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

Watanabe, Seiya ; Yoshiwara, Kentaroh ; Matsubara, Ryo ; Watanabe, Yasunori

Biochemical and biophysical research communications, 2022-05, Vol.604, p.14-21 [Periódico revisado por pares]

United States: Elsevier Inc

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  • Título:
    Crystal structure of L-arabinose 1-dehydrogenase as a short-chain reductase/dehydrogenase protein
  • Autor: Watanabe, Seiya ; Yoshiwara, Kentaroh ; Matsubara, Ryo ; Watanabe, Yasunori
  • Assuntos: Arabinose - chemistry ; Coenzyme specificity ; Crystal structure ; L-Arabinose 1-dehydrogenase ; Molecular evolution ; NAD - metabolism ; Oxidoreductases - metabolism ; Short Chain Dehydrogenase-Reductases - metabolism ; Short-chain dehydrogenase/reductase ; Substrate Specificity
  • É parte de: Biochemical and biophysical research communications, 2022-05, Vol.604, p.14-21
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
  • Descrição: 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. •l-Arabinose 1-dehydrogenase belongs to short-chain dehydrogenase/reductase (SDR) protein superfamily.•Crystal structure in complex with NAD+ was herein reported.•Active sites including a catalytic base differed from those of other SDR members.•The novel structure is helpful for understanding of catalysis and molecular evolution.
  • Editor: United States: Elsevier Inc
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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