期刊
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 80
卷 80, 期 -, 页码 669-702出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-060409-092741
关键词
transition state; enzymes; linear free energy relationship; kinetic isotope effects; phosphate ester
资金
- NIGMS NIH HHS [GM080865, F32 GM080865, GM64798, R01 GM064798] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [F32GM080865, R01GM064798] Funding Source: NIH RePORTER
Phosphoryl-transfer reactions are central to biology. These reactions also have some of the slowest nonenzymatic rates and thus require enormous rate accelerations from biological catalysts. Despite the central importance of phosphoryl transfer and the fascinating catalytic challenges it presents, substantial confusion persists about the properties of these reactions. This confusion exists despite decades of research on the chemical mechanisms underlying these reactions. Here we review phosphoryl-transfer reactions with the goal of providing the reader with the conceptual and experimental background to understand this body of work, to evaluate new results and proposals, and to apply this understanding to enzymes. We describe likely resolutions to some controversies, while emphasizing the limits of our current approaches and understanding. We apply this understanding to enzyme-catalyzed phosphoryl transfer and provide illustrative examples of how this mechanistic background can guide and deepen our understanding of enzymes and their mechanisms of action. Finally, we present important future challenges for this field.
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