Adenosylmethionine—8-amino-7-oxononanoate transaminase

In enzymology, an adenosylmethionine-8-amino-7-oxononanoate transaminase is an enzyme that catalyzes the chemical reaction


 * S-adenosyl-L-methionine + 8-amino-7-oxononanoate $$\rightleftharpoons$$ 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, , , , , , , , , , and.