Crystal structure of L-arabinose 1-dehydrogenase as a short-chain reductase/dehydrogenase protein

Biochem Biophys Res Commun. 2022 May 14:604:14-21. doi: 10.1016/j.bbrc.2022.03.028. Epub 2022 Mar 8.


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.

Keywords: Coenzyme specificity; Crystal structure; L-Arabinose 1-dehydrogenase; Molecular evolution; Short-chain dehydrogenase/reductase; Substrate specificity.

MeSH terms

  • Arabinose* / chemistry
  • NAD / metabolism
  • Oxidoreductases / metabolism
  • Short Chain Dehydrogenase-Reductases* / metabolism
  • Substrate Specificity


  • NAD
  • Arabinose
  • Oxidoreductases
  • Short Chain Dehydrogenase-Reductases