Department of Chemistry, University of Waterloo, Waterloo, Ontario, Canada.
Semin Cell Dev Biol. 2011 May;22(3):285-92. doi: 10.1016/j.semcdb.2011.02.004. Epub 2011 Feb 15.
The glyoxalase system is composed of two metalloenzymes, Glyoxalase I and Glyoxalase II. This system is important in the detoxification of methylglyoxal, among other roles. Detailed studies have determined that a number of bacterial Glyoxalase I enzymes are maximally activated by Ni(2+) and Co(2+) ions, but are inactive in the presence of Zn(2+). This is in contrast to the Glyoxalase I enzyme from humans, which is catalytically active with Zn(2+) as well as a number of other metal ions. The structure-activity relationships between these two classes of Glyoxalase I are serving as important clues to how the molecular structures of these proteins control metal activation profiles as well as to clarify the mechanistic chemistry of these catalysts. In addition, the possibility of targeting inhibitors against the bacterial versus human enzyme has the potential to lead to new approaches to combat bacterial infections.
该 Glyoxalase 系统由两种金属酶，即 Glyoxalase I 和 Glyoxalase II 组成。该系统在甲基乙二醛的解毒等方面发挥着重要作用。详细研究表明，一些细菌 Glyoxalase I 酶在 Ni(2+)和 Co(2+)离子的存在下被最大程度地激活，但在 Zn(2+)存在下则失去活性。这与来自人类的 Glyoxalase I 酶形成鲜明对比，后者在 Zn(2+)以及其他一些金属离子存在下具有催化活性。这两类 Glyoxalase I 的结构-活性关系为如何控制这些蛋白质的分子结构以激活金属以及阐明这些催化剂的机械化学提供了重要线索。此外，针对细菌与人类酶的抑制剂的靶向治疗方法有可能为对抗细菌感染提供新的方法。
