title: Structural insights for the substrate recognition mechanism of LL-diaminopimelate aminotransferase.
abstract: The enzymes involved in the lysine biosynthetic pathway have long been considered to be attractive targets for novel antibiotics due to the absence of this pathway in humans. Recently, a novel pyridoxal 5'-phosphate (PLP) dependent enzyme called LL-diaminopimelate aminotransferase (LL-DAP-AT) was identified in the lysine biosynthetic pathway of plants and Chlamydiae. Understanding its function and substrate recognition mechanism would be an important initial step toward designing novel antibiotics targeting LL-DAP-AT. The crystal structures of LL-DAP-AT from Arabidopsis thaliana in complex with various substrates and analogues have been solved recently. These structures revealed how L-glutamate and LL-DAP are recognized by LL-DAP-AT without significant conformational changes in the enzyme's backbone structure. This review article summarizes the recent developments in the structural characterization and the inhibitor design of LL-DAP-AT from A. thaliana. This article is part of a Special Issue entitled: Pyridoxal Phospate Enzymology.
authors: Department of Biochemistry, School of Medicine and Systems Medicine, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada.
authors: Nobuhiko
authors: N
authors: Watanabe
authors: Michael N G
authors: MN
authors: James
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011487:Protein Conformation; D013379:Substrate Specificity; D000637:Transaminases / Q000737:chemistry / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; C561488:LL-diaminopimelate aminotransferase, Chlamydia trachomatis; D000637:Transaminases