کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1178482 | 962695 | 2012 | 13 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Enzyme catalyzed formation of radicals from S-adenosylmethionine and inhibition of enzyme activity by the cleavage products Enzyme catalyzed formation of radicals from S-adenosylmethionine and inhibition of enzyme activity by the cleavage products](/preview/png/1178482.png)
A large superfamily of enzymes have been identified that make use of radical intermediates derived by reductive cleavage of S-adenosylmethionine. The primary nature of the radical intermediates makes them highly reactive and potent oxidants. They are used to initiate biotransformations by hydrogen atom abstraction, a process that allows a particularly diverse range of substrates to be functionalized, including substrates with relatively inert chemical structures. In the first part of this review, we discuss the evidence supporting the mechanism of radical formation from S-adenosylmethionine. In the second part of the review, we examine the potential of reaction products arising from S-adenosylmethionine to cause product inhibition. The effects of this product inhibition on kinetic studies of ‘radical S-adenosylmethionine’ enzymes are discussed and strategies to overcome these issues are reviewed. This article is part of a Special Issue entitled: Radical SAM enzymes and Radical Enzymology.
► Alternative SAM cleavage pathways.
► SAM cleavage products and product-like molecules may be inhibitory.
► Product inhibition of radical SAM enzymes can be relieved by MTAN.
► Substrate binding lowers the energetic barrier to radical formation.
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1824, Issue 11, November 2012, Pages 1165–1177