L,L-diaminopimelate aminotransferase () is a pyridoxal phosphate-dependent enzyme that catalyzes the chemical reaction
The three substrates of this enzyme characterised from plants are (S)-2,3,4,5-tetrahydrodipicolinic acid (1), L-glutamic acid, and water. Its products are (S,S)-2,6-diaminopimelic acid a.k.a. L,L-diaminopimelic acid (2) and α-ketoglutaric acid. The product (2) goes on in a biosynthetic pathway leading to the amino acid lysine.
This enzyme is a transferases, specifically a transaminase, 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.
Structural studies As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References