Examinations of the Chemical Step in Enzyme Catalysis

被引:14
|
作者
Singh, P. [1 ]
Islam, Z. [1 ]
Kohen, A. [1 ]
机构
[1] Univ Iowa, Iowa City, IA 52242 USA
来源
COMPUTATIONAL APPROACHES FOR STUDYING ENZYME MECHANISM, PT A | 2016年 / 577卷
关键词
COLI DIHYDROFOLATE-REDUCTASE; LIVER ALCOHOL-DEHYDROGENASE; THYMIDYLATE SYNTHASE; HYDRIDE TRANSFER; ESCHERICHIA-COLI; TEMPERATURE-DEPENDENCE; PROTEIN DYNAMICS; DISTAL MUTATIONS; ACTIVE-SITE; COUPLED MOTIONS;
D O I
10.1016/bs.mie.2016.05.017
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Advances in computational and experimental methods in enzymology have aided comprehension of enzyme-catalyzed chemical reactions. The main difficulty in comparing computational findings to rate measurements is that the first examines a single energy barrier, while the second frequently reflects a combination of many microscopic barriers. We present here intrinsic kinetic isotope effects and their temperature dependence as a useful experimental probe of a single chemical step in a complex kinetic cascade. Computational predictions are tested by this method for two model enzymes: dihydrofolate reductase and thymidylate synthase. The description highlights the significance of collaboration between experimentalists and theoreticians to develop a better understanding of enzyme-catalyzed chemical conversions.
引用
收藏
页码:287 / 318
页数:32
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