Information on EC 2.5.1.108 - 2-(3-amino-3-carboxypropyl)histidine synthase

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The expected taxonomic range for this enzyme is: Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.5.1.108
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RECOMMENDED NAME
GeneOntology No.
2-(3-amino-3-carboxypropyl)histidine synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] = S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
diphthamide biosynthesis (archaea)
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diphthamide biosynthesis (eukaryotes)
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:L-histidine-[translation elongation factor 2] 2-[(3S)-3-amino-3-carboxypropyl]transferase
A [4Fe-4S] enzyme that modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical. The enzyme is present in archae and eukaryotes but not in eubacteria. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Part of diphthamide biosynthesis.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine
2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
show the reaction diagram
L-histidine-[translation elongation factor 2] + [[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl][(2E)-3-carboxyprop-2-en-1-yl]methylsulfonium
2-(3-carboxyprop-2-en-1-yl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
show the reaction diagram
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S-adenosyl-L-methionine analogue, in which the 3-amino-3-carboxypropyl group is replaced with a 3-carboxyallyl group. The analogue is cleaved by Dph2, yielding a paramagnetic (S = 1/2) species, which is assigned to a complex formed between the reaction product, alpha-sulfinyl-3-butenoic acid, and the [4Fe-4S] cluster. Data support a pi-complex between the C=C double bond of alpha-sulfinyl-3-butenoic acid and the unique iron of the [4Fe-4S] cluster, i.e. a radical S-adenosyl-L-methionine-related [4Fe-4S]+ cluster forming an organometallic complex with an alkene
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-
?
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]
show the reaction diagram
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-carboxypropyl]-L-histidine-[translation elongation factor 2]
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine500-[translation elongation factor 2]
show the reaction diagram
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the enzyme is involved in diphthamide biosynthesis
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-
?
S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
show the reaction diagram
S-adenosyl-L-methionine + L-histidine699-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine699-[translation elongation factor 2]
show the reaction diagram
the enzyme is involved in diphthamide biosynthesis
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-
?
S-adenosyl-L-methionine + L-histidine715-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine715-[translation elongation factor 2]
show the reaction diagram
the enzyme is involved in diphthamide biosynthesis
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-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-histidine-[translation elongation factor 2] + S-adenosyl-L-methionine
2-((3S)-3-amino-3-carboxypropyl)-L-histidine-[translation elongation factor 2] + S-methyl-5'-thioadenosine
show the reaction diagram
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]
show the reaction diagram
O58832
first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2
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-
?
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-carboxypropyl]-L-histidine-[translation elongation factor 2]
show the reaction diagram
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-
-
-
?
S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine500-[translation elongation factor 2]
show the reaction diagram
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the enzyme is involved in diphthamide biosynthesis
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-
?
S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
show the reaction diagram
O58832
the enzyme is involved in diphthamide biosynthesis
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-
?
S-adenosyl-L-methionine + L-histidine699-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine699-[translation elongation factor 2]
show the reaction diagram
P32461
the enzyme is involved in diphthamide biosynthesis
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-
?
S-adenosyl-L-methionine + L-histidine715-[translation elongation factor 2]
S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine715-[translation elongation factor 2]
show the reaction diagram
Q9CR25
the enzyme is involved in diphthamide biosynthesis
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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dependent on
[4Fe-4S]-center
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cleavage of a S-adenosyl-L-methionine analogue, in which the 3-amino-3-carboxypropyl group is replaced with a 3-carboxyallyl group, yields a paramagnetic (S = 1/2) species, which is assigned to a complex formed between the reaction product, alpha-sulfinyl-3-butenoic acid, and the [4Fe-4S] cluster. Data support a pi-complex between the C=C double bond of alpha-sulfinyl-3-butenoic acid and the unique iron of the [4Fe-4S] cluster, i.e. a radical S-adenosyl-L-methionine-related [4Fe-4S]+ cluster forming an organometallic complex with an alkene
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
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a [4Fe–4S] enzyme
Iron-sulfur cluster
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
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2 * 34000, SDS-PAGE
59772
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x * 59772, calculated from amino acid sequence
60000
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x * 60000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure at 2.3 A resolution; hanging-drop vapour-diffusionmethod, X-ray crystal structure at 2.3 A resolution using selenomethionine single-wavelength anomalous diffraction phasing
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; wild-type and mutant enzymes
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli and in NIH-3T3 cells
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expressed in Escherichia coli; expression in Escherichia coli
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expression in Escherrichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C163A
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difference in the EPR spectrum of the reduced form, pronounced rhombic main features with greatly increased g-value anisotropy, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600; mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster
C259A/C287A
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homodimeric mutant enzyme not stable. It is inactive and cannot bind a [4Fe-4S] cluster. Heterodimeric enzyme with a wild-type subunit and a mutant subunit is active
C287A
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difference in the EPR spectrum, g-tensors are more axial than wild type, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600; mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster
C59A
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difference in the EPR spectrum, g-tensors are more axial than wild type, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600; mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster
C59A/C287A
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inactive mutant lacks the Fe-S cluster. A heterodimer of wild-type subunit and C59A/C287A mutant subunit is stable and active