Adenosylmethionine—8-amino-7-oxononanoate transaminase
| adenosylmethionine-8-amino-7-oxononanoate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.6.1.62 | ||||||||
| CAS no. | 37259-71-5 | ||||||||
| 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 adenosylmethionine-8-amino-7-oxononanoate transaminase (EC 2.6.1.62) is an enzyme that catalyzes the chemical reaction
- S-adenosyl-L-methionine + 8-amino-7-oxononanoate S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Thus, the two substrates of this enzyme are S-adenosyl-L-methionine and 8-amino-7-oxononanoate, whereas its two products are S-adenosyl-4-methylthio-2-oxobutanoate and 7,8-diaminononanoate.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase. Other names in common use include 7,8-diaminonanoate transaminase, 7,8-diaminononanoate transaminase, DAPA transaminase, 7,8-diaminopelargonic acid aminotransferase, DAPA aminotransferase, 7-keto-8-aminopelargonic acid, diaminopelargonate synthase, and 7-keto-8-aminopelargonic acid aminotransferase. This enzyme participates in biotin metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
[edit]As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1DTY, 1MGV, 1MLY, 1MLZ, 1QJ3, 1QJ5, 1S06, 1S07, 1S08, 1S09, and 1S0A.
References
[edit]- Izumi Y, Sato K, Tani Y, Ogata K (1973). "Purification of 7-keto-8-aminopelargonic acid-7,8-diaminopelargonic acid aminotransferase, an enzyme involved in biotin synthesis, from Brevibacterium divaricatum". Agric. Biol. Chem. 37 (11): 2683–2684. doi:10.1271/bbb1961.37.2683.
- Izumi Y, Sato K, Tani Y, Ogata K (1975). "7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin synthesis by microorganisms". Agric. Biol. Chem. 39: 175–181. doi:10.1271/bbb1961.39.175.
- Stoner GL, Eisenberg MA (1973). "Purification and properties of 7,8-diaminopelargonic acid aminotransferase. An enzyme in the biotin biosynthetic pathway". J. Biol. Chem. 250: 4029–4036. doi:10.1016/S0021-9258(19)41381-1.
