| alanine-oxo-acid transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.12 | ||||||||
| CAS no. | 9030-41-5 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an alanine-oxo-acid transaminase ( EC 2.6.1.12) is an enzyme that catalyzes the chemical reaction
- L-alanine + a 2-oxo acid pyruvate + an L-amino acid
Thus, the two substrates of this enzyme are L-alanine and 2-oxo acid, whereas its two products are pyruvate and L-amino acid.
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:2-oxo-acid aminotransferase. Other names in common use include L-alanine-alpha-keto acid aminotransferase, leucine-alanine transaminase, alanine-keto acid aminotransferase, and alanine-oxo acid aminotransferase. This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, pyridoxal phosphate.
References
- ALTENBERN RA, HOUSEWRIGHT RD (1953). "Transaminases in smooth Brucella abortus, strain 19" (PDF). J. Biol. Chem. 204 (1): 159â67. PMID 13084587.
- Rowsell EV (1956). "Transaminations with pyruvate and other alpha-keto acids". Biochem. J. 64 (2): 246â252. PMC 1199724. PMID 13363834.
- Sallach HJ (1956). "Formation of serine from hydroxypyruvate and L-alanine" (PDF). J. Biol. Chem. 223 (2): 1101â1108.
- Wilson DG, King KW, Burris RH (1954). "Transaminase reactions in plants" (PDF). J. Biol. Chem. 208 (2): 863â874.
| alanine-oxo-acid transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.12 | ||||||||
| CAS no. | 9030-41-5 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an alanine-oxo-acid transaminase ( EC 2.6.1.12) is an enzyme that catalyzes the chemical reaction
- L-alanine + a 2-oxo acid pyruvate + an L-amino acid
Thus, the two substrates of this enzyme are L-alanine and 2-oxo acid, whereas its two products are pyruvate and L-amino acid.
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:2-oxo-acid aminotransferase. Other names in common use include L-alanine-alpha-keto acid aminotransferase, leucine-alanine transaminase, alanine-keto acid aminotransferase, and alanine-oxo acid aminotransferase. This enzyme participates in alanine and aspartate metabolism. It employs one cofactor, pyridoxal phosphate.
References
- ALTENBERN RA, HOUSEWRIGHT RD (1953). "Transaminases in smooth Brucella abortus, strain 19" (PDF). J. Biol. Chem. 204 (1): 159â67. PMID 13084587.
- Rowsell EV (1956). "Transaminations with pyruvate and other alpha-keto acids". Biochem. J. 64 (2): 246â252. PMC 1199724. PMID 13363834.
- Sallach HJ (1956). "Formation of serine from hydroxypyruvate and L-alanine" (PDF). J. Biol. Chem. 223 (2): 1101â1108.
- Wilson DG, King KW, Burris RH (1954). "Transaminase reactions in plants" (PDF). J. Biol. Chem. 208 (2): 863â874.