Multiplicity of N-terminal structures of medium-ch...[FEBS Lett. 1995]

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1: FEBS Lett. 1995 Jul 3;367(3):237-40. Links

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.

Hjelmqvist L, Hackett M, Shafqat J, Danielsson O, Iida J, Hendrickson RC, Michel H, Shabanowitz J, Hunt DF, Jörnvall H.

Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.

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.

PMID: 7607314 [PubMed - indexed for MEDLINE]

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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.

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