绵羊肝脏醛脱氢酶催化的乙醛和丁醛氧化反应的部分逆转
Partial reversal of the acetaldehyde and butyraldehyde oxidation reactions catalysed by aldehyde dehydrogenases from sheep liver.
作者信息
Hart G J, Dickinson F M
出版信息
Biochem J. 1978 Nov 1;175(2):753-6. doi: 10.1042/bj1750753.
Abstract
In the presence of acetic anhydride or butyric anhydride, liver aldehyde dehydrogenases catalyse the oxidation of NADH at pH 7.0 and 25 degrees C. The maximum velocities and Michaelis constants for NADH at saturating anhydride concentrations are independent of which anhydride is used, the values being V'max. = 12 min-1 and Km for NADH = 9 micrometer for the mitochondrial enzyme and V'max = 25 min-1 and Km for NADH = 20 micrometer for the cytoplasmic enzyme. Substitution of [4A-2H]NADH for NADH resulted in 2-fold and 4-fold decreases in rate for the mitochondrial and cytoplasmic enzymes respectively.
摘要
在乙酸酐或丁酸酐存在的情况下，肝脏醛脱氢酶在pH 7.0和25℃时催化NADH的氧化。在饱和酸酐浓度下，NADH的最大反应速度和米氏常数与使用哪种酸酐无关，线粒体酶的值为V'max = 12 min-1，NADH的Km = 9微摩尔；细胞质酶的值为V'max = 25 min-1，NADH的Km = 20微摩尔。用[4A-2H]NADH替代NADH后，线粒体酶和细胞质酶的反应速率分别降低了2倍和4倍。
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