Serine—pyruvate transaminase

In enzymology, a serine-pyruvate transaminase (EC 2.6.1.51) is an enzyme that catalyzes the chemical reaction

L-serine + pyruvate ${\displaystyle \rightleftharpoons }$ 3-hydroxypyruvate + L-alanine

serine-pyruvate transaminase
Serine-pyruvate transaminase dimer, Human
Identifiers
EC no.	2.6.1.51
CAS no.	9030-88-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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 1J04.