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Information on EC 3.5.4.10 - IMP cyclohydrolase
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3.5.4.10 IMP cyclohydrolaseSpecify your search results
Word Map
- 3.5.4.10
- integrins
-
itgav
-
ecm-receptor
-
faicar
- alpha2beta1
-
tfase
- medicine
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
itga2, imp cyclohydrolase, impch, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/imp cyclohydrolase, inosine monophosphate cyclohydrolase, purh2, inosinicase, aicar transformylase/imp cyclohydrolase, mthpuro, puro-type imp cyclohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
-
5-aminoimidazole-4-carboxamide ribonucleotide tranformylase/IMP cyclohydrolase
AF1811
AICAR tranformylase/IMP cyclohydrolase
ATIC
IMP synthetase
-
-
-
-
IMPCH
IMPCHase
-
-
-
-
inosinate cyclohydrolase
-
-
-
-
inosine 5'-monophosphate cyclohydrolase
inosine monophosphate cyclohydrolase
inosinicase
-
-
-
-
PurH
PurH2
PurH2-type IMP cyclohydrolase
PurO
PurO-type IMP cyclohydrolase
TK0430
5-aminoimidazole-4-carboxamide ribonucleotide tranformylase/IMP cyclohydrolase
-
5-aminoimidazole-4-carboxamide ribonucleotide tranformylase/IMP cyclohydrolase
-
-
ATIC
-
-
-
-
inosine monophosphate cyclohydrolase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
-
-
-
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
mechanism
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
mechanism,kinetics, enzyme reaction draws the overall bifunctional reaction towards the IMP product
-
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
orbital steering mechanism
-
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
catalytic mechanism, Glu104 is essential for catalysis
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
two possible catalytic mechanisms for cyclization, Glu102 is essential for catalysis
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
internal C-N condensation
-
-
H2O elimination
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
IMP 1,2-hydrolase (decyclizing)
-
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CAS REGISTRY NUMBER
COMMENTARY
9013-81-4
-
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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
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide + H2O
?
catalyzation of the final two steps of de novo purine biosynthesis pathway
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
the enzyme catalyze the final step of de novo purine biosynthesis
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
the enzyme catalyze the final step of de novo purine biosynthesis
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
the two activities of the bifunctional AICAR transformylase/IMP cyclohydrolase reside on separate domains
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
the enzyme catalyze the final step of de novo purine biosynthesis
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
the enzyme catalyze the final step of de novo purine biosynthesis
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
ir
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
ir
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
ir
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
ir
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
?
5-formaminoimidazole-4-carboxamide ribonucleotide
IMP + H2O
the enzyme catalyzes the cyclization of 5-formaminoimidazole-4-carboxamide ribonucleotide, FAICAR, to IMP in the final step of de novo purine biosynthesis
-
-
?
5-formaminoimidazole-4-carboxamide ribonucleotide
IMP + H2O
the IMPCH domain catalyzes the intramolecular cyclization of 5-formyl-AICAR, FAICAR, to IMP
-
-
?
trans-alpha,beta-diformamido-beta-(5'-phosphoribosylamino)acrylamide
IMP + H2O
-
-
-
ir
trans-alpha,beta-diformamido-beta-(5'-phosphoribosylamino)acrylamide
IMP + H2O
-
-
-
ir
additional information
?
-
bifunctional enzyme aminoimidazole-comprising the 4-carboxamide ribonucleotide transformylase, AICAR or Tfase, residues 200-593 and the IMPCH, ATIC, activities and catalyzes the final step in the de novo purine biosynthesis pathway that produces IMP, overview
-
-
?
additional information
?
-
the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview
-
-
?
additional information
?
-
-
the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview
-
-
?
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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
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide + H2O
?
catalyzation of the final two steps of de novo purine biosynthesis pathway
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
the enzyme catalyze the final step of de novo purine biosynthesis
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
the enzyme catalyze the final step of de novo purine biosynthesis
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
-
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
the enzyme catalyze the final step of de novo purine biosynthesis
-
-
?
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP + H2O
the enzyme catalyze the final step of de novo purine biosynthesis
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
5-formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
?
-
de novo purine synthesis step 10
-
-
?
additional information
?
