S-adenosylmethionine radical enzymes.
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 X-ray structures of SAM radical enzymes, coproporphyrinogen-III oxidase, and biotin synthase have been solved, providing a structural framework within which to interpret mechanistic studies.
Marsh
E Neil G
EN
Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA. nmarsh@umich.edu
Patwardhan
Anjali
A
Huhta
Marja S
MS
D003304:Coproporphyrinogen Oxidase / Q000737:chemistry / Q000378:metabolism; D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D005609:Free Radicals; D007700:Kinetics; D008958:Models, Molecular; D008968:Molecular Conformation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012436:S-Adenosylmethionine / Q000737:chemistry / Q000378:metabolism*; D013466:Sulfurtransferases / Q000737:chemistry / Q000378:metabolism
D004798:Enzymes; D005609:Free Radicals; D012436:S-Adenosylmethionine; D003304:Coproporphyrinogen Oxidase; D013466:Sulfurtransferases; C057985:biotin synthetase