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UniProt functional annotation for Q8N5Z0 | ||
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| UniProt code: Q8N5Z0. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro). {ECO:0000269|PubMed:18620547}. |
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| Catalytic activity: | |
Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L- glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.7; |
| Catalytic activity: | |
Reaction=2-oxoglutarate + L-2-aminoadipate = 2-oxoadipate + L- glutamate; Xref=Rhea:RHEA:12601, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57499, ChEBI:CHEBI:58672; EC=2.6.1.39; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:12126930, ECO:0000269|PubMed:18056995, ECO:0000269|PubMed:18056996}; |
| Activity regulation: | |
Kynurenine transaminase activity is competitively inhibited by aminoadipate, asparagine, glutamate, histidine, cysteine, lysine, 3-hydroxy-kynurenine and phenylalanine. {ECO:0000269|PubMed:18620547}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.9 mM for aminoadipate {ECO:0000269|PubMed:18620547}; KM=4.7 mM for kynurenine {ECO:0000269|PubMed:18620547}; KM=1.7 mM for methionine {ECO:0000269|PubMed:18620547}; KM=1.6 mM for glutamate {ECO:0000269|PubMed:18620547}; KM=1.8 mM for tyrosine {ECO:0000269|PubMed:18620547}; KM=1.2 mM for 2-oxoglutarate {ECO:0000269|PubMed:18620547}; KM=1.5 mM for 2-oxocaproic acid {ECO:0000269|PubMed:18620547}; KM=1.8 mM for phenylpyruvate {ECO:0000269|PubMed:18620547}; KM=1.4 mM for ino-3-pyruvate {ECO:0000269|PubMed:18620547}; pH dependence: Optimum pH is 7-9. {ECO:0000269|PubMed:18620547}; Temperature dependence: Optimum temperature is 50 degrees Celsius. {ECO:0000269|PubMed:18620547}; |
| Pathway: | |
Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 4/6. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:18056995, ECO:0000269|PubMed:18056996, ECO:0000269|PubMed:18620547}. |
| Subcellular location: | |
Mitochondrion {ECO:0000305}. |
| Tissue specificity: | |
Higher expression in the liver. Also found in heart, brain, kidney, pancreas, prostate, testis and ovary. |
| Miscellaneous: | |
[Isoform 1]: May be due to a competing donor splice site. |
| Similarity: | |
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.