM or 0.8 mM MnCl2
in complex with inhibitors, hanging drop vapour diffusion method, with 10-15% PEG20000, 0.1 M MES pH 6.5 and 2 mM MnCl2, or 33% PEG 3350, 0.1 M Bis-Tris pH 6.5, 0.2 M NH4OAc and 1.2 mM CoCl2
Mn(II)-form of enzyme, in complex with inhibitor 5-(2-chlorophenyl)-2-furoic acid
-
mono- and dimetalated enzyme in complex with transition state analog norleucine phosphonate
1.8 resolution crystal structure of free enzyme and enzyme complexed with fumagillin. Crystals are grown in 1 to 2 weeks at 4°C from sitting drops, with a protein concentration of 12 mg/ml
complexed with inhibitor, sitting drop vapour diffusion method with 15-20% tert-butyl alcohol containing 0.4-0.1 M aqueous sodium citrate at pH 5.5
crystal structure of N-terminally truncated MetAP1 in complex with inhibitor 4-[4-(4-methoxyphenyl)piperazin-1-yl]-2-(pyridin-2-yl)quinazoline and Co(II)
in complex with inhibitor 5-((R)-1-[1,2,4]triazolo[1,5-a]pyrimidin-7-yl-pyrrolidin-2-ylmethoxy)-isoquinoline. The His339 side-chain imidazole ring is coplanar sandwiched between the imidazole of His331 and the aryl-ether moiety of the inhibitor
MetAP1 in complex with ovalicin, hanging drop vapour diffusion method, with 4%-6% PEG 10000 or 12%-16% PEG monomethyl ether 2000, in 100 mM HEPES at pH 5.4-6.2
N-terminally truncated isoform AP1 in complex with inhibitor 5-chloro-2-(5-chloropyridin-2-yl)-6-methyl-N-((R)-2-phenyl-2-(4-phenylbutylamino)ethyl)pyrimidin-4-amine. Both pyridine nitrogen N1 and pyrimidine nitrogen N1 are bound to Co3, displaying a near-perfect octahedral coordination which is completed by the nitrogen atom from the side chain of His212 and three water molecules
sitting drop vapour diffusion method, in complex with L-methionine and D-methionine at 1.9 and 2.0 A resolution, respectively
presence of a unique C-H to S hydrogen bond between the enzyme and its N-terminal-methionine polypeptide substrate, which allows specific interaction between apparent apolar interfaces, imposing a strict substrate recognition specificity and efficient catalysis
purified recombinant isozyme MetAP1c in complex with inhibitors 3-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazole and 5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine, hanging drop vapor diffusion method at room temperature, mxing of 10 mg/ml protein with 2 mM metal in 50 mM Tris, pH 8.0, and 150 mM NaCl, and inhibitor in a molar ratio of 5:1 or 10:1 of inhibitor to enzyme, with an equal volume of reservoir solution containing 100 mM Bis-Tris, pH 5.5, 1.4 M NH4SO4, and 15% glycerol for 3-[(4-fluorobenzyl)sulfanyl]-4H-1,2,4-triazole, and 100 mM Bis-Tris, pH 5.5, 1.3 M NH4SO4, and 15% glycerol for 5-[(2,4-dichlorobenzyl)sulfanyl]-4H-1,2,4-triazol-3-amine, X-ray diffraction structure determination and analysis at 1.4-1.88 A resolution, molecular replacement
wild-type enzyme crystals are soaked with N-ethylmaleimide, 2-hydroxyethyl disulfide, and methyl homocysteine disulfide. Crystal structure determined in the presence of cobalt chloride shows electron density for the mercaptoethanol covalently linked to Cys105. However, in the absence of cobalt chloride, the whole 2-hydroxyethyl disulfide molecule is observed in the S1 pocket without any covalent modification. Metal ions in the active site assist in the covalent modification of Cys105 by orienting the reagents appropriately for a successful reaction
electronic absorption spectrum in the absence and presence of both nitric oxide and the substrate-analog butaneboronic acid. Both bind to the catalytic Fe(II)-center of enzyme forming a complex that mimics an intermediate step between the Michaelis complex and the tetrahedral transition-state
-
sitting-drop variant of the vapor-diffusion method at room temperature, crystallization of monoclinic crystals and the transformation of original crystals to low-humidity form which is accompanied by a significant extension of resolution, in particular, from 3.2 to 1.75 A
structure is determined by the multiple isomorphous replacement method and refined in three different crystal forms, one monoclinic and two hexagonal, at resolutions of 2.8, 2.9 and 3.5 A. Crystals are grown by the sitting-drop variant of the vapor-diffusion method
-
