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UniProt functional annotation for Q76EQ0 | ||
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| UniProt code: Q76EQ0. |
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| Organism: | |
Rattus norvegicus (Rat). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus. |
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| Function: | |
Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine. {ECO:0000269|PubMed:16713567, ECO:0000269|PubMed:20106978}. |
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| Catalytic activity: | |
Reaction=L-serine = D-serine; Xref=Rhea:RHEA:10980, ChEBI:CHEBI:33384, ChEBI:CHEBI:35247; EC=5.1.1.18; Evidence={ECO:0000269|PubMed:20106978}; |
| Catalytic activity: | |
Reaction=D-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:13977, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; EC=4.3.1.18; Evidence={ECO:0000250|UniProtKB:Q9QZX7}; |
| Catalytic activity: | |
Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169, ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17; Evidence={ECO:0000250|UniProtKB:Q9QZX7}; |
| Cofactor: | |
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:20106978}; |
| Activity regulation: | |
Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP (By similarity). Competitively inhibited by malonate. {ECO:0000250, ECO:0000269|PubMed:20106978}. |
| Biophysicochemical properties: | |
Kinetic parameters: KM=3.7 mM for L-serine {ECO:0000269|PubMed:20106978}; |
| Subunit: | |
Homodimer. {ECO:0000269|PubMed:20106978}. |
| Ptm: | |
S-nitrosylated, leading to decrease the enzyme activity. {ECO:0000250}. |
| Similarity: | |
Belongs to the serine/threonine dehydratase family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.