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Serine—pyruvate transaminase : ウィキペディア英語版 | Serine—pyruvate transaminase
In enzymology, a serine-pyruvate transaminase () is an enzyme that catalyzes the chemical reaction :L-serine + pyruvate 3-hydroxypyruvate + L-alanine Thus, the two substrates of this enzyme are L-serine and pyruvate, whereas its two products are 3-hydroxypyruvate and L-alanine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-serine:pyruvate aminotransferase. Other names in common use include SPT, and hydroxypyruvate:L-alanine transaminase. This enzyme participates in glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate. ==Structural studies==
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
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