crystal structure of MetAP-1 as an apoenzyme and its complexes with various 1,2,4-triazole-based derivatives at high-resolution. Form 1 crystals are grown in the presence of 0.1 mM NiCl2 with 25% PEG 3350, 100 mM bis-Tris, pH 6.5, 200 mM LiSO4. Form 2 crystals are grown in the absence of metal ions using 25% PEG, 100 mM bis-Tris, pH 5.5, 200 mM ammonium acetate as precipitating agent
-
in complex with inhibitors 2-amino-4-(methylthio)-1-(1,3-thiazol-2-yl)butan-1-one, 2-amino-4-(methylthio)-1-pyridin-2-ylbutan-1-one, and 3-amino-1-(cyclopropylamino)heptan-2
molecular docking of inhibitor N-2-[(3,5-difluorophenyl)acetyl]-N-[(3S,7R)-1-methyl-2-oxo-7-phenyl-2,3,4,7-tetrahydro-1H-azepin-3-yl]-L-alaninamide and comparison with docking in Escherichia coli structure
-
contains two molecules in the asymmetric unit and well ordered inserts with structural features that corroborate the possible posttranslational modification. Both the new inserts present structurally align with the P-X-X-P motif found in other type I Metionine aminopeptidases as well as the 60 amino acid insert in the human type II. In addition, one of the beta-hairpins within in the catalytic domain undergoes a flip placing a residue which is essential for enzyme activity away from the active site and the beta-hairpin loop of this secondary structure in the active site obstructing substrate binding
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C70A
hydrolysis of Met-Ala-Ser similar to wild-type, relaxed specificity
C70S
D108A
-
2% of the activity compared to the wild-type enzyme, cobalt content is 6% of that of the wild-type enzyme
D97A
D97E
the mutation causes an about 9000fold decrease in kcat and a 2000fold decreased catalytic efficiency (kcat/Km) for the Co(II)-loaded enzyme towards L-Met-Gly-L-Met-L-Met as compared to the wild type enzyme
D97N
the mutation causes an about 9000fold decrease in kcat and a 3000fold decreased catalytic efficiency (kcat/Km) for the Co(II)-loaded enzyme towards L-Met-Gly-L-Met-L-Met as compared to the wild type enzyme
E204V
-
5% of the activity compared to the wild-type enzyme, cobalt content is not detectable
E235V
-
3% of the activity compared to the wild-type enzyme, cobalt content is 3% of that of the wild-type enzyme
H171L
-
6% of the activity compared to the wild-type enzyme, cobalt content is 6% of that of the wild-type enzyme
H178A
-
the mutant enzyme binds only one equivalent of Co(II) or Fe(II) tightly with affinities that are identical to the wild-type. The turnover-number for Co(II) loaded H178A decreases 70fold towards Met-Gly-Met-Met ans 290fold towards Met-Pro-p-nitroanilide. The KM-value for Met-Gly-Met-Met remains unaffected, while that for Met-Pro-p-nitroanilide increases approximately 2fold for Co(II) - and Fe(II)-loaded H178A. The ratio of turnover-number to Km-value for both Co(II)- and Fe(II)-loaded H178A towards both substrates ranges from 50fold to 580fold reduction
H63A
-
the mutation does not affect the ability of the enzyme to bind divalent metal ions but affects the hydrolysis of small peptide substrates whereas large peptides can overcome the observed loss in binding energy by additional hydrophilic and hydrophobic interactions
H79A
Y168A
-
increase in initiator methionine removal with valine in penultimate position of substrate
A362T
-
type II enzyme, mutation results in resistance to ovalicin, TNP-470 and fumagillin when expressed in yeast
C202A
-
hydrolysis of Met-PSI[C(O)S]Gly-Phe similar to wild-type, relaxed specificity
H382Y
T334A
-
type I enzyme, mutation renders the resistant wild-type enzyme sensitive to ovalicin
Y444C
C105S
C105V
6fold decrease in kcat/Km value compared to wild-type
DELTA 2-10
-
30% activity with 10fold amount of enzyme in the assay relative to wild type
DELTA 2-15
-
30% activity with 10fold amount of enzyme in the assay relative to wild type
C105S
C105T
-
4old decrease in kcat/Km value compared to wild-type
-
C105V
-
6fold decrease in kcat/Km value compared to wild-type
-
B255L
no substantial growth defect in comparison to the growth of control strains
V18G
no substantial growth defect in comparison to the growth of control strains
V18G/W55L
