serine-pyruvate transaminase | |||||||||
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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 | ||||||||
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In enzymology, a serine-pyruvate transaminase (EC 2.6.1.51) is an enzyme that catalyzes the chemical reaction
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.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1J04.
Transaminases or aminotransferases are enzymes that catalyze a transamination reaction between an amino acid and an α-keto acid. They are important in the synthesis of amino acids, which form proteins.
Amino acid biosynthesis is the set of biochemical processes by which the amino acids are produced. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesize all amino acids. For example, humans can synthesize 11 of the 20 standard amino acids. These 11 are called the non-essential amino acids.
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