Adenosylmethionine—8-amino-7-oxononanoate transaminase
| adenosylmethionine-8-amino-7-oxononanoate transaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.6.1.62 | ||||||||
| CAS number | 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 / EGO | ||||||||
| |||||||||
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
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
- 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: 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.