Chern M K, Pietruszko R
Center of Alcohol Studies, Rutgers University, Piscataway, NJ 08855-0969, USA.
Biochem Biophys Res Commun. 1995 Aug 15;213(2):561-8. doi: 10.1006/bbrc.1995.2168.
The E3 isozyme of human aldehyde dehydrogenase (EC 1.2.1.3), with broad substrate specificity, which also catalyzes dehydrogenation of 4-aminobutyraldehyde, was purified and sequenced recently (1,3). It has been shown during this investigation to have betaine aldehyde dehydrogenase activity. Betaine aldehyde and 4-aminobutyraldehyde activities copurified on six chromatographic columns. Molecular properties of the homogeneous product were identical with those of E3 isozyme. Activity with betaine aldehyde was considerably higher than that with 4-aminobutyraldehyde, the best known substrate. Thus, human E3 isozyme and betaine aldehyde dehydrogenase (EC 1.2.1.8) are the same enzyme.
人类醛脱氢酶（EC 1.2.1.3）的E3同工酶具有广泛的底物特异性，它也催化4-氨基丁醛的脱氢反应，最近已被纯化和测序（1,3）。在这项研究中已表明它具有甜菜碱醛脱氢酶活性。甜菜碱醛和4-氨基丁醛活性在六个色谱柱上共纯化。均一产物的分子特性与E3同工酶相同。与甜菜碱醛的活性明显高于与最知名底物4-氨基丁醛的活性。因此，人类E3同工酶和甜菜碱醛脱氢酶（EC 1.2.1.8）是同一种酶。
