Phosphoserine aminotransferase
From Proteopedia
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| - | {{STRUCTURE_1bjo| PDB=1bjo | SIZE=400| SCENE= |right|CAPTION=E. coli phosphoserine aminotransferase complex with pyridoxal phosphate and glutamate [[1bjo]] }} | + | {{STRUCTURE_1bjo| PDB=1bjo | SIZE=400| SCENE= |right|CAPTION=E. coli phosphoserine aminotransferase dimer complex with pyridoxal phosphate and glutamate [[1bjo]] }} |
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Revision as of 09:27, 12 November 2012
Phosphoserine aminotransferase (PSAT) catalyzes the reversible conversion of phosphoserine and oxoglutarate to produce glutamate and 3-phosphonooxypyruvate. PSAT is part of the phosphoserine biosynthesis. Pyridoxal phosphate (vitamin B6, PLP) is a cofactor of PAT. PSAT is over-expressed in colon tumors and its inhibition is being tested as drug treatment.
3D structures of phosphoserine aminotransferase
3m5u – PSAT – Campylobacter jejuni
3qm2 – PSAT – Salmonella enterica
Phosphoserine aminotransferase complex with pyridoxal phosphate
1bt4, 1w3u, 2c0r – PSAT (mutant) + PLP – Bacillus circulans
1bjn – EcPSAT + PLP – Escherichia coli
1w23, 2bhx, 2bi1, 2bi2, 2bi3, 2bi5, 2bi9, 2bia, 2bie, 2big - PSAT + PLP – Bacillus alcalophilus
3e77 – PSAT + PLP – human
3ffr – PSAT + PLP – Cytophaga hutchinsonii
3qbo – PSAT + PLP
Phosphoserine aminotransferase ternary complex
1bjo - EcPSAT + α-methyl-glutamate + PLP
