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B6db activities: 2.6.1.52

2.6.1.52
Description Phosphoserine aminotransferase.
Alternative names L-phosphoserine aminotransferase;
Phosphohydroxypyruvic--glutamic transaminase;
PSAT;
3PHP transaminase;
Hydroxypyruvic phosphate--glutamic transaminase;
Phosphohydroxypyruvate transaminase.
Catalyzed 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
Cofactor Pyridoxal-phosphate.
Comments This enzyme catalyses the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli.
It also catalyses the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in Escherichia coli (using Reaction 2 above).
In Escherichia coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis. Non-phosphorylated forms of serine and threonine are not substrates.
Diseases Phosphoserine aminotransferase deficiency
Prosite PROSITE; PDOC00514;
PDB 1BT4; 1BJO; 1BJN;
Organisms -Eubacteria -Archea -Plants -Fungi -Metazoa -Human
 

Family 

2.6.1.52 (40)
 
Links Enzyme (activities) 2.6.1.52
BRENDA (activities) 2.6.1.52
KEGG (pathways) 2.6.1.52
PLPMDB (PLP mutants) 2.6.1.52
 
References
 Ali V, Nozaki T. (2006) Biochemical and functional characterization of phosphoserine aminotransferase from Entamoeba histolytica, which possesses both phosphorylated and non-phosphorylated serine metabolic pathways Mol Biochem Parasitol 145 :71-83.

 Dubnovitsky A.P.; Kapetaniou, E.G.; Papageorgiou, A.C. (2005) Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus Protein Sci 14 97-110.

 Baek, J.Y.; Jun do, Y.; Taub, D.; Kim, Y.H. (2003) Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis Biochem J 373 191-200.

 Hester, G.; Stark, W.; Moser, M.; Kallen, J.; Markovic-Housley, Z.; Jansonius, J. N. (1999) Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 A resolution: comparison of the unligated enzyme and a complex with alpha-methyl-l-glutamate J Mol Biol 286 829-50.

 Saito, K.; Takagi, Y.; Ling, H.C.; Takahashi, H.; Noji, M. (1997) Molecular cloning, characterization and expression of cDNA encoding phosphoserine aminotransferase involved in phosphorylated pathway of serine biosynthesis from spinach Plant Mol Biol 33 359-66.

 Battchikova, N.; Himanen, J. P.; Ahjolahti, M.; Korpela, T. (1996) Phosphoserine aminotransferase from Bacillus circulans subsp. alkalophilus: purification, gene cloning and sequencing Biochim Biophys Acta 1295 187-94.

 Metcalf, W.W.; Zhang, J.K.; Shi, X.; Wolfe, R.S. (1996) Molecular, genetic, and biochemical characterization of the serC gene of Methanosarcina barkeri Fusaro J Bacteriol 178 5797-802.

Articles on 2.6.1.52
 
last changed 2010/03/11 16:23

B6db activities