Biology:Alanine—glyoxylate transaminase
| alanine-glyoxylate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Alanine-glyoxylate transaminase dimer, Human | |||||||||
| Identifiers | |||||||||
| EC number | 2.6.1.44 | ||||||||
| CAS number | 9015-67-2 | ||||||||
| 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-glyoxylate transaminase (EC 2.6.1.44) is an enzyme that catalyzes the chemical reaction
- L-alanine + glyoxylate [math]\displaystyle{ \rightleftharpoons }[/math] pyruvate + glycine
Thus, the two substrates of this enzyme are L-alanine and glyoxylate, whereas its two products are pyruvate and glycine.
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:glyoxylate aminotransferase. Other names in common use include AGT, alanine-glyoxylate aminotransferase, alanine-glyoxylic aminotransferase, and L-alanine-glycine transaminase. This enzyme participates in alanine and aspartate metabolism and glycine, serine and threonine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1H0C, 1J04, 1VJO, 2BKW, 2HUF, 2HUI, and 2HUU.
References
- "Characteristics of hepatic alanine-glyoxylate aminotransferase in different mammalian species". Biochem. J. 169 (1): 113–22. 1978. doi:10.1042/bj1690113. PMID 629740.
- "Co-purification of alanine-glyoxylate aminotransferase with 2-aminobutyrate aminotransferase in rat kidney". Biochim. Biophys. Acta 715 (1): 97–104. 1982. doi:10.1016/0304-4165(82)90054-x. PMID 6803844.
- "Isolation and characterization of an L-alanine: glyoxylate aminotransferase from human liver". J. Biol. Chem. 242 (16): 3614–9. 1967. doi:10.1016/S0021-9258(18)95853-9. PMID 6038488.
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