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Transferases;
Transferring nitrogenous groups;
Transaminases
O-phospho-L-serine:2-oxoglutarate aminotransferase
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].
EC 2.6.1.52 created 1972, modified 2006
| Glycine, serine and threonine metabolism |
| Cysteine and methionine metabolism |
| Biosynthesis of secondary metabolites |
| Microbial metabolism in diverse environments |
| phosphoserine aminotransferase |
PIZER LI.
THE PATHWAY AND CONTROL OF SERINE BIOSYNTHESIS IN ESCHERICHIA COLI.
J Biol Chem 238:3934-44 (1963)
Hirsch H, Greenberg DM.
Studies on phosphoserine aminotransferase of sheep brain.
J Biol Chem 242:2283-7 (1967)
Zhao G, Winkler ME
A novel alpha-ketoglutarate reductase activity of the serA-encoded 3-phosphoglycerate dehydrogenase of Escherichia coli K-12 and its possible implications for human 2-hydroxyglutaric aciduria.
Drewke C, Klein M, Clade D, Arenz A, Muller R, Leistner E.
4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis.
Zhao G, Winkler ME.
4-Phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5′-phosphate coenzyme biosynthesis in Escherichia coli K-12.
Baek JY, Jun DY, Taub D, Kim YH
Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis.
Helgadottir S, Rosas-Sandoval G, Soll D, Graham DE
Biosynthesis of phosphoserine in the Methanococcales.
| 2.6.1.52 |
| 2.6.1.52 |
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