Multiplicity of N-terminal structures of medium-chain alcohol dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and higher vertebrate class I, II, and III forms of the enzyme.
Ten different alcohol dehydrogenases, representing several classes of the enzyme and a wide spread of organisms, were analyzed for patterns of N-terminal structures utilizing a combination of conventional and mass spectrometric peptide analysis. Results show all forms to be N-terminally acetylated and allow comparisons of now 40 such alcohol dehydrogenases covering a large span of forms and origins. Patterns illustrate roles of acetylation in proteins in general, define special importance of the class I N-terminal acetylation, and distinguish separate acetylated structures for all classes, as well as a common alcohol dehydrogenase motif.
Hjelmqvist
L
L
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
Hackett
M
M
Shafqat
J
J
Danielsson
O
O
Iida
J
J
Hendrickson
R C
RC
Michel
H
H
Shabanowitz
J
J
Hunt
D F
DF
Jörnvall
H
H
D000107:Acetylation; D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000145:classification; D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000145:classification; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010940:Plant Proteins / Q000737:chemistry; D010944:Plants / Q000201:enzymology; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D014714:Vertebrates
D007527:Isoenzymes; D010940:Plant Proteins; D000426:Alcohol Dehydrogenase