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Information on EC 2.6.1.38 - histidine transaminase Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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L-histidine + 2-oxoglutarate = (imidazol-5-yl)pyruvate + L-glutamate
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amino group transfer
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imidazole-lactate degradation
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L-histidine degradation IV
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L-histidine:2-oxoglutarate aminotransferase
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histidine aminotransferase
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histidine-2-oxoglutarate aminotransferase
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N.C.I.B. 10808
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N.C.I.B. 10808
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mouse, inbred strains C57BL, DBA, Peru, SM and SWR
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Tue901/AEC6, mutant hut-11
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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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histidine + 2-oxoisovalerate
imidazol-5-yl-pyruvate + L-valine
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histidine + 2-oxovalerate
imidazol-5-yl-pyruvate + L-norvaline
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imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
imidazol-5-yl-pyruvate + L-glutamate
L-histidine + 2-oxoglutarate
L-histidine + 2-oxobutyrate
imidazol-5-yl-pyruvate + 2-aminobutanoate
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r
L-histidine + glyoxylate
imidazol-5-yl-pyruvate + glycine
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L-histidine + pyruvate
imidazol-5-yl-pyruvate + L-alanine
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ping pong reaction mechanism
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r
additional information
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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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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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imidazol-5-yl-pyruvate + L-glutamate
L-histidine + 2-oxoglutarate
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imidazol-5-yl-pyruvate + L-glutamate
L-histidine + 2-oxoglutarate
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L-histidinol phosphate, D-histidine, 5'-N-methyl-L-histidine and pyruvate are no substrates
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L-histidinol phosphate, D-histidine, 5'-N-methyl-L-histidine and pyruvate are no substrates
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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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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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imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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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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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imidazol-5-yl-pyruvate + L-glutamate
histidine + 2-oxoglutarate
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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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pyridoxal 5'-phosphate
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inactive in absence, Km 0.000059 mM
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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p-chloromercuribenzoate
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2.5
imidazolylpyruvate
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pH 8.0, 30°C
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L-glutamate
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pH 8.0, 30°C
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pyruvate
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pH 8.0, 37°C
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L-histidine
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pH 8.0, 30°C
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L-histidine
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pH 8.0, 37°C
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0.0015
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substrate L-tryptophan
0.0019
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substrate L-histidine
0.002
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substrate L-tyrosine
0.0021
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substrate L-phenylalanine
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7.5 - 8.5
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optimal activity in this pH range, outside this range activity decreases sharply
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45000
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2 * 45000, SDS-PAGE
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homodimer
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2 * 45000, SDS-PAGE
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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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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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HIS8_CALS4
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
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40031
Swiss-Prot
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Coote, J.G.; Hassall, H.
The role of imidazol-5-yl-lactate-nicotinamide-adenine dinucleotide phosphate oxidoreductase and histidine-2-oxoglutarate aminotransferase in the degradation of imidazol-5-yl-lactate by Pseudomonas acidovorans
Biochem. J.
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237-239
1969
Delftia acidovorans
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Hacking, A.J.; Hassall, H.
The purification and properties of L-histidine--2-oxoglutarate aminotransferase from Pseudomonas testosteroni
Biochem. J.
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327-334
1975
Comamonas testosteroni, Comamonas testosteroni N.C.I.B. 10808
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Bulfield, G.
Genetic variation in the activity of the histidine catabolic enzymes between inbred strains of mice: a structural locus for a cytosol histidine aminotransferase isozyme (Hat-1)
Biochem. Genet.
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1233-1241
1978
Mus musculus
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Roos, U.; Mattern, S.; Schrempf, H.; Bormann, C.
Histidine aminotransferase activity in Streptomyces tendae and its correlation with nikkomycin production
FEMS Microbiol. Lett.
97
185-190
1992
Streptomyces tendae
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Roos, U.; Bormann, C.
Purification and characterization of L-histidine aminotransferase from nikkomycin-producing Streptomyces tendae Tu901
J. Gen. Microbiol.
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2773-2778
1993
Streptomyces tendae
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