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Adenosylmethionine—8-amino-7-oxononanoate transaminase
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Adenosylmethionine—8-amino-7-oxononanoate transaminase : ウィキペディア英語版
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 .

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