-
bifunctional enzyme aminoimidazole-comprising the 4-carboxamide ribonucleotide transformylase, AICAR or Tfase, residues 200-593 and the IMPCH, ATIC, activities and catalyzes the final step in the de novo purine biosynthesis pathway that produces IMP, overview
-
-
?
additional information
?
-
the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview
-
-
?
additional information
?
-
-
the TM1249 gene or gene purH of Thermotoga maritima encodes a bifunctional enzyme with 5-aminoimidazole-4-carboxamide ribonucleotide transformylase, AICAR Tfase, EC 2.1.2.3, and inosine 5'-monophosphate cyclohydrolase, IMPCH, EC 3.5.4.10, activities. These activities represent the final two steps of the de novo purine biosynthesis pathway, overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2-dioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one
construction of 1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one 2,2-dioxide, the corresponding nucleoside, and the nucleoside monophosphate, as mimics of the tetrahedral intermediate in the cyclization reaction. All compounds are competitive inhibitors against IMPCH, but the simpler heterocycle has a completely different IMPCH binding mode, compared to the nucleosides, and is relocated to the phosphate binding pocket, the aromatic imidazole ring interacts with a helix dipole, inhibitor synthesis, binding structure, and mechanism of inhibition, overview
2-flouroinosine 5'-monophosphate
-
IC50-value in cell culture 0.0049 mM; potent inhibitor
2-mercaptoinosine 5'-monophosphate
-
most potent competitive inhibitor, precursor of GMP in the purine pathway
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
decreased IMP cyclohydrolase activity by 10-50%
7-(3,4-dihydroxy-5-hydroxymethyltetrahydrofuran-2-yl)-2,2-dioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one
construction of 1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one 2,2-dioxide, the corresponding nucleoside, and the nucleoside monophosphate, as mimics of the tetrahedral intermediate in the cyclization reaction. All compounds are competitive inhibitors against IMPCH, but the simpler heterocycle has a completely different IMPCH binding mode, compared to the nucleosides, and is relocated to the phosphate binding pocket, the aromatic imidazole ring interacts with a helix dipole, inhibitor synthesis, binding structure, and mechanism of inhibition, overview
N2-acetyl-2'deoxyguanosine 5'-monophosphate
-
decreased IMP cyclohydrolase activity by 10-50%
N6-(carboxymethyl)adenosine 5'-monophosphate
-
strong competitive inhibitor
phosphoric acid mono-[3,4-dihydroxy-5-(2,2,4-trioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-7-yl)tetrahydrofuran-2-yl]methyl ester
construction of 1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one 2,2-dioxide, the corresponding nucleoside, and the nucleoside monophosphate, as mimics of the tetrahedral intermediate in the cyclization reaction. All compounds are competitive inhibitors against IMPCH, but the simpler heterocycle has a completely different IMPCH binding mode, compared to the nucleosides, and is relocated to the phosphate binding pocket, the aromatic imidazole ring interacts with a helix dipole, inhibitor synthesis, binding structure, and mechanism of inhibition, overview
2-fluoroadenine arabinoside 5'-monophosphate
-
IC50-value in cell culture 0.0002 mM; strong competitive inhibitor, derivative of anti-cancer drug
2-fluoroadenine arabinoside 5'-monophosphate
-
strong competitive inhibitor, derivative of anti-cancer drug
6-mercaptopurine riboside 5'-monophosphate
-
IC50-value in cell culture 0.0075 mM; strong competitive inhibitor, derivative of anti-cancer drug
6-mercaptopurine riboside 5'-monophosphate
-
strong competitive inhibitor, derivative of anti-cancer drug
adenosine N1-oxide 5'-monophosphate
-
IC50-value in cell culture 0.0011 microM; strong competitive inhibitor
IMP
-
minor 5% IMP contaminant in the substrate found to have no effects on the inosinicase assay
additional information
not inhibitory: EDTA at 2 mM, iodoacetamide at 20mM, XMP, at 0.05 mM, IMP, at 0.02 mM
-
additional information
-
not inhibitory: EDTA at 2 mM, iodoacetamide at 20mM, XMP, at 0.05 mM, IMP, at 0.02 mM
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00156
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.3, 50°C
0.00184
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
IMP cyclohydrolase of the domain truncation mutant pET-28c-IMPCH, pH 7.4, temperature not specified in the publication
0.0078
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.3, 50°C
0.0346
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.5, temperature not specified in the publication
0.21
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
full length bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC), pH 7.4, temperature not specified in the publication
0.0009
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, wild type
