Mechanism-Based Strategies for Structural Characterization of Radical SAM Reaction Intermediates

Katherine M. Davis, Amie K. Boal

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations

Abstract

X-ray crystallographic characterization of enzymes at different stages in their reaction cycles can provide unique insight into the reaction pathway, the number and type of intermediates formed, and their structural context. The known mechanistic diversity in the radical S-adenosylmethionine (SAM) superfamily of enzymes makes it an appealing target for such studies as more than 100,000 sequences have been identified to date with wide-ranging reactivities that share a pattern of complex radical-mediated chemistry. Here, we review selected examples of radical SAM enzyme crystal structures representative of reactant, product, and intermediate state complexes with a particular emphasis on the strategies employed to capture these states. Broader application of structural characterization techniques to analyze mechanism and substrate specificity is certain to play an important role as more members of this family become tractable for biochemical study.

Original languageEnglish (US)
Title of host publicationMethods in Enzymology
PublisherAcademic Press Inc.
Pages331-359
Number of pages29
DOIs
StatePublished - Jan 1 2017

Publication series

NameMethods in Enzymology
Volume595
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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    Davis, K. M., & Boal, A. K. (2017). Mechanism-Based Strategies for Structural Characterization of Radical SAM Reaction Intermediates. In Methods in Enzymology (pp. 331-359). (Methods in Enzymology; Vol. 595). Academic Press Inc.. https://doi.org/10.1016/bs.mie.2017.07.008