Complex biotransformations catalyzed by radical S-adenosylmethionine enzymes.

Qi Zhang, Wen Liu

Journal: The Journal of biological chemistry 2011;286(35):30245-30252

PMID: 21771780

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Abstract

The radical S-adenosylmethionine (AdoMet) superfamily currently comprises thousands of proteins that participate in numerous biochemical processes across all kingdoms of life. These proteins share a common mechanism to generate a powerful 5'-deoxyadenosyl radical, which initiates a highly diverse array of biotransformations. Recent studies are beginning to reveal the role of radical AdoMet proteins in the catalysis of highly complex and chemically unusual transformations, e.g. the ThiC-catalyzed complex rearrangement reaction. The unique features and intriguing chemistries of these proteins thus demonstrate the remarkable versatility and sophistication of radical enzymology.

Address: State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China. Electronic address: [email protected].; State Key Laboratory of Bioorganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China. Electronic address: [email protected].

DOI: 10.1074/jbc.R111.272690

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MeSH Terms: Biochemistry, Biotransformation, Catalysis, Escherichia coli, Free Radicals, Guanosine Triphosphate, Methylation, Models, Chemical, Molybdenum, Ribosomes, S-Adenosylmethionine, Software