mutant has traces of enzymatic activity, and has no substantial growth defect in comparison to the growth of control strains. When isof0orm MapA is present, the 8% activity of MapB mutant V18G/W255L is sufficient for viability and normal growth, whereas bacteria without MapA can retrieve no viable colonies
C22S
C27S
-
the activity with Met-Gly-Met-Met is 107% of that of the wild-type enzyme
C37S
-
the activity with Met-Gly-Met-Met is 94% of that of the wild-type enzyme
C40S
-
the activity with Met-Gly-Met-Met is 85% of that of the wild-type enzyme
C50S
-
the activity with Met-Gly-Met-Met is 99% of that of the wild-type enzyme
C54S
-
the activity with Met-Gly-Met-Met is 97% of that of the wild-type enzyme
D219N
-
the mutant enzyme has 1000fold lower activity and a different substrate specificity when compared to wild-type enzyme. Expression of the mutant enzyme in yeast causes a slow-growth phenotype and interferes with wild-type metAP1 in a dominant manner. The mutant enzyme contains 0.43 mol of Co2+ per mol. The wild-type enzyme contains 0.75 mol of Co2+ per mol of enzyme. The mutant enzyme prefers substrates, having Ser or Pro at P1', over substrates that contain glycine and alanine at that position. The wild-type enzyme prefers substrates that have Ala, Gly, Ser or Pro at P1'
DELTA2-69
H174A
-
no enzymic activity, overexpression using a strong promoter in map1 null strain is lethal, overexpression using a weak promoter slightly inhibits growth
H62R
H66R
-
the activity with Met-Gly-Met-Met is 84% of that of the wild-type enzyme
M329A
-
mutation produces an avarage catalytic efficiency 1.5fold higher than the native enzyme on normal substrates and cleaves substrates containing penultimate Asn, Gln, Ile, Leu, Met and Phe
additional information
D97A
-
4% of the activity compared to the wild-type enzyme, cobalt content is not detectable
D97A
the mutation causes an about 9000fold decrease in kcat and a 6100fold decreased catalytic efficiency (kcat/Km) for the Co(II)-loaded enzyme towards L-Met-Gly-L-Met-L-Met as compared to the wild type enzyme, the mutation effectively removes the ability of the enzyme to form a dinuclear site, providing a MetAP enzyme that retains catalytic activity, albeit at extremely low levels
H79A
-
Co2+-loaded H79A exhibits an overall of more than 7000fold decrease in specific activity, the almost complete loss of activity is primarily due to a more than 6000fold decrease in kcat, the Km value obtained for Co2+-loaded H79A is approximately half the value observed for wild type MetAP-I, specific activity of Mn2+-loaded H79A decreases by about 2.6fold while kcat decreases by about 3.5fold, the observed Km value for Mn2+ loaded H79A is about 1.4fold larger than that observed for wild type enzyme
H382Y
-
type II enzyme, mutation results in resistance to ovalicin, TNP-470 and fumagillin when expressed in yeast
H382Y
-
the single site mutation in the S1 subsite of human MetAP2b results in inhibitor resistance
Y444C
-
type II enzyme, mutation results in resistance to TNP-470, but not to fumagillin when expressed in yeast
Y444C
-
the single site mutation in the S1 subsite of human MetAP2b results in inhibitor resistance
C105S
contratry to wild-type, no inhibition by cysteien-modifying compounds N-ethylmaleimide, 5,5'-dithiobis(2-nitrobenzoic acid) and 2-hydroxyethyl disulfide
C105S
10fold decrease in kcat/Km value compared to wild-type
C105S
-
contratry to wild-type, no inhibition by cysteien-modifying compounds N-ethylmaleimide, 5,5'-dithiobis(2-nitrobenzoic acid) and 2-hydroxyethyl disulfide
-
C105S
-
10fold decrease in kcat/Km value compared to wild-type
-
C22S
-
zinc finger point mutant, processing efficiency of the mutant enzyme is less than that of the wild-type enzyme in vivo. Association of the mutant enzyme with the 60S ribosome subunit is disrupted
C22S
-
the activity with Met-Gly-Met-Met is 116% of that of the wild-type enzyme
DELTA2-69
-
zinc-finger deletion mutant, processing efficiency of the mutant enzyme is less than that of the wild-type enzyme in vivo
DELTA2-69
-
1 mol of wild-type enzyme contains 2 mol of zinc ions and at least 1 mol of cobalt ion, whereas 1 mol of the truncated methionine aminopeptidase DELTA2-69 lacking the putative zinc fingers cotains only a trace amount of zinc ions but still contains one mole of cobalt ion,the activity with Met-Gly-Met-Met is 84% of that of the wild-type enzyme
