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Conserved Enzymatic Cascade for Bacterial Azoxy Biosynthesis.
Shi, Jingkun; Zang, Xin; Zhao, Zhijie; Shen, Zhuanglin; Li, Wei; Zhao, Guiyun; Zhou, Jiahai; Du, Yi-Ling.
Affiliation
  • Shi J; Department of Microbiology, and Department of Pharmacy of the Fourth Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Zang X; Key Laboratory of Quantitative Synthetic Biology, Shenzhen Institute of Synthetic Biology, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China.
  • Zhao Z; Department of Microbiology, and Department of Pharmacy of the Fourth Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Shen Z; Key Laboratory of Quantitative Synthetic Biology, Shenzhen Institute of Synthetic Biology, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China.
  • Li W; Department of Microbiology, and Department of Pharmacy of the Fourth Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Zhao G; Department of Microbiology, and Department of Pharmacy of the Fourth Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
  • Zhou J; Key Laboratory of Quantitative Synthetic Biology, Shenzhen Institute of Synthetic Biology, Shenzhen Institute of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China.
  • Du YL; Department of Microbiology, and Department of Pharmacy of the Fourth Affiliated Hospital, Zhejiang University School of Medicine, Hangzhou 310058, China.
J Am Chem Soc ; 145(49): 27131-27139, 2023 12 13.
Article in En | MEDLINE | ID: mdl-38018127
ABSTRACT
Azoxy compounds exhibit a wide array of biological activities and possess distinctive chemical properties. Although there has been considerable interest in the biosynthetic mechanisms of azoxy metabolites, the enzymatic basis responsible for azoxy bond formation has remained largely enigmatic. In this study, we unveil the enzyme cascade that constructs the azoxy bond in valanimycin biosynthesis. Our research demonstrates that a pair of metalloenzymes, comprising a membrane-bound hydrazine synthase and a nonheme diiron azoxy synthase, collaborate to convert an unstable pathway intermediate to an azoxy product through a hydrazine-azo-azoxy pathway. Additionally, by characterizing homologues of this enzyme pair from other azoxy metabolite pathways, we propose that this two-enzyme cascade could represent a conserved enzymatic strategy for azoxy bond formation in bacteria. These findings provide significant mechanistic insights into biological N-N bond formation and should facilitate the targeted isolation of bioactive azoxy compounds through genome mining.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacteria / Hydrazines Language: En Journal: J Am Chem Soc Year: 2023 Document type: Article Affiliation country:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacteria / Hydrazines Language: En Journal: J Am Chem Soc Year: 2023 Document type: Article Affiliation country: