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Structure and function relationship of formate dehydrogenases: an overview of recent progress.
Kobayashi, Ami; Taketa, Midori; Sowa, Keisei; Kano, Kenji; Higuchi, Yoshiki; Ogata, Hideaki.
Afiliación
  • Kobayashi A; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto 606-8502, Japan.
  • Taketa M; Graduate School of Science, University of Hyogo, Koto 3-2-1 Kamigori, Ako, Hyogo 678-1297, Japan.
  • Sowa K; Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Sakyo, Kyoto 606-8502, Japan.
  • Kano K; Office of Society Academia Collaboration for Innovation, Kyoto University, Gokasho, Uji 611-0011, Japan.
  • Higuchi Y; Graduate School of Science, University of Hyogo, Koto 3-2-1 Kamigori, Ako, Hyogo 678-1297, Japan.
  • Ogata H; Graduate School of Science, University of Hyogo, Koto 3-2-1 Kamigori, Ako, Hyogo 678-1297, Japan.
IUCrJ ; 10(Pt 5): 544-554, 2023 Sep 01.
Article en En | MEDLINE | ID: mdl-37668215
ABSTRACT
Formate dehydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions. Metal-dependent (Mo- or W-containing) FDHs from prokaryotic organisms belong to the superfamily of molybdenum enzymes and are members of the dimethylsulfoxide reductase family. In this short review, recent progress in the structural analysis of FDHs together with their potential biotechnological applications are summarized.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Biotecnología / Formiato Deshidrogenasas Idioma: En Revista: IUCrJ Año: 2023 Tipo del documento: Article País de afiliación: Japón

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Asunto principal: Biotecnología / Formiato Deshidrogenasas Idioma: En Revista: IUCrJ Año: 2023 Tipo del documento: Article País de afiliación: Japón