Structural highlights
Publication Abstract from PubMedRecombinant NAD(+)-dependent ribitol dehydrogenase derived from Klebsiella oxytoca (KoRdh) exhibits activity toward both ribitol and allitol. KoRdh catalyzes the NAD(+)-dependent oxidation of allitol to d-allulose and the NADH-dependent reduction of d-allulose to allitol. Notably, the flexible loop of KoRdh undergoes conformational changes upon NAD(+) and substrate binding. To elucidate the flexible loop's role in substrate recognition, we determined the X-ray structures of KoRdh alone and in complexes with NAD(+), d-allulose, or d-allose. Although d-allose is an aldose and not a substrate of KoRdh, it binds to KoRdh in the pyranose form, revealing the location of the substrate-binding site. Based on these structures, we propose a substrate recognition mechanism for KoRdh. Impact statement This research reveals an insight into a substrate recognition mechanism in the flexible region of ribitol dehydrogenase. Because ribitol dehydrogenase is a member of the short-chain reductases/oxidases (SDR) family, the current study will provide further insight into related enzymes that harbor the flexible region. Crystal structures of Klebsiella oxytoca ribitol dehydrogenase in complex with NAD(+), d-allose, or d-allulose reveal insight into substrate recognition.,Yoshida H, Matsumoto M, Yamamoto N, Yoshihara A, Izumori K, Kamitori S FEBS Lett. 2026 Apr 21. doi: 10.1002/1873-3468.70345. PMID:42015598[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 08:31, 29 April 2026.