Class 2 aldehyde dehydrogenase. Characterization of the hamster enzyme, sensitive to daidzin and conserved within the family of multiple forms.
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.
Hjelmqvist
L
L
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Lundgren
R
R
Norin
A
A
Jörnvall
H
H
Vallee
B
B
Klyosov
A
A
Keung
W M
WM
D000444:Aldehyde Dehydrogenase / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D017124:Conserved Sequence; D006224:Cricetinae; D007529:Isoflavones / Q000494:pharmacology*; D008930:Mitochondria, Liver / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data
D007529:Isoflavones; C013908:daidzin; D000444:Aldehyde Dehydrogenase