Class 2 aldehyde dehydrogenase. Characterization of the hamster enzyme, sensitive to daidzin and conserved within the family of multiple forms

Abstract

Mitochondrial (class 2) hamster aldehyde dehydrogenase has been purified and characterized. Its primary structure has been determined and correlated with the tertiary structure recently established for this class from another species. The protein is found to represent a constant class within a complex family of multiple forms. Variable segments that occur in different species correlate with non-functional segments, in the same manner as in the case of the constant class of alcohol dehydrogenases (class III type) of another protein family, but distinct from the pattern of the corresponding variable enzymes. Hence, in both these protein families, overall variability and segment architectures behave similarly, with at least one 'constant' form in each case, class III in the case of alcohol dehydrogenases, and at least class 2 in the case of aldehyde dehydrogenases.

Molecular cloning and expression of a second zebrafish aldehyde dehydrogenase 2 gene (aldh2b)

“…Till now, aldh2 gene has been characterized in several mammals including human (Yoshida 1992), rat (Hammen et al 1996), mouse (Chang and Yoshida 1994), hamster (Hjelmqvist et al 1997), horse (Johansson et al 1988) and cattle (Guan and Weiner 1990). Recently, Lassen et al (2005) reported molecular cloning of a zebrafish aldh2 gene and demonstrated that the zebrafish aldh2 had the similar activity to human aldh2 in metabolizing acetaldehyde and propionaldehyde.…”