0.0009
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, wild-type
0.0027
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant D125N
0.0027
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant K137R
0.0027
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant D125N
0.0027
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant K137R
0.003
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant Y104A
0.003
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant Y104A
0.0036
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant Y104F
0.0036
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant Y104F
0.0052
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant D125E
0.0052
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant D125E
0.0091
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant D125A
0.0091
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant D125A
0.031
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant K137A
0.031
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant K137A
0.082
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
0.115
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant K66A
0.115
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant K66A
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.48
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.3, 50°C
1.32
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.3, 50°C
3.63
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.5, temperature not specified in the publication
0.014
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant D125A
0.014
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutantD125A
0.036
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant Y104F
0.036
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutantY104F
0.062
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant K66A
0.062
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutantK66A
0.136
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant Y104A
0.136
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutantY104A
0.147
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant D125E
0.147
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant D125E
0.276
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant K137A
0.276
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutantK137A
0.507
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant K137R
0.507
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant K137R
0.603
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant D125N
0.603
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, mutant D125N
6.08
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant D125N
6.08
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, mutant K137R
8.6
5-Formamido-1-(5-phosphoribosyl)imidazole-4-carboxamide
-
pH 7.5, 22°C, wild-type
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
104.9
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.5, temperature not specified in the publication
307.7
5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
pH 7.3, 50°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.13
1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one 2,2-dioxide
pH 7.4
0.23
7-(3,4-dihydroxy-5-hydroxymethyltetrahydrofuran-2-yl)-2,2-dioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one
about, pH 7.4
0.15
phosphoric acid mono-[3,4-dihydroxy-5-(2,2,4-trioxo-1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-7-yl)tetrahydrofuran-2-yl]methyl ester
about, pH 7.4
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
2-fluoroadenine arabinoside 5'-monophosphate
Homo sapiens
-
IC50-value in cell culture 0.0002 mM
0.0075
6-mercaptopurine riboside 5'-monophosphate
Homo sapiens
-
IC50-value in cell culture 0.0075 mM
0.0000011
adenosine N1-oxide 5'-monophosphate
Homo sapiens
-
IC50-value in cell culture 0.0011 microM
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.8
extract from Escherichia coli expression mutants after several pufification steps
additional information
additional information
proteomic approach to identify phophorylated proteins with a pathogenic role in transformation mediated by anaplastic lymphoma kinase (ALK), profiling of tyrosine-phosphorylation, mass spectrometry, anti-phosphotyrosine protein immunoprecipitation, posttranslational modification of the bifunctional 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) formyltransferase/inosine monophosphate (IMP) cyclohydrolase (AICAR-FT/IMP-CHase, ATIC) by phosphorylation, enzyme is a direct target of anaplastic lymphoma kinase (ALK), phoshorylation increases enzyme activity posttranslational modification of a key purine synthesis enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
8.4
IMP cyclohydrolase activity of the bifunctional enzyme
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
