L,L-diaminopimelate aminotransferase explained

L,L-diaminopimelate aminotransferase
Ec Number:	2.6.1.83
Go Code:	0010285

In enzymology, a L,L-diaminopimelate aminotransferase is an enzyme that catalyzes the chemical reaction

LL-2,6-diaminoheptanedioate + 2-oxoglutarate

\rightleftharpoons (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 .

References

• Hudson AO, Singh BK, Leustek T, Gilvarg C . 2006 . An LL-diaminopimelate aminotransferase defines a novel variant of the lysine biosynthesis pathway in plants . Plant Physiol. . 140 . 292 - 301 . 16361515 . 10.1104/pp.105.072629 . 1 . 1326051 .