Journal
BIOORGANIC CHEMISTRY
Volume 32, Issue 5, Pages 326-340Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bioorg.2004.06.001
Keywords
S-Adenosylmethionine
Funding
- NIGMS NIH HHS [GM 59277] Funding Source: Medline
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The role of S-adenosylmethionine (SAM) as a precursor to organic radicals, generated by one-electron reduction of SAM and subsequent fission to form 5'-deoxyadenosyl radical and methionine, has been known for some time. Only recently, however, has it become apparent how widespread such enzymes are, and what a wide range of chemical reactions they catalyze. In the last few years several new SAM radical enzymes have been identified. Spectroscopic and kinetic investigations have begun to uncover the mechanism by which an iron sulfur cluster unique to these enzymes reduces SAM to generate adenosyl radical. Most recently, the first Xray structures of SAM radical enzymes, coproporphyrinogen-Ill oxidase, and biotin synthase have been solved, providing a structural framework within which to interpret mechanistic studies. (C) 2004 Elsevier Inc. All rights reserved.
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