Phosphoserine transaminase

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Phosphoserine transaminase
Identifiers
EC number 2.6.1.52
CAS number 9030-90-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Phosphoserine transaminase (EC 2.6.1.52, 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]

References[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 177644Freely accessible. 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]