Following the electrons: peculiarities in the catalytic cycles of radical SAM enzymes.

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  • Author(s): Ruszczycky MW;Ruszczycky MW; Zhong A; Liu HW
  • Source:
    Natural product reports [Nat Prod Rep] 2018 Jul 18; Vol. 35 (7), pp. 615-621.
  • Publication Type:
    Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Review
  • Language:
    English
  • Additional Information
    • Source:
      Publisher: Royal Society of Chemistry Country of Publication: England NLM ID: 8502408 Publication Model: Print Cited Medium: Internet ISSN: 1460-4752 (Electronic) Linking ISSN: 02650568 NLM ISO Abbreviation: Nat Prod Rep Subsets: MEDLINE
    • Publication Information:
      Original Publication: [London, England] : Royal Society of Chemistry, c1984-
    • Subject Terms:
      Enzymes/*chemistry ; Enzymes/*metabolism ; S-Adenosylmethionine/*metabolism; Alkylation ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Carbon-Carbon Lyases/chemistry ; Carbon-Carbon Lyases/metabolism ; Carbon-Nitrogen Lyases/chemistry ; Carbon-Nitrogen Lyases/metabolism ; Catalysis ; Oxidation-Reduction
    • Abstract:
      Radical SAM enzymes use S-adenosyl-l-methionine as an oxidant to initiate radical-mediated transformations that would otherwise not be possible with Lewis acid/base chemistry alone. These reactions are either redox neutral or oxidative leading to certain expectations regarding the role of SAM as either a reusable cofactor or the ultimate electron acceptor during each turnover. However, these expectations are frequently not realized resulting in fundamental questions regarding the redox handling and movement of electrons associated with these biological catalysts. Herein we provide a focused perspective on several of these questions and associated hypotheses with an emphasis on recently discovered radical SAM enzymes.
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    • Grant Information:
      R01 GM035906 United States GM NIGMS NIH HHS; R01 GM040541 United States GM NIGMS NIH HHS; R37 GM035906 United States GM NIGMS NIH HHS
    • Accession Number:
      0 (Bacterial Proteins)
      0 (Enzymes)
      0 (LipA protein, Bacteria)
      7LP2MPO46S (S-Adenosylmethionine)
      EC 4.1.- (Carbon-Carbon Lyases)
      EC 4.1.- (S-adenosyl-L-methionine tryptophan lyase, Streptomyces actuosus)
      EC 4.3.- (Carbon-Nitrogen Lyases)
      EC 4.3.99.3 (7-carboxy-7-deazaguanine synthase, Burkholderia multivorans)
    • Publication Date:
      Date Created: 20180228 Date Completed: 20190430 Latest Revision: 20190718
    • Publication Date:
      20240829
    • Accession Number:
      PMC6051909
    • Accession Number:
      10.1039/c7np00058h
    • Accession Number:
      29485151