H62R
-
zinc finger point mutant, processing efficiency of the mutant enzyme is less than that of the wild-type enzyme in vivo. Association of the mutant enzyme with the 60S ribosome subunit is disrupted
H62R
-
the activity with Met-Gly-Met-Met is 95% of that of the wild-type enzyme
additional information
-
the 107 N-terminal residues of MetAP2 are not required for either the peptidolytic activity of the enzyme or its stability. The N-terminally truncated enzyme and the full-length enzyme yield essentially identical kinetic behavior and physical properties
additional information
-
truncated MetAP1 lacking N-terminal 89 amino acids, 2.5fold increase in KM-value
additional information
-
truncated mutant lacking N-terminal 66 amino acids, 2.5fold increase in kcat value. Truncated mutant lacking N-terminal 135 amino acids, 4fold increase in KM-value
additional information
-
enzyme deletion mutant, N-terminal region (residues 2-57) is essential but not sufficient for enzyme to fully interfere with map1 null growth
additional information
-
the map-2 deficient mutant is severely impaired in surviving conditions of prolonged nitrogen starvation and high light exposure
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50 - 65
-
the enzyme is stable at 50 °C with half-life of more than 8 h, at 50°C and 55°C, the enzyme shows stable activity over a period of 1 h with only a slight decrease of 10% in activity, at 60 °C the relative activity decreases to 50% within 50 min, whereas at 65°C the relative activity decreases to 19% and declines to 0 after a period of 50 min
55
-
10 min, inactivation of isozyme MetAP1c, while isozyme MetAP1a retains 50% activity
additional information
50
-
85% activity after 10 min at 50°C, Tm: 53,6°C (determination by CD spectroscopy)
additional information
3.3 degrees C increase in melting temperature for methionine bound protein compared to its norleucine homolog
additional information
-
3.3 degrees C increase in melting temperature for methionine bound protein compared to its norleucine homolog
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
recombinant full-lenth enzyme is not stable during purification and storage at 4°C, and a smaller but active protein appears that corresponds to N-terminally truncated protein lacking amino acids 1-66
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, DEAE Toyopearl column chromatography, and Q Sepharose Fast Flow column chromatography
ammonium sulfate precipitation, Q-Sepharose column chromatography, and Sephadex G-100 gel filtration
-
ammonium sulfate precipitation, Superose-6 column chromatography, and Q-Sepharose column chromatography
-
immobilized metal ion affinity chromatography (Ni2+)
ion exchange chromatography (Q-Sepharose), hydrophobic interaction chromatography (Phenyl Sepharose), gel filtration (Sephacryl S-200)
-
Mono Q column chromatography and Q-Sepharose column chromatography
recombinant His-tagged isozymes from Escherichia coli by nickel affinity chromatography and gel filtration
-
recombinant His-tagged isozymes from Escherichia coli, the tag is cleaved off by thrombin
-
recombinant peptidase M is also purified from Escherichia coli
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
adenoviral transfer of c-Myc increaseds the expression of MetAP2 in human umbilical vein endothelial cells and reveals that cellular proliferation may involve a cross-talk between c-Myc and MetAP2
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain BL21, Saccharomyces cerevisiae strain INVSc1, and insect cells, none of the recombinant forms of MetAP2 exhibits enzymatic activity
-
expressed in Saccharomyces cerevisiae strain S228C (ATCC 201388)
expression in Escherichia coli
expression in Escherichia coli BL21 cells, Pichia pastoris and Saccharomyces cerevisiae, glutathione S-transferase-Met AP I fusion protein
-
gene mapB or Rv2861c, recombinant expression of isozyme MetAP1c in enzyme-deficient Escherichia coli cells. Plasmid-expressed MtMetAP1c complements the essential function of MetAP in Escherichia coli and supports the cell growth
genes map-1, map-2, and map-3, encoding three isozymes, DNA and amino acid sequence determination and analysis, expression as His-tagged enzymes in Escherichia coli
-
genes Rv0734 and Rv2861c, expression of the His-tagged isozymes in Escherichia coli
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glutathione-S-transferase fusion protein expressed in Escherichia coli BL21(DE3), expressed in Arabidopsis
His-tagged protein expressed in Escherichia coli BL21(DE3)
isozymes MetAP1a, MetAP1b, MetAP1c, and MetAP2 are encoded on chromosomes 5, 10, 8, and 14
-
mutant enzymes are expressed in Escherichia coli BL21 Star(DE3) cells
expressed in Saccharomyces cerevisiae strain S228C (ATCC 201388)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the 3,5-bis(benzylidene)-4-piperidone derivative 2-(3-[3,5-bis[4-nitrobenzylidene]-4-oxopiperidin-1-yl]-3-oxopropylsulfanyl) ethanesulfonic acid, or NC2213, downregulates the enzyme in HT-29 cells
-
ubiquitous at 6 hours postfertilization, predominantly in eye, brain and intersomitic regions at 2 hours postfertilization, also in developing heart at 30 hours postfertilization
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
synthesis
drug development
-
MetAP is a promising target for developing broad spectrum antibacterial agents
drug development
-
the isoyzmes are targets for the development of antimalarial drugs, and ienzyme inhibitors may be useful as anticancer compounds
drug development
-
the MetAP isozymes are potential targets to develop antitubercular therapeutics
medicine
-
MetAP2 is a molecular target for antiangiogenesis and anticancer therapy
medicine
-
the modification of the active site residue His79 by the inhibitors fumagillin and ovalicin may prevent the action of the enzyme on proteins or peptides involved in angiogenesis. These compounds may be effective pharmacological agents against pathogenic and resistant forms of Escherichia coli and other microorganisms
medicine
-
enzyme expression is increased in 8 out of 12 tumor samples. Reduction of enzyme level by MAP1D shRNa does not result in any difference of proliferation, cell survival, or cell numbers, but cells exhibit a dramatically reduced potential to form colonies in soft agar
medicine
-
enzyme inhibitor PPI-2458 inhibits proliferation of human fibroblast-like synviocytes derived from patients with rheumatoid arthritis with a growth inhibitory concentration of 0.04 nM. Growth inhibition is linked to enzyme inhibition
medicine
-
enzyme MetAP2 activity is elevated in all human colorectal adenocarcinomas examined compared with normal tissue. Immunohistochemistry shows moderate to strong cytoplasmic positivity for enzyme with increased intensity in the invasive tumor component
medicine
-
in colon cancer cell line HT-29, expression of enzyme is inversely correlated to cell density
medicine
-
inhibitor A357300 in combination with cyclophosphamide sustains tumor regression and inhibits establishment and growth rate of hematogenous metastatic deposits following tail vein inocculation in CHP-134 neuroblastoma cells
medicine
inhibitor PPI-2458 potently inhibits growth of several non-Hodgkin's lymphoma cell lines in a manner correlating with enzyme inhibition
medicine
recombinant MetAP1 is able to provide considerable protection to mice against a Babesia microti challenge infection based on a reduction in peak parasitemia levels and earlier clearance of the parasite as compared with control mice
synthesis
-
recombinant human interferon alpha-2b is produced in Escherichia coli in two types of molecules, one type, in majority, having N-terminal methionine intact, whereas the other type, in minority, having the N-terminal methionine cleaved by methionine aminopeptidase of the host. The N-terminal methionine of the remaining molecules can be removed by utilizing methionine aminopeptidase from Pyrococcus furiosus
synthesis
KT943909
the covalently immobilized enzyme bound to iminodiacetic acid-agarose or chloroacetamido-hexyl-agarose shows long-term stability and allows a continuous, heterogenous processing of N-terminal methionines, for example, in recombinant proteins. Activation by zinc avoids the introduction of heavy metals with toxicological liabilities and oxidative potential into biotechnological processes
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Release 2023.1 (January 2023)
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