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Enzyme Nomenclature
Information on EC 2.6.1.38 - histidine transaminase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
2.6.1.38
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RECOMMENDED NAME
GeneOntology No.
histidine transaminase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-histidine + 2-oxoglutarate = (imidazol-5-yl)pyruvate + L-glutamate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
L-histidine:2-oxoglutarate aminotransferase
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CAS REGISTRY NUMBER
COMMENTARY
37277-92-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
histidine + 2-oxocaproate
imidazol-5-yl-pyruvate + L-norleucine
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-
-
-
r
histidine + 2-oxoglutarate
imidazol-5-yl-pyruvate + L-glutamate
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-
-
-
r
L-histidine + 2-oxobutyrate
imidazol-5-yl-pyruvate + 2-aminobutanoate
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-
-
-
r
L-histidine + pyruvate
imidazol-5-yl-pyruvate + L-alanine
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ping pong reaction mechanism
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-
r
imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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essential for utilization of imidazolyl-L-lactate as sole carbon source
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r
imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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essential for utilization of imidazolyl-L-lactate as sole carbon source
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r
imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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-
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r
imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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involved in nikkomycin biosynthesis, essential in the utilization of imidazol-L-lactate and imidazole pyruvate as carbon sources
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r
imidazol-5-yl-pyruvate + L-glutamate
L-histidine + 2-oxoglutarate
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reaction mechanism ping pong, great specificity for histidine as amino donor, highly specific for 2-oxoglutarate in the reverse reaction, very slight activity with 2-oxomalonate or 4-methyl-2-oxopentanoate, L-tyrosine, phenylalanine or L-tryptophan
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r
imidazol-5-yl-pyruvate + L-glutamate
L-histidine + 2-oxoglutarate
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reaction mechanism ping pong, great specificity for histidine as amino donor, highly specific for 2-oxoglutarate in the reverse reaction, very slight activity with 2-oxomalonate or 4-methyl-2-oxopentanoate, L-tyrosine, phenylalanine or L-tryptophan
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r
imidazol-5-yl-pyruvate + L-glutamate
L-histidine + 2-oxoglutarate
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-
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r
imidazol-5-yl-pyruvate + L-glutamate
L-histidine + 2-oxoglutarate
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-
-
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r
additional information
?
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L-histidinol phosphate, D-histidine, 5'-N-methyl-L-histidine and pyruvate are no substrates
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additional information
?
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L-histidinol phosphate, D-histidine, 5'-N-methyl-L-histidine and pyruvate are no substrates
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additional information
?
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no activity observed if L-alanine or L-aspartate replaces glutamate, no activity observed if 2-oxoglutarate is replaced by glyoxylate, pyruvate, 2-oxobutyrate or 2-oxoisocaproate
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additional information
?
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does not use aromatic amino acids as amino substrates, L-phenylalanine, L-tyrosine, L-tryptophan and D-histidine are no substrates, does not react with L-histidinol phosphate, no activity on gels towards L-alanine, L-leucine, L-lysine, L-glutamate and L-aspartate with pyruvate as amino acceptor, no activity towards L-aspartate with 2-oxoglutarate
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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essential for utilization of imidazolyl-L-lactate as sole carbon source
-
r
imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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essential for utilization of imidazolyl-L-lactate as sole carbon source
-
r
imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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-
-
r
imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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involved in nikkomycin biosynthesis, essential in the utilization of imidazol-L-lactate and imidazole pyruvate as carbon sources
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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activity is dependent on the coenzyme and a keto acceptor such as pyruvate or 2-oxoglutarate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 8.5
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optimal activity in this pH range, outside this range activity decreases sharply
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 70
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preincubation of the reaction mixture at 50, 60 and 70°C results in a increase of the reaction rate
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified preparations are unstable, activity is lost during purification, EDTA, DTT or 2-mercaptoethanol stabilizes during purification, pyridoxal 5'-phosphate restores activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 2.6.1.38)
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