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Reactivating chaperones for coenzyme B12-dependent diol and glycerol dehydratases and ethanolamine ammonia-lyase.
Toraya, Tetsuo; Tobimatsu, Takamasa; Shibata, Naoki; Mori, Koichi.
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  • Toraya T; Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka, Kita-ku, Okayama, Japan. Electronic address: toraya@cc.okayama-u.ac.jp.
  • Tobimatsu T; Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka, Kita-ku, Okayama, Japan.
  • Shibata N; Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo, Japan.
  • Mori K; Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka, Kita-ku, Okayama, Japan.
Methods Enzymol ; 668: 243-284, 2022.
Article en En | MEDLINE | ID: mdl-35589195
Adenosylcobalamin (AdoCbl) or coenzyme B12-dependent enzymes tend to undergo mechanism-based inactivation during catalysis or inactivation in the absence of substrate. Such inactivation may be inevitable because they use a highly reactive radical for catalysis, and side reactions of radical intermediates result in the damage of the coenzyme. How do living organisms address such inactivation when enzymes are inactivated by undesirable side reactions? We discovered reactivating factors for radical B12 eliminases. They function as releasing factors for damaged cofactor(s) from enzymes and thus mediate their exchange for intact AdoCbl. Since multiple turnovers and chaperone functions were demonstrated, they were renamed "reactivases" or "reactivating chaperones." They play an essential role in coenzyme recycling as part of the activity-maintaining systems for B12 enzymes. In this chapter, we describe our investigations on reactivating chaperones, including their discovery, gene cloning, preparation, characterization, activity assays, and mechanistic studies, that have been conducted using a wide range of biochemical and structural methods that we have developed.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Propanodiol Deshidratasa / Etanolamina Amoníaco-Liasa Idioma: En Revista: Methods Enzymol Año: 2022 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Propanodiol Deshidratasa / Etanolamina Amoníaco-Liasa Idioma: En Revista: Methods Enzymol Año: 2022 Tipo del documento: Article Pais de publicación: Estados Unidos