Emerging themes in radical SAM chemistry.
作者： Krista A Shisler , Joan B Broderick
DOI: 10.1016/J.SBI.2012.10.005
关键词: Cysteine 、 Triosephosphate isomerase 、 Biocatalysis 、 Cluster (physics) 、 SUPERFAMILY 、 TIM barrel 、 Chemistry 、 Stereochemistry 、 Radical SAM 、 Organic chemistry 、 Radical
摘要: Enzymes in the radical SAM (RS) superfamily catalyze a wide variety of reactions through unique chemistry. The characteristic markers include [4Fe–4S] cluster coordinated to protein via cysteine triad motif, typically CX3CX2C, with fourth iron by S-adenosylmethionine (SAM). serves as precursor for 5′-deoxyadenosyl radical, central intermediate nearly all RS enzymes studied date. SAM-bound is located within partial or full triosephosphate isomerase (TIM) barrel where chemistry occurs protected from surroundings. In addition TIM and cluster, many members contain additional domains and/or Fe–S clusters. Recently characterized are providing new examples remarkable range that can be catalyzed, well structural mechanistic insights into these fascinating reactions.
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