pH 6.0: about 60% of maximal activity, pH 10.0: about 60% of maximal activity, IMP cyclohydrolase activity of the bifunctional enzyme
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
37
IMP cyclohydrolase activity of the bifunctional enzyme
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
20°C: about 45% of maximal activity, 50°C: about 40% of maximal activity, IMP cyclohydrolase activity of the bifunctional enzyme
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme is expressed at nearly constant levels in both nondiapausing and prediapausing adults and downregulated by temperature in diapausing beetles stored at 10°C
-
-
brenda
bifunctional protein, including EC 3.5.4.10 and EC 2.1.2.3
UniProt
brenda
bifunctional aminoimidazole carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase
-
-
brenda
bifunctional enzyme 5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase
-
-
brenda
bifunctional enzyme 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase
-
-
brenda
bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase
SwissProt
brenda
bifunctional inosine monophosphate cyclohydrolase/AICAR transformylase. Female infant patient with lack in transformylase activity and about 40% residual enzymic activity, showing massive excretion of 5-amino-4-imidazolecarboxamide riboside, dysmorphic features, severe neurological defects, and congenital blindness
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
ALCL cell line TS, Sup-M2 cells, JB-6 cells, SU-DHL1 cells
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
malfunction
-
impact of the ITGA2 gene polymorphism C807T on gastric cancer risk, overview. Increased risk of gastric cancer associated with the polymorphism is pronounced in rural subjects, but not in urban subjects
malfunction
growth deficiency phenotypes (in un-supplemented M9 minimal medium containing thymidine) are direct consequences of the gene deletions
malfunction
-
growth deficiency phenotypes (in un-supplemented M9 minimal medium containing thymidine) are direct consequences of the gene deletions
-
metabolism
last enzyme of the de novo purine synthesis pathway. The enzyme plays a central role in insulin signaling and the Golgi/endosomes protein network
metabolism
the 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) transformylase/inosine monophosphate (IMP) cyclohydrolase (ATIC) catalyzes final two steps of purine nucleotide de novo biosynthetic pathway. The cell proliferation activity of the enzyme is observed where it promotes proliferation and viability of NIH 3T3 and RIN-5F cells, exhibits in vitro wound healing in NIH 3T3 fibroblast cells, and rescues RIN-5F cells from the cytotoxic effects of palmitic acid and high glucose
metabolism
the enzyme AICAR-transformylase/IMP cyclohydrolase (ATIC) catalyzes the last two steps of purine de novo synthesis. High glucose up-regulates the expression and activity of the enzyme and increases the levels of reactive oxygen species and methylglyoxal-derived advanced glycation end products. Overexpression of the enzyme (atic-1) decreases the lifespan and head motility and increases neuronal damage under both standard and high glucose conditions. Inhibition of atic-1 expression, by RNAi, under high glucose is associated with increased lifespan and head motility and reduced neuronal damage, reactive oxygen species, and methylglyoxal-derived advanced glycation end product accumulation. The enzyme (atic-1) is involved in glucotoxic effects under high glucose conditions, either by blocked atic-1 expression or viainduction of 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) and AMP-activated kinase (AMPK) induction
metabolism
the enzyme catalyze the final step of de novo purine biosynthesis
metabolism
the enzyme catalyze the final step of de novo purine biosynthesis
metabolism
-
the enzyme catalyze the final step of de novo purine biosynthesis
-
metabolism
-
the enzyme catalyze the final step of de novo purine biosynthesis
-
Show AA Sequence and Transmembrane Helices (37909 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
49700
1 * 49700, enzyme comprising residues 1-452, i.e. the IMP cyclohydrolase part of the bifunctional enzyme, SDS-PAGE
64200
-
2 * 64200, open reading frame, polypeptide of 592 amino acids, 91% similar to human IMPCHase
64425
2 * 64425, open reading frame, polypeptide of 591 amino acids, 81% similar to chicken IMPCHase, truncation mutant, IMPCHase activity located within the NH2-terminal 223 amino acids
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
1 * 49700, enzyme comprising residues 1-452, i.e. the IMP cyclohydrolase part of the bifunctional enzyme, SDS-PAGE
tetramer
MthPurO has a four-layered alphabetabetaalpha core structure, showing an N-terminal nucleophile hydrolase fold. The active site is located at the deep pocket between two central beta-sheets and contains residues strictly conserved within PurOs, structure analysis, modelling, detailed overview
additional information
?
