論文

査読有り 招待有り 国際誌
2022年

Reactivating chaperones for coenzyme B12-dependent diol and glycerol dehydratases and ethanolamine ammonia-lyase.

Methods in enzymology
  • Tetsuo Toraya
  • ,
  • Takamasa Tobimatsu
  • ,
  • Naoki Shibata
  • ,
  • Koichi Mori

668
開始ページ
243
終了ページ
284
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1016/bs.mie.2021.11.028

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.

リンク情報
DOI
https://doi.org/10.1016/bs.mie.2021.11.028
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/35589195
ID情報
  • DOI : 10.1016/bs.mie.2021.11.028
  • PubMed ID : 35589195

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