Isotope effects in the study of enzymatic phosphoryl transfer reactions

被引:25
作者
Hengge, AC [1 ]
机构
[1] Utah State Univ, Dept Chem & Biochem, Logan, UT 84322 USA
来源
FEBS LETTERS | 2001年 / 501卷 / 2-3期
关键词
isotope effect; phosphoryl transfer; transition state; phosphatase;
D O I
10.1016/S0014-5793(01)02638-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Protein-tyrosine phosphatases and serine/threonine protein phosphatases utilize very different catalytic machinery to catalyze phosphoryl transfer reactions. Tyrosine is a better leaving group than serine or threonine, having a pK(a) more than three units lower. Has the difference in the catalytic machinery used by these enzyme families evolved as a result of the difference in the]ability of their substrates? Are the transition states for phosphoryl transfer similar for the two classes of enzymes? This review summarizes what has been learned from kinetic isotope effects about the nature of enzymatic phosphoryl transfer, and how the enzymatic mechanisms compare to uncatalyzed phosphoryl transfer reactions. (C) 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:99 / 102
页数:4
相关论文
共 32 条