-
open reading frame of 527 amino acids, complementatition analysis show that the IMP cyclohydrolase activity resides on the N-terminal region
dimer
2 * 64425, open reading frame, polypeptide of 591 amino acids, 81% similar to chicken IMPCHase, truncation mutant, IMPCHase activity located within the NH2-terminal 223 amino acids
dimer
-
2 * 64200, open reading frame, polypeptide of 592 amino acids, 91% similar to human IMPCHase
dimer
2 * 54000, SDS-PAGE, gel filtration and glutaraldehyde cross-linking studies, the purified recombinant enzyme and its truncated domains exist mainly in dimeric form
additional information
-
MthPurO has a four-layered alphabetabetaalpha core structure, showing an N-terminal nucleophile hydrolase fold. The active site is located at the deep pocket between two central beta-sheets and contains residues strictly conserved within PurOs
additional information
MthPurO has a four-layered alphabetabetaalpha core structure, showing an N-terminal nucleophile hydrolase fold. The active site is located at the deep pocket between two central beta-sheets and contains residues strictly conserved within PurOs
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with inhibitors, sitting drop vapor diffusion method, 22°C, 10 mg/ml protein, mixing of equal volumes of protein and reservoir solutions, the latter containing 20% w/v PEG 8000, 0.2 M imidazole, pH 7.2, 5 mM dithiothreitol, X-ray diffraction structure determination and analysis at 2.0-2.7 A resolution
MthPurO in complex with either IMP or 5-aminoimidazole-4-carboxamide ribonucleotide, crystals from 30 mg/ml protein in 25-30% MPD, 0.2 M ammonium acetate, and 0.1 M sodium citrate buffer, pH 5.6, 0.001 ml protein solution is mixed with 0.001 ml of reservoir solution, equilibration against 0.5 mL reservoir solution, 24°C, od-shaped crystals, 3-4 weeks, X-ray diffraction structure determination and analysis at 2.0 A and 2.6 A resolution, respectively, method optimization, molecular replacement and modelling
MthPurO in complex with either IMP or 5-aminoimidazole-4-carboxamide ribonucleotide, X-ray diffraction structure determination and analysis at 2.0 A and 2.6 A resolution, respectively
20 mg/ml purified recombinant enzyme in 20 mM Tris, pH 7.9, 150 mM NaCl, 0.25 mM TCEP, nanodroplet vapor diffusion method, the crystallization solution contains 20% w/v PEG 6000 and 0.1 M citrate pH 5.0, 10% v/v PEG 200 as a cryoprotectant, X-ray diffraction structure determination and anaylsis at 1.88 A resolution, modelling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D125A
D125E
D125N
K137A
K137R
K246R
natural mutation observed in female infant patient with lack in transformylase activity and about 40% residual enzymic activity, showing massive excretion of 5-amino-4-imidazolecarboxamide riboside, dysmorphic features, severe neurological defects, and congenital blindness. Recombinant protein with K426R mutation completely lacks AICAR transformylase activity
K66A
Y104A
Y104A/D125A
Y104F
Y104F/D125A
C61A
site-directed mutagenesis, the mutant shows 8fold increased activity compared to the wild-type enzyme
E102Q
site-directed mutagenesis, inactive mutant
R31K
site-directed mutagenesis, the mutant shows 76% reduced activity compared to the wild-type enzyme
Y59F
site-directed mutagenesis, the mutant shows 34% reduced activity compared to the wild-type enzyme
H256A
complete loss of activity, mutation lowers the thermostability
K255A
complete loss of activity, mutation lowers the thermostability
K255R
mutation reduces activity by 76%. Mutation increases the Tm by approximately 3°C
N415A
decrease in AICAR transformylase activity as compared with wild-type SlugATIC, indicating it might also play essential role in substrate binding. Increase in the thermostability
Y104A/D125A
-
enzyme activity very low but detectable, contrary to wild type a minimal dependence of specific activity on concentration
Y104F/D125A
-
enzyme activity very low but detectable, contrary to wild type a minimal dependence of specific activity on concentration
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
1 h, enzyme retains 20% of its IMP cyclohydrolase activity
756701
6
1 h, enzyme retains 60% of its IMP cyclohydrolase activity
756701
6.5 - 10
1 h, quite stable over a broad pH range from 6.5 to 10
756701
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42.1
three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C
44.7
three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C
45
10 min, the bifunctional AICAR transformylase/IMP cyclohydrolase (ATIC) is stable at lower temperatures and both the activities start declining after 45°C
46.9
three transitions at a Tm of 42.1°C, 44.7°C and 46.9°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as glutathione-S-transferase fusion protein in Escherichia coli mutants
-
recombinant His-tagged enzyme from Escherichia coli by nickel affinity and anion exchange chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21 by cobalt affinity chromatography, elution with imidazole, to homogeneity
soluble recombinant wild-type and mutant enzymes from Escherichia coli strain BL21 by heat treatment for 15 min at 70°C, and anion exchange chromatography, to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene ITGA2, genotyping of 614 male subjects, 1:1 ratio of gastric cancer patients and healthy controls, overview
-
overexpressed in Rosetta2 (DE3) cells
overexpression of His-tagged enzyme in Escherichia coli strain BL21
overexpression of wild-type and mutant enzymes in Escherichia coli strain BL21
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high glucose up-regulates the expression and activity of the enzyme and increases the levels of reactive oxygen species and methylglyoxal-derived advanced glycation end products. Overexpression of the enzyme (atic-1) decreases the lifespan and head motility and increases neuronal damage under both standard and high glucose conditions
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
medicine
determination of differentially expressed genes in HT-29 cells, both after short treatment with methotrexate and after the resistance to methotrexate has been established. Enzyme as well as survivin and inosine monophosphate dehydrogenase type II are upregulated
drug development
the enzyme is a potential target for antineoplastic intervention, design of IMPCH inhibitors, overview
drug development
the enzyme is an important drug target
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ebbole, D.J.; Zalkin, H.
Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis
J. Biol. Chem.
262
8274-8287
1987
Bacillus subtilis
brenda
Flaks, J.G.; Erwin, M.J.; Buchanan, J.M.
Biosynthesis of the purines: XVIII. 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase and inosinicase
J. Biol. Chem.
229
603-612
1957
Sus scrofa
brenda
Gots, S.J.; Dalal, F.R.; Shumas, S.R.
Genetic separation of the inosinic acid cyclohydrolase-transformylase complex of Salmonella typhimurium
J. Bacteriol.
99
441-449
1969
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Geiger, R.; Guglielmi, H.
[IMP-cyclohydrolase/transformylase from Ehrlich-ascites carcinoma
Hoppe-Seyler's Z. Physiol. Chem.
356
819-825
1975
Mus musculus
brenda
Baggott, J.E.; Krumdieck, C.L.
trans-alpha, beta-Diformamido-beta-(5-phosphoribosylamino)acrylamide: a possible new intermediate in de novo purine biosynthesis
Biochemistry
18
3501-3506
1979
Gallus gallus, Rattus norvegicus
brenda
Ni, L.; Guan, K.; Zalkin, H.; Dixon, J.D.
De novo purine biosynthesis: cloning, sequencing and expression of a chicken PurH cDNA encoding 5-aminoimidazole-4-carboxamide-ribinucleotide transformylase-IMP cyclohydrolase
Gene
106
197-205
1981
Gallus gallus
brenda
Szabados, E.; Hindmarsh, E.J.; Phillips, L.; Duggleby, R.G.; Christopherson, R.I.
5-Aminoimidazole-4-carboxamide ribotide transformylase-IMP cyclohydrolase from human CCRF-CEM leukemia cells: purification, pH dependence and inhibitors
Biochemistry
33
14237-14245
1994
Homo sapiens
brenda
Christopherson, R.I.; Williams, N.K.; Schoettle, S.L.; Szabados, E.; Hambley, T.W.; Manthey, M.K.
Inhibitors of dihydroorotase, amidophosphoribosyltransferase and IMP cyclohydrolase as potential drugs
Biochem. Soc. Trans.
23
888-893
1995
Homo sapiens
brenda
Rayl, E.A.; Moroson, B.A.; Beardsley, G.P.
The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping
J. Biol. Chem.
271
2225-2233
1996
Homo sapiens (P31939), Homo sapiens
brenda
Akira, T.; Komatsu, M.; Nango, R.; Tomooka, A.; Konaka, K.; Yamauchi, M.; Kitamura, Y.; Nomura, S.; Tsukamoto, I.
Molecular cloning and expression of a rat cDNA encoding 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase
Gene
197
289-293
1997
Rattus norvegicus
brenda
Szabados, E.; Manthey, M.K.; Wilson, P.K.; Christopherson, R.I.
Inosine-5'-monophosphate analogues as inhibitors of human IMPcyclohydrolase and cellular growth
Biochem. Mol. Biol. Int.
