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Your query returned 1 entry. Printable version
EC | 2.6.1.52 | ||||||||||||||
Accepted name: | phosphoserine transaminase | ||||||||||||||
Reaction: | (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphooxypyruvate + L-glutamate (2) 4-phosphooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + L-glutamate |
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For diagram of EC 2.6.1, click here, for diagram of serine biosynthesis, click here and for diagram of pyridoxal biosynthesis, click here | |||||||||||||||
Other name(s): | PSAT; phosphoserine aminotransferase; 3-phosphoserine aminotransferase; hydroxypyruvic phosphate-glutamic transaminase; L-phosphoserine aminotransferase; phosphohydroxypyruvate transaminase; phosphohydroxypyruvic-glutamic transaminase; 3-O-phospho-L-serine:2-oxoglutarate aminotransferase; SerC; PdxC; 3PHP transaminase | ||||||||||||||
Systematic name: | O-phospho-L-serine:2-oxoglutarate aminotransferase | ||||||||||||||
Comments: | A pyridoxal 5′-phosphate protein. This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis [1,3] and the third step in pyridoxal 5′-phosphate biosynthesis in the bacterium Escherichia coli [3]. Pyridoxal 5′-phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis [4]. Non-phosphorylated forms of serine and threonine are not substrates [4]. The archaeal enzyme has a relaxed specificity and can act on L-cysteate and L-alanine as alternative substrates to O-phospho-L-serine [7]. | ||||||||||||||
Links to other databases: | BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-90-4 | ||||||||||||||
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