Radical SAM, A Novel Protein Superfamily Linking Unresolved Steps in Familiar Biosynthetic Pathways with Radical Mechanisms: Functional Characterization Using New Analysis and Information Visualization Methods

Journal Article · Thu Mar 01 00:00:00 EST 2001 · Nucleic Acids Research, 29(5):1097-1106

DOI:https://doi.org/10.1093/nar/29.5.1097· OSTI ID:15005647

Sofia, Heidi J; Chen, Guang; Hetzler, Elizabeth G; Reyes Spindola, Jorge F; Miller, Nancy E

A large protein superfamily with over 500 members has been discovered and analyzed using powerful new bioinformatics and information visualization methods. Evidence exists that these proteins generate a 5?-deoxyadenosyl radical by reductive cleavage of S-adenosylmethionine (SAM) through an unusual Fe-S center. Radical SAM superfamily proteins function in DNA precursor, vitamin, cofactor, antibiotic, and herbicide biosynthesis in a collection of basic and familiar pathways. One of the members is interferon-inducible and is considered a candidate drug target for osteoporosis. The identification of this superfamily suggests that radical-based catalysis is important in a number of previously well-studied but unresolved biochemical pathways.

• Research Organization: Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC06-76RL01830
• OSTI ID: 15005647
• Report Number(s): PNNL-SA-34089
• Journal Information: Nucleic Acids Research, 29(5):1097-1106, Journal Name: Nucleic Acids Research, 29(5):1097-1106
• Country of Publication: United States
• Language: English