Structure-function characterization of an aldo-keto reductase involved in detoxification of the mycotoxin, deoxynivalenol.

ABSTRACT: Deoxynivalenol (DON) is a mycotoxin, produced by filamentous fungi such as Fusarium graminearum, that causes significant yield losses of cereal grain crops worldwide. One of the most promising methods to detoxify this mycotoxin involves its enzymatic epimerization to 3-epi-DON. DepB plays a critical role in this process by reducing 3-keto-DON, an intermediate in the epimerization process, to 3-epi-DON. DepB_Rleg from Rhizobium leguminosarum is a member of the new aldo-keto reductase family, AKR18, and it has the unusual ability to utilize both NADH and NADPH as coenzymes, albeit with a 40-fold higher catalytic efficiency with NADPH compared to NADH. Structural analysis of DepB_Rleg revealed the putative roles of Lys-217, Arg-290, and Gln-294 in NADPH specificity. Replac

SUBMITTER: Abraham N 

PROVIDER: S-EPMC9427786 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature