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L,L-diaminopimelate aminotransferase : ウィキペディア英語版 | L,L-diaminopimelate aminotransferase
In enzymology, a L,L-diaminopimelate aminotransferase () is an enzyme that catalyzes the chemical reaction :LL-2,6-diaminoheptanedioate + 2-oxoglutarate (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + H2O Thus, the two substrates of this enzyme are LL-2,6-diaminoheptanedioate and 2-oxoglutarate, whereas its 3 products are (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, L-glutamate, and H2O. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase. Other names in common use include LL-diaminopimelate transaminase, LL-DAP aminotransferase, and LL-DAP-AT. This enzyme participates in lysine biosynthesis. ==Structural studies==
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
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