44
617-623
1998
Homo sapiens
brenda
Caperelli, C.A.; Benkovic, P.A.; Chettur, G.; Benkovic, S.J
Purification of a complex catalizing folate cofactor synthesis and transformylation in de novo purine biosynthesis
J. Biol. Chem.
255
1885-1890
1980
Gallus gallus
brenda
Aiba, A.; Mizobuchi, K.
Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli
J. Biol. Chem.
264
21239-21246
1989
Escherichia coli
brenda
Flannigan, K.A.; Hennigan, S.H.; Vogelbacker, H.H.; Gots, J.S.; Smith, J.M.
Purine biosynthesis in Escherichia coli K12: structure and DNA sequence studies of the purHD locus
Mol. Microbiol.
4
381-392
1990
Escherichia coli
brenda
Mueller, W.T.; Benkovic, S.J.
On the purification and mechanism of action of 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase from chicken liver
Biochemistry
20
337-344
1981
Gallus gallus
brenda
Vergis, J.M.; Bulock, K.G.; Fleming, K.G.; Beardsley, G.P.
Human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase. A bifunctional protein requiring dimerization for transformylase activity but not for cyclohydrolase activity
J. Biol. Chem.
276
7727-7733
2001
Homo sapiens
brenda
Bulock, K.G.; Beardsley, G.P.; Anderson, K.S.
The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5'-monophosphate cyclohydrolase): A surprising lack of substrate channeling
J. Biol. Chem.
277
22168-22174
2002
Homo sapiens
brenda
Wolan, D.W.; Cheong, C.G.; Greasley, S.E.; Wilson, I.A.
Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor
Biochemistry
43
1171-1183
2004
Homo sapiens (P31939), Homo sapiens
brenda
Graupner, M.; Xu, H.; White, R.H.
New class of IMP cyclohydrolases in Methanococcus jannaschii
J. Bacteriol.
184
1471-1473
2002
Methanocaldococcus jannaschii (Q58043), Methanocaldococcus jannaschii
brenda
Cheong, C.G.; Wolan, D.W.; Greasley, S.E.; Horton, P.A.; Beardsley, G.P.; Wilson, I.A.
Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates
J. Biol. Chem.
279
18034-18045
2004
Homo sapiens (P31939), Homo sapiens
brenda
Vergis, J.M.; Beardsley, G.P.
Catalytic mechanism of the cyclohydrolase activity of human aminoimidazole carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase
Biochemistry
43
1184-1192
2004
Homo sapiens
brenda
Marie, S.; Heron, B.; Bitoun, P.; Timmerman, T.; Van Den Berghe, G.; Vincent, M.F.
AICA-ribosiduria: a novel, neurologically devastating inborn error of purine biosynthesis caused by mutation of ATIC
Am. J. Hum. Genet.
74
1276-1281
2004
Homo sapiens (P31939), Homo sapiens
brenda
Yocum, G.D.
Environmental regulation of the purine synthesis enzyme purH transcript during adult diapause in Leptinotarsa decemlineata (Coleoptera: Chrysomelidae)
Eur. J. Entomol.
101
199-203
2004
Leptinotarsa decemlineata
-
brenda
Penuelas, S.; Noe, V.; Ciudad, C.J.
Modulation of IMPDH2, survivin, topoisomerase I and vimentin increases sensitivity to methotrexate in HT29 human colon cancer cells
FEBS J.
272
696-710
2005
Homo sapiens (P31939), Homo sapiens
brenda
Kang, Y.N.; Tran, A.; White, R.H.; Ealick, S.E.
A novel function for the N-terminal nucleophile hydrolase fold demonstrated by the structure of an archaeal inosine monophosphate cyclohydrolase
Biochemistry
46
5050-5062
2007
Methanothermobacter thermautotrophicus, Methanothermobacter thermautotrophicus (O27089)
brenda
Xu, L.; Chong, Y.; Hwang, I.; DOnofrio, A.; Amore, K.; Beardsley, G.P.; Li, C.; Olson, A.J.; Boger, D.L.; Wilson, I.A.
