Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism

John M. Brewer; Claiborne V. C. Glover; Michael J. Holland; Lukasz Lebioda

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Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism

机译：酵母S39A烯醇酶的酶学性质对催化机理的意义

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The S39A mutant of yeast enolase (isozyme 1), prepared by site-directed mutagenesis, has a relative V_(max) of 0.01% and an activation constant for Mg~(2+) ca. 10-fold higher, compared with native enzyme. It is correctly folded. There is little effect of solvent viscosity on activity. We think that the loop Ser36-His43 fails to move to the 'closed' position upon catalytic Mg~(2+) binding, weakening several electrostatic interactions involved in the mechanism.

机译：通过定点诱变制备的酵母烯醇酶S39A突变体（同工酶1）的相对V_（max）为0.01％，Mg〜（2+）的激活常数为ca。与天然酶相比，高10倍。正确折叠。溶剂粘度对活性几乎没有影响。我们认为，环Ser36-His43在催化Mg〜（2+）结合后无法移动到“闭合”位置，从而削弱了该机理中涉及的几种静电相互作用。

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《Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology》 |1998年第0期|共5页
作者
John M. Brewer; Claiborne V. C. Glover; Michael J. Holland; Lukasz Lebioda;
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正文语种 eng
中图分类生物化学;分子生物学;
关键词
enolase; mutagenesis; catalytic mechanism; loop closure;

机译：烯醇酶诱变催化机理闭环;

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1. Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism. [J] . Brewer JM, Glover CV, Holland MJ, Biochimica et biophysica acta: international journal of biochemistry and biophysics . 1998,第2期

机译：酵母S39A烯醇化酶的酶学性质对催化机理的意义。
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Significance of the enzymatic properties of yeast S39A enolase to the catalytic mechanism

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