Duncan R J
Biochem J. 1979 Nov 1;183(2):459-62. doi: 10.1042/bj1830459.
An aldehyde dehydrogenase from rabbit liver, a homogeneous protein on three distinct polyacrylamide-gel systems, has an associated 4-nitrophenyl esterase activity. At pH 7.0 in the presence of 80 micrometer-NADH and 800 micrometer-4-nitrophenyl acetate the enzyme produces NAD+ and a stoicheiometric amount of an aldehyde, as well as hydrolysing the ester. On this and other evidence it is proposed that ester hydrolysis occurs at the usual active site of the enzyme.
来自兔肝脏的一种醛脱氢酶,在三种不同的聚丙烯酰胺凝胶系统中均为均一蛋白质,它具有相关的4-硝基苯酯酶活性。在pH 7.0、存在80微摩尔NADH和800微摩尔4-硝基苯乙酸酯的情况下,该酶产生NAD⁺和化学计量的醛,同时水解酯。基于这一及其他证据,有人提出酯水解发生在该酶通常的活性位点。