, an adenosylmethionine-8-amino-7-oxononanoate transaminase
is an enzyme
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.
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , , , , , and .
- Izumi Y, Sato K, Tani Y and Ogata K "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.
- Izumi Y, Sato K, Tani Y and Ogata K "7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin synthesis by microorganisms". Agric. Biol. Chem. 39 175–181.
- Stoner GL and Eisenberg MA "Purification and properties of 7,8-diaminopelargonic acid aminotransferase. An enzyme in the biotin biosynthetic pathway". J. Biol. Chem. 250 4029–4036.
- The CAS registry number for this enzyme class is .
Gene Ontology (GO) codes