alanine-oxomalonate transaminase | |||||||||
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Identifiers | |||||||||
EC no. | 2.6.1.47 | ||||||||
CAS no. | 37277-96-6 | ||||||||
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, an alanine-oxomalonate transaminase (EC 2.6.1.47) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are L-alanine and oxomalonate, whereas its two products are pyruvate and aminomalonate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-alanine:oxomalonate aminotransferase. Other names in common use include alanine-oxomalonate aminotransferase, L-alanine-ketomalonate transaminase, and alanine-ketomalonate (mesoxalate) transaminase. It employs one cofactor, pyridoxal phosphate.
Alanine transaminase (ALT) is a transaminase enzyme. It is also called alanine aminotransferase and was formerly called serum glutamate-pyruvate transaminase or serum glutamic-pyruvic transaminase (SGPT) and was first characterized in the mid-1950s by Arthur Karmen and colleagues. ALT is found in plasma and in various body tissues but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST level, and their ratio are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels.
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.
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