|
|
||
|
|
|
|
|
UniProt functional annotation for Q16773 | ||
|
|
|
|
|
|
||
| UniProt code: Q16773. |
|
||
| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
|
||
|
||
| Function: | |
Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in the tryptophan catabolic pathway which is also a broad spectrum antagonist of the three ionotropic excitatory amino acid receptors among others (PubMed:19338303, PubMed:28097769). Also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites (PubMed:7883047). Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (PubMed:7883047). {ECO:0000269|PubMed:19338303, ECO:0000269|PubMed:28097769, ECO:0000269|PubMed:7883047}. |
|
||
| 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; Evidence={ECO:0000269|PubMed:19338303, ECO:0000269|PubMed:28097769}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561; Evidence={ECO:0000305|PubMed:19338303}; |
| Catalytic activity: | |
Reaction=3-phenylpyruvate + L-glutamine = 2-oxoglutaramate + L- phenylalanine; Xref=Rhea:RHEA:17593, ChEBI:CHEBI:16769, ChEBI:CHEBI:18005, ChEBI:CHEBI:58095, ChEBI:CHEBI:58359; EC=2.6.1.64; Evidence={ECO:0000269|PubMed:7883047}; |
| Catalytic activity: | |
Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) + pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13; Evidence={ECO:0000269|PubMed:7883047}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122; Evidence={ECO:0000305|PubMed:7883047}; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:15364907}; |
| Activity regulation: | |
Inhibited by tryptophan, indole-3-pyruvic acid, 3- indolepropionic acid, DL-indole-3-lactic acid, indole-3-acetic acid (IAC), amino-oxyacetate (AOAA), aminooxy-phenylpropionic acid (AOPP) and Tris. {ECO:0000269|PubMed:19338303}. |
| Pathway: | |
Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2. {ECO:0000269|PubMed:19338303, ECO:0000269|PubMed:28097769}. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:15364907, ECO:0000269|PubMed:19338303, ECO:0000269|PubMed:28097769}. |
| Subcellular location: | |
Cytoplasm, cytosol {ECO:0000269|PubMed:7883047}. |
| Similarity: | |
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.