Reptilian alcohol dehydrogenase. Heterogeneity relevant to class multiplicity of the mammalian enzyme.
Liver alcohol dehydrogenase of the ethanol-active type ('class I enzyme') from the lizard, Uromastix hardwickii, was purified and screened for relationships with other vertebrate forms of the enzyme. Two different acetylated N-termini (acetyl-Gly and acetyl-Ser) and further positional differences already in the N-terminal segments establish the presence of two types of protein chain. The multiplicity is different from that hitherto detected within vertebrate class I alcohol dehydrogenase isozymes but typical of that which would be expected for subunits of different classes. In particular, relationships to class II or to class II-related forms appear likely. This may indicate yet further vertebrate alcohol dehydrogenase multiplicity or discovery of a class II non-mammalian enzyme. The results give prospects of defining gene duplications corresponding to more than one alcohol dehydrogenase class split to at an early vertebrate stage.
Hjelmqvist
L
L
Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden.
Ericsson
M
M
Shafqat
J
J
Carlquist
M
M
Siddiqi
A R
AR
Höög
J O
JO
Jörnvall
H
H
D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000145:classification / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism*; D008099:Liver / Q000201:enzymology; D008116:Lizards; D008322:Mammals; D008969:Molecular Sequence Data; D016415:Sequence Alignment
D007527:Isoenzymes; D000426:Alcohol Dehydrogenase