| Function
Phosphoserine aminotransferase (PSAT) catalyzes the reversible conversion of phosphoserine and oxoglutarate to produce glutamate and 3-phosphonooxypyruvate. PSAT is part of the phosphoserine biosynthesis[1]. Pyridoxal phosphate (vitamin B6, PLP) is a cofactor of PAT.
Relevance
PSAT is over-expressed in colon tumors and increases their chemoresistance. PSAT1 inhibition is being tested as drug treatment[2].
Structural highlights
PSAT overall structure shows a small domain and a large one. The active site contains the PLP co-factor bound to lysine side chain[3]. Water molecules are shown as red spheres.
- ↑ Basurko MJ, Marche M, Darriet M, Cassaigne A. Phosphoserine aminotransferase, the second step-catalyzing enzyme for serine biosynthesis. IUBMB Life. 1999 Nov;48(5):525-9. PMID:10637769 doi:https://dx.doi.org/10.1080/713803557
- ↑ Vie N, Copois V, Bascoul-Mollevi C, Denis V, Bec N, Robert B, Fraslon C, Conseiller E, Molina F, Larroque C, Martineau P, Del Rio M, Gongora C. Overexpression of phosphoserine aminotransferase PSAT1 stimulates cell growth and increases chemoresistance of colon cancer cells. Mol Cancer. 2008 Jan 25;7:14. doi: 10.1186/1476-4598-7-14. PMID:18221502 doi:https://dx.doi.org/10.1186/1476-4598-7-14
- ↑ Dubnovitsky AP, Kapetaniou EG, Papageorgiou AC. Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus. Protein Sci. 2005 Jan;14(1):97-110. PMID:15608117 doi:14/1/97
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3D structures of phosphoserine aminotransferase
Phosphoserine aminotransferase 3D structures
References
