Serine–pyruvate transaminase () is a pyridoxal phosphate-dependent enzyme that catalyzes the chemical reaction
The two substrates of this enzyme first characterised from plants are -serine and pyruvic acid. Its products are hydroxypyruvic acid and -alanine.
This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is -serine:pyruvate aminotransferase. Other names in common use include SPT, and hydroxypyruvate:-alanine transaminase. This enzyme participates in glycine, serine and threonine metabolism.
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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