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2.6.1.52 |
| Description |
Phosphoserine aminotransferase. |
| Alternative names |
L-phosphoserine aminotransferase.
Phosphohydroxypyruvic--glutamic transaminase.
PSAT.
3PHP transaminase.
Hydroxypyruvic phosphate--glutamic transaminase.
Phosphohydroxypyruvate transaminase.
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| 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 |
-Bacteria -Archea -Plants -Fungi -Metazoa -Human |
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| 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
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| 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. |
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| last changed |
2007/12/05 18:17 |
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