2.6.1.52: phosphoserine transaminase
This is an abbreviated version!
For detailed information about phosphoserine transaminase, go to the full flat file.
Reaction
Synonyms
3-O-phospho-L-serine:2-oxoglutarate aminotransferase, 3-phosphoserine aminotransferase, AspAT, AtPSAT, AtPSAT1, BCIR PSAT, bmPSAT, EhPSAT, hydroxypyruvic phosphate-glutamic transaminase, L-phosphoserine aminotransferase, phosphohydroxypyruvate transaminase, phosphohydroxypyruvic-glutamic transaminase, phosphoserine aminotransferase, phosphoserine aminotransferase 1, phosphoserine aminotransferase1, phosphoserine aminotransferase2, phosphoserine aminotransferases, PSAT, PSAT alpha, PSAT beta, PSAT-BALC, PSAT-BCIRA, PSAT-ECOLI, PSAT1, PSAT2, PSerAT, serC, sll1559
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Subunits
Subunits on EC 2.6.1.52 - phosphoserine transaminase
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dimer
homodimer
additional information
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x * 39500-40500, recombinant enzyme, SDS-PAGE, x * 40200, about, sequence calculation
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x * 40199, sequence calculation, x * 66000, recombinant SUMO-His6-tagged enzyme, SDS-PAGE
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Bombyx mori b94
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x * 40199, sequence calculation, x * 66000, recombinant SUMO-His6-tagged enzyme, SDS-PAGE
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?
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x * 40199, sequence calculation, x * 66000, recombinant SUMO-His6-tagged enzyme, SDS-PAGE
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homodimer
2 * 39000-40000, SDS-PAGE, 2 * 39834, sequence calculation
homodimer
2 * 38000-39800, recombinant enzyme mutant K2G, SDS-PAGE, 2 * 39793, sequence calculation
the crystal asymmetric unit with four subunits represents two functional AtPSAT1 dimers. The subunit of AtPSAT1 consists of two domains with mixed alpha/beta topology. This is a typical fold of class IV of the alpha-type aminotransferases with a much larger N-terminal catalytic domain and a smaller C-terminal domain. Hydrophobic core of the N-terminal domain is constituted by a seven-stranded beta-sheet with one anti-parallel strand. Subunit structure model, overview
additional information
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the crystal asymmetric unit with four subunits represents two functional AtPSAT1 dimers. The subunit of AtPSAT1 consists of two domains with mixed alpha/beta topology. This is a typical fold of class IV of the alpha-type aminotransferases with a much larger N-terminal catalytic domain and a smaller C-terminal domain. Hydrophobic core of the N-terminal domain is constituted by a seven-stranded beta-sheet with one anti-parallel strand. Subunit structure model, overview
additional information
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enzyme forms a protein-protein complex with D-phosphoglycerate dehydrogenase, which has a 1:1 stoichiometry. Ionic interactions play a significant role in complex formation and stability. The nucleotide binding domain of D-phosphoglycerate dehydrogenase specifically interacts with the enzyme. The purified nucleotide binding domain of D-phosphoglycerate dehydrogenase interacts with phosphoserine transaminase. The reactions catalyzed by the complex suggest a possibility of substrate channelling in the protein complex