Structures of Medicago truncatula L-Histidinol Dehydrogenase Show Rearrangements Required for NAD⁺ Binding and the Cofactor Positioned to Accept a Hydride.

ABSTRACT: Plants, lower eukaryotes, bacteria, and archaebacteria synthesise L-histidine (His) in a similar, multistep pathway that is absent in mammals. This makes the His biosynthetic route a promising target for herbicides, antifungal agents, and antibiotics. The last enzyme of the pathway, bifunctional L-histidinol dehydrogenase (HDH, EC 1.1.1.23), catalyses two oxidation reactions: from L-histidinol (HOL) to L-histidinaldehyde and from L-histidinaldehyde to His. Over the course of the reaction, HDH utilises two molecules of NAD⁺ as the hydride acceptor. The object of this study was the HDH enzyme from the model legume plant, Medicago truncatula (MtHDH). Three crystal structures complexed with imidazole, HOL, and His with NAD⁺ provided in-depth insights into the enzyme archi

SUBMITTER: Ruszkowski M 

PROVIDER: S-EPMC5585171 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature