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
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
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
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
Lepirudin in patients with heparin-induced thrombocytopenia - results of the third prospective study (HAT-3) and a combined analysis of HAT-1, HAT-2, and HAT-3.
development and evaluation of a method for the prediction of possible genes of orphan enzyme reactions where any associated gene sequences are not determined to date. The candidate enzyme gene of a reaction is detected using the chemical structures of the substrate-product pair (reactant pair). The proposed method is based on a search for similar reactant pairs in a reference database (KEGG database) and offers orthologeous groups that possibly mediate the given reaction. One example is the histidine transaminase (R01161, EC 2.6.1.38), which transfers an amino group from histidine to glutamate. For the query consisting of histidine and imidazol-5-pyruvate (RP01339 in the RPAIR database), K00817 is predicted by the method with the highest score (0.971). The function of this KO entry is the transfer of an amino group from phenylalanine, tyrosine, and histidinol phosphate (histidinol-phosphate transaminase, EC 2.6.1.9), which are structurally similar to histidine, to glutamate. In addition, this KO entry contains the enzyme gene sequence tte:TTE2137 of Thermoanaerobacter tengcongensis, for which a histidine transaminase activity has been detected in the heterologous expression study
development and evaluation of a method for the prediction of possible genes of orphan enzyme reactions where any associated gene sequences are not determined to date. The candidate enzyme gene of a reaction is detected using the chemical structures of the substrate-product pair (reactant pair). The proposed method is based on a search for similar reactant pairs in a reference database (KEGG database) and offers orthologeous groups that possibly mediate the given reaction. One example is the histidine transaminase (R01161, EC 2.6.1.38), which transfers an amino group from histidine to glutamate. For the query consisting of histidine and imidazol-5-pyruvate (RP01339 in the RPAIR database), K00817 is predicted by the method with the highest score (0.971). The function of this KO entry is the transfer of an amino group from phenylalanine, tyrosine, and histidinol phosphate (histidinol-phosphate transaminase, EC 2.6.1.9), which are structurally similar to histidine, to glutamate. In addition, this KO entry contains the enzyme gene sequence tte:TTE2137 of Thermoanaerobacter tengcongensis, for which a histidine transaminase activity has been detected in the heterologous expression study
development and evaluation of a method for the prediction of possible genes of orphan enzyme reactions where any associated gene sequences are not determined to date. The candidate enzyme gene of a reaction is detected using the chemical structures of the substrate-product pair (reactant pair). The proposed method is based on a search for similar reactant pairs in a reference database (KEGG database) and offers orthologeous groups that possibly mediate the given reaction. One example is the histidine transaminase (R01161, EC 2.6.1.38), which transfers an amino group from histidine to glutamate. For the query consisting of histidine and imidazol-5-pyruvate (RP01339 in the RPAIR database), K00817 is predicted by the method with the highest score (0.971). The function of this KO entry is the transfer of an amino group from phenylalanine, tyrosine, and histidinol phosphate (histidinol-phosphate transaminase, EC 2.6.1.9), which are structurally similar to histidine, to glutamate. In addition, this KO entry contains the enzyme gene sequence tte:TTE2137 of Thermoanaerobacter tengcongensis, for which a histidine transaminase activity has been detected in the heterologous expression study
development and evaluation of a method for the prediction of possible genes of orphan enzyme reactions where any associated gene sequences are not determined to date. The candidate enzyme gene of a reaction is detected using the chemical structures of the substrate-product pair (reactant pair). The proposed method is based on a search for similar reactant pairs in a reference database (KEGG database) and offers orthologeous groups that possibly mediate the given reaction. One example is the histidine transaminase (R01161, EC 2.6.1.38), which transfers an amino group from histidine to glutamate. For the query consisting of histidine and imidazol-5-pyruvate (RP01339 in the RPAIR database), K00817 is predicted by the method with the highest score (0.971). The function of this KO entry is the transfer of an amino group from phenylalanine, tyrosine, and histidinol phosphate (histidinol-phosphate transaminase, EC 2.6.1.9), which are structurally similar to histidine, to glutamate. In addition, this KO entry contains the enzyme gene sequence tte:TTE2137 of Thermoanaerobacter tengcongensis, for which a histidine transaminase activity has been detected in the heterologous expression study
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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
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
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)