Structure-based design, synthesis, evaluation, and crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase
J. Biol. Chem.
282
13033-13046
2007
Gallus gallus (P31335)
brenda
Axelrod, H.L.; McMullan, D.; Krishna, S.S.; Miller, M.D.; Elsliger, M.; Abdubek, P.; Ambing, E.; Astakhova, T.; Carlton, D.; Chiu, H.; Clayton, T.; Duan, L.; Feuerhelm, J.; Grzechnik, S.K.; Hale, J.; Han, G.W.; Haugen, J.; Jaroszewski, L.; Jin, K.K.; Klock, H.E.; Knuth, M.W.; Koesema, E.; Morse, A.T.; Nigoghossian, E.; Okach, L.; Oommachen, S.; Paulsen, J.; Quijano, K.; Reyes, R.; Rife, C.L.; van den Bedem, H.; Weekes, D.; White, A.; Wolf, G.; Xu, Q.; Hodgson, K.O.; Wooley, J.; Deacon. A.M.; Godzik, A.; Lesley, S.A.; Wilson, I.A.
Crystal structure of AICAR transformylase IMP cyclohydrolase (TM1249) from Thermotoga maritima at 1.88 ANG. resolution
Proteins Struct. Funct. Bioinform.
71
1042-1049
2008
Thermotoga maritima (Q9X0X6), Thermotoga maritima
brenda
Boccalatte, F.E.; Voena, C.; Riganti, C.; Bosia, A.; DAmico, L.; Riera, L.; Cheng, M.; Ruggeri, B.; Jensen, O.N.; Goss, V.L.; Lee, K.; Nardone, J.; Rush, J.; Polakiewicz, R.D.; Comb, M.J.; Chiarle, R.; Inghirami, G.
The enzymatic activity of 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase is enhanced by NPM-ALK: new insights in ALK-mediated pathogenesis and the treatment of ALCL
Blood
113
2776-2790
2009
Homo sapiens (P31939)
brenda
Chen, X.; Zhao, J.; Xu, X.; Zeng, R.
Screening and cloning of IMP cyclohydrolase from a metagenomic cosmid library of a deep-sea sediment sample
Chin. J. Appl. Environ. Biol.
17
855-859
2011
Homo sapiens
-
brenda
Verma, P.; Kar, B.; Varshney, R.; Roy, P.; Sharma, A.
Characterization of AICAR transformylase/IMP cyclohydrolase (ATIC) from Staphylococcus lugdunensis
FEBS J.
284
4233-4261
2017
Staphylococcus lugdunensis (A0A133Q8U5), Staphylococcus lugdunensis
brenda
Riedinger, C.; Mendler, M.; Schlotterer, A.; Fleming, T.; Okun, J.; Hammes, H.P.; Herzig, S.; Nawroth, P.P.
High-glucose toxicity is mediated by AICAR-transformylase/IMP cyclohydrolase and mitigated by AMP-activated protein kinase in Caenorhabditis elegans
J. Biol. Chem.
293
4845-4859
2018
Caenorhabditis elegans (Q95QQ4)
brenda
Sah, S.; Shah, R.; Govindan, A.; Varada, R.; Rex, K.; Varshney, U.
Utilisation of 10-formyldihydrofolate as substrate by dihydrofolate reductase (DHFR) and 5-aminoimidazole-4-carboxamide ribonucleotide (AICAR) tranformylase/IMP cyclohydrolase (PurH) in Escherichia coli
Microbiology
164
982-991
2018
Escherichia coli (P15639), Escherichia coli K12 (P15639)
brenda
Boutchueng-Djidjou, M.; Collard-Simard, G.; Fortier, S.; Hebert, S.; Kelly, I.; Landry, C.; Faure, R.
The last enzyme of the de novo purine synthesis pathway 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase (ATIC) plays a central role in insulin signaling and the Golgi/endosomes protein network
Mol. Cell. Proteomics
14
1079-1092
2015
Rattus norvegicus (O35567)
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Hunter, C.; Plymale, N.; Smee, K.; Sarisky, C.
Experimental characterization of two archaeal inosine 5'-monophosphate cyclohydrolases
PLoS ONE
14
e0223983
2019
Archaeoglobus fulgidus (O28464), Thermococcus kodakarensis (Q5JD29), Archaeoglobus fulgidus ATCC 49558 (O28464), Thermococcus kodakarensis ATCC BAA-918 (Q5JD29)
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Release 2023.1 (January 2023)
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