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UniProt functional annotation for Q71RI9 | ||
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| UniProt code: Q71RI9. |
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| Organism: | |
Mus musculus (Mouse). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus. |
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| 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:19029248). May catalyze 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:19029248). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro) (PubMed:19029248). {ECO:0000269|PubMed:19029248}. |
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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; Evidence={ECO:0000269|PubMed:19029248}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561; Evidence={ECO:0000305|PubMed:19029248}; |
| Catalytic activity: | |
Reaction=glyoxylate + L-kynurenine = glycine + H2O + kynurenate; Xref=Rhea:RHEA:65896, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.63; Evidence={ECO:0000269|PubMed:19029248}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65897; Evidence={ECO:0000305|PubMed:19029248}; |
| Catalytic activity: | |
Reaction=3-hydroxy-L-kynurenine + glyoxylate = glycine + H2O + xanthurenate; Xref=Rhea:RHEA:65900, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58125, ChEBI:CHEBI:71201; EC=2.6.1.63; Evidence={ECO:0000269|PubMed:19029248}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65901; Evidence={ECO:0000305|PubMed:19029248}; |
| 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:19029248}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122; Evidence={ECO:0000305|PubMed:19029248}; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:19029248}; |
| Activity regulation: | |
Kynurenine transamination is competitively inhibited by cysteine, glutamine, histidine, methionine, leucine, or phenylalanine. {ECO:0000269|PubMed:19029248}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.7 mM for glutamine {ECO:0000269|PubMed:19029248}; KM=0.7 mM for histidine {ECO:0000269|PubMed:19029248}; KM=0.7 mM for cysteine {ECO:0000269|PubMed:19029248}; KM=0.9 mM for methionine {ECO:0000269|PubMed:19029248}; KM=1.1 mM for phenylalanine {ECO:0000269|PubMed:19029248}; KM=1.4 mM for asparagine {ECO:0000269|PubMed:19029248}; KM=1.5 mM for kynurenine {ECO:0000269|PubMed:19029248}; KM=7.1 mM for tryptophan {ECO:0000269|PubMed:19029248}; KM=3.0 mM for serine {ECO:0000269|PubMed:19029248}; KM=0.4 mM for glyoxylate {ECO:0000269|PubMed:19029248}; KM=0.6 mM for phenylpyruvate {ECO:0000269|PubMed:19029248}; pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:19029248}; Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:19029248}; |
| Pathway: | |
Amino-acid degradation; L-kynurenine degradation; kynurenate from L-kynurenine: step 1/2. {ECO:0000269|PubMed:19029248}. |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:19029248}. |
| Tissue specificity: | |
Widely expressed, with higher expression levels in liver, kidney, heart and neuroendocrine tissues. {ECO:0000269|PubMed:16376499}. |
| Developmental stage: | |
Expressed from postnatal day (PND) 7 and peaks in adult. {ECO:0000269|PubMed:16376499}. |
| Similarity: | |
Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.