ALDEHYDE DEHYDROGENASE - AN ENZYME WITH 2 DISTINCT CATALYTIC ACTIVITIES AT A SINGLE TYPE OF ACTIVE-SITE
ALDEHYDE DEHYDROGENASE - AN ENZYME WITH 2 DISTINCT CATALYTIC ACTIVITIES AT A SINGLE TYPE OF ACTIVE-SITE
复制标题
DOI：
10.1042/bj2300261
复制
发表时间：
1985-01-01
影响因子：
4.1
通讯作者：
DUNCAN, RJS
中科院分区：
文献类型：
--
作者：
DUNCAN, RJS
研究了乙醛脱氢酶的酯酶和脱氢酶活性位点在拓扑结构上不同的证据。研究发现，所有的证据（包括以前由其他人积累的支持不同结合域的证据）实际上都与具有两种活性的单一类型的催化位点一致，并且有利于这一观点。该酶是否存在单独的高km调节位点也受到质疑。
The evidence for and against the esterase and dehydrogenase active sites of aldehyde dehydrogenase being topologically distinct is examined. It is found that all the evidence (including all that previously amassed by others in favor of distinct binding domains) is actually consistent with, and in favor of, a single type of catalytic site having both activities. The existence of separate high-Km modulating sites for the enzyme is also questioned.