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Crystal structure of l ‐rhamnose 1‐dehydrogenase involved in the nonphosphorylative pathway of l ‐rhamnose metabolism in bacteria
Author(s) -
Yoshiwara Kentaroh,
Watanabe Seiya,
Watanabe Yasunori
Publication year - 2021
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.14046
Subject(s) - nad+ kinase , rhamnose , oxidoreductase , dehydrogenase , chemistry , stereochemistry , biochemistry , cofactor , azotobacter vinelandii , enzyme , polysaccharide , organic chemistry , nitrogenase , nitrogen fixation , nitrogen
Several microorganisms can utilize l ‐rhamnose as a carbon and energy source through the nonphosphorylative 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 Å 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.