磷酸丙糖异构酶催化的反应中亲电成分的存在。
The existence of an electrophilic component in the reaction catalysed by triose phosphate isomerase.
作者信息
Webb M R, Knowles J R
出版信息
Biochem J. 1974 Aug;141(2):589-92. doi: 10.1042/bj1410589.
Abstract
In the presence of triose phosphate isomerase, the substrate dihydroxyacetone phosphate is reduced stereoselectively by NaBH(4). The reduction of enzyme-bound substrate is almost completely or completely stereoselective and occurs about one order of magnitude faster than that in free solution. This acceleration implies a polarization of the carbonyl group when dihydroxyacetone phosphate is bound.
摘要
在磷酸丙糖异构酶存在的情况下，底物磷酸二羟丙酮被硼氢化钠（NaBH₄）立体选择性地还原。酶结合底物的还原几乎是完全或完全立体选择性的，并且比在游离溶液中快约一个数量级。这种加速意味着当磷酸二羟丙酮结合时羰基的极化。
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本文引用的文献
1
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Brookhaven Symp Biol. 1962 Dec;15:293-309.
2
Synthesis of phosphatides in isolated mitochondria. III. The enzymatic phosphorylation of glycerol.分离线粒体中磷脂的合成。III. 甘油的酶促磷酸化作用。
J Biol Chem. 1954 Dec;211(2):951-61.
3
Active-site labelling of triose phosphate isomerase. The reaction of bromohydroxyacetone phosphate with a unique glutamic acid residue and the migration of the label to tyrosine.磷酸丙糖异构酶的活性位点标记。磷酸溴代羟基丙酮与一个独特的谷氨酸残基的反应以及标记向酪氨酸的迁移。
Biochem J. 1972 Sep;129(2):321-31. doi: 10.1042/bj1290321.
4
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5
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6
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