7b81

Publication Abstract from PubMed

Several microorganisms can utilize L-rhamnose as a carbon and energy source through the non-phosphorylative metabolic pathway, in which L-rhamnose 1-dehydrogenase (RhaDH) catalyzes the NAD(P)(+) -dependent oxidization of L-rhamnose to L-rhamnono-1,4-lactone. We herein investigated the crystal structures of RhaDH from Azotobacter vinelandii in ligand-free, NAD(+) -bound, NADP(+) -bound, and L-rhamnose- and NAD(+) -bound forms at 1.9, 2.1, 2.4, and 1.6 A resolution, respectively. The significant interactions with the 2'-phosphate group of NADP(+) , but not the 2'-hydroxyl group of NAD(+) , were consistent with a preference for NADP(+) over NAD(+) . The C5-OH and C6-methyl groups of L-rhamnose were recognized by specific residues of RhaDH through hydrogen bonds and hydrophobic contact, respectively, which contribute to the different substrate specificities from other aldose 1-dehydrogenases in the short-chain dehydrogenase/reductase superfamily.

Crystal structure of L-rhamnose 1-dehydrogenase involved in the non-phosphorylative pathway of L-rhamnose metabolism in bacteria.,Yoshiwara K, Watanabe S, Watanabe Y FEBS Lett. 2021 Jan 22. doi: 10.1002/1873-3468.14046. PMID:33482017^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.