期刊
FEBS JOURNAL
卷 278, 期 20, 页码 3835-3845出版社
WILEY
DOI: 10.1111/j.1742-4658.2011.08190.x
关键词
active sites; catalysis; enzyme; evolution; MACiE; mechanism; specificity; structure
资金
- Wellcome Trust
- EMBL
- IBM
- Scottish Universities Life Sciences Alliance (SULSA)
Enzymes are basically composed of 20 naturally occurring amino acids, yet they catalyse a dizzying array of chemical reactions, with regiospecificity and stereospecificity and under physiological conditions. In this review, we attempt to gain some understanding of these complex proteins, from the chemical versatility of the catalytic toolkit, including the use of cofactors (both metal ions and organic molecules), to the complex mapping of reactions to proteins (which is rarely one-to-one), and finally the structural complexity of enzymes and their active sites, often involving multidomain or multisubunit assemblies. This work highlights how the enzymes that we see today reflect millions of years of evolution, involving de novo design followed by exquisite regulation and modulation to create optimal fitness for life.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据