OXALOACETATE DECARBOXYLASE FROM COD . CATALYSIS OF HYDROGEN-DEUTERIUM EXCHANGE IN PYRUVATE

被引：24

作者：

KOSICKI, GW

机构：

[1] James Bryant Conant Laboratory, Department of Chemistry, Harvard University, Cambridge, Massachusetts

来源：

BIOCHEMISTRY | 1968年 / 7卷 / 12期

关键词：

D O I：

10.1021/bi00852a024

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：

The mechanism for the decarboxylation of oxaloacetate by oxaloacetate decarboxylase proceeds by way of a metal ion-oxaloacetate-enzyme complex through the enol form of pyruvate to the keto form of pyruvate. The reverse reaction should then lead to the enol from the keto form of pyruvate, so that the enzyme in the presence of metal ion should catalyze the exchange of hydrogen atoms of pyruvate with the solvent. This prediction has been realized; the rate of the reaction has been measured by nuclear magnetic resonance techniques. This catalyzed hydrogen exchange has been found to be both metal-ion dependent and inhibited by oxalate, as is the catalyzed decarboxylation of oxaloacetate and the catalyzed NaBH4 reduction of pyruvate. © 1968, American Chemical Society. All rights reserved.

引用

页码：4310 / &

共 11 条

[1] MAGNETIC RESONANCE STUDIES OF METAL ACTIVATION OF ENZYMIC REACTIONS OF NUCLEOTIDES AND OTHER PHOSPHATE SUBSTRATES [J].