Phosphoserine transaminase

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
Phosphoserine transaminase
EC no.
CAS no.9030-90-4
IntEnzIntEnz view
ExPASyNiceZyme view
MetaCycmetabolic pathway
PDB structuresRCSB PDB PDBe PDBsum

Phosphoserine transaminase (EC, 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) is an enzyme with systematic name O-phospho-L-serine:2-oxoglutarate aminotransferase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

(1) O-phospho-L-serine + 2-oxoglutarate 3-phosphonooxypyruvate + L-glutamate
(2) 4-phosphonooxy-L-threonine + 2-oxoglutarate (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate

This enzyme is a pyridoxal-phosphate protein.

See also[edit]


  1. ^ Hirsch H, Greenberg DM (May 1967). "Studies on phosphoserine aminotransferase of sheep brain". The Journal of Biological Chemistry. 242 (9): 2283–7. PMID 6022873.
  2. ^ Pizer LI (December 1963). "The pathway and control of serine biosynthesis in Escherichia coli". The Journal of Biological Chemistry. 238: 3934–44. PMID 14086727.
  3. ^ Zhao G, Winkler ME (January 1996). "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". Journal of Bacteriology. 178 (1): 232–9. PMC 177644. PMID 8550422.
  4. ^ Drewke C, Klein M, Clade D, Arenz A, Müller R, Leistner E (July 1996). "4-O-phosphoryl-L-threonine, a substrate of the pdxC(serC) gene product involved in vitamin B6 biosynthesis". FEBS Letters. 390 (2): 179–82. doi:10.1016/0014-5793(96)00652-7. PMID 8706854.
  5. ^ Zhao G, Winkler ME (January 1996). "4-Phospho-hydroxy-L-threonine is an obligatory intermediate in pyridoxal 5'-phosphate coenzyme biosynthesis in Escherichia coli K-12". FEMS Microbiology Letters. 135 (2–3): 275–80. doi:10.1111/j.1574-6968.1996.tb08001.x. PMID 8595869.

External links[edit]