Hiscox Martyn J, Driesener Rebecca C, Roach Peter L
School of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, UK.
Biochim Biophys Acta. 2012 Nov;1824(11):1165-77. doi: 10.1016/j.bbapap.2012.03.013. Epub 2012 Apr 3.
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.
已经鉴定出一大类酶超家族，它们利用通过S-腺苷甲硫氨酸还原裂解产生的自由基中间体。自由基中间体的主要性质使其具有高反应性和强氧化性。它们通过氢原子提取来启动生物转化，这一过程允许对特别多样的底物进行功能化，包括具有相对惰性化学结构的底物。在本综述的第一部分，我们讨论了支持从S-腺苷甲硫氨酸形成自由基机制的证据。在综述的第二部分，我们研究了由S-腺苷甲硫氨酸产生的反应产物导致产物抑制的可能性。讨论了这种产物抑制对“自由基S-腺苷甲硫氨酸”酶动力学研究的影响，并综述了克服这些问题的策略。本文是名为：自由基SAM酶和自由基酶学的特刊的一部分。
