Structural highlights
Publication Abstract from PubMed
l-Arabinose 1-dehydrogenase (AraDH) catalyzes the NAD(P)(+)-dependent oxidation of l-arabinose to L-arabinono-1,4-lactone in the non-phosphorylative l-arabinose pathway, and is classified into glucose-fructose oxidoreductase and short-chain dehydrogenase/reductase (SDR). We herein report the crystal structure of a SDR-type AraDH (from Herbaspirillum huttiense) for the first time. The interactions between Asp49 and the 2'- and 3'-hydroxyl groups of NAD(+) were consistent with strict specificity for NAD(+). In a binding model for the substrate, Ser155 and Tyr168, highly conserved in the SDR superfamily, interacted with the C1 and/or C2 hydroxyl(s) of l-arabinose, whereas interactions between Asp107, Arg109, and Gln206 and the C2 and/or C3 hydroxyl(s) were unique to AraDH. Trp200 significantly contributed to the selectivities of the C4 hydroxyl and C6 methyl of substrates.
Crystal structure of L-arabinose 1-dehydrogenase as a short-chain reductase/dehydrogenase protein.,Watanabe S, Yoshiwara K, Matsubara R, Watanabe Y Biochem Biophys Res Commun. 2022 Mar 8;604:14-21. doi:, 10.1016/j.bbrc.2022.03.028. PMID:35279441[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Watanabe S, Yoshiwara K, Matsubara R, Watanabe Y. Crystal structure of L-arabinose 1-dehydrogenase as a short-chain reductase/dehydrogenase protein. Biochem Biophys Res Commun. 2022 May 14;604:14-21. PMID:35279441 doi:10.1016/j.bbrc.2022.03.028
