Radical SAM enzymes in methylation and methylthiolation.
Radical SAM enzymes in methylation and methylthiolation.
复制标题
甲基化和甲硫基化中的自由基 SAM 酶。
DOI:
10.1039/c2mt20136d
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发表时间:
2012
期刊:
影响因子:
--
通讯作者:
Broderick,JoanB
中科院分区:
文献类型:
--
作者:
Hutcheson,RachelU;Broderick,JoanB
RadicalS-adenosyl-l-methionine (SAM) enzymes are a large and diverse superfamily with functions ranging from enzyme activation through a single H atom abstraction to complex organic and metal cofactor synthesis involving a series of steps. Though these enzymes carry out a variety of functions, they share common structural and mechanistic characteristics. All of them contain a site-differentiated [4Fe–4S] cluster, ligated by a CX3CX2C or similar motif, which binds SAM at the unique iron. The [4Fe–4S]1+state of the cluster reductively cleaves SAM to produce a 5′-deoxyadenosyl radical, which serves to initiate the diverse reactions catalyzed by these enzymes. Recent highlights in the understanding of radical SAM enzymes will be presented, with a particular emphasis on enzymes catalyzing methylation and methythiolation reactions.