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

FEBS Letters

Shafqat, Jawed¹  Hjelmqvist, Lars¹  Shabanowitz, Jeffrey²  Hunt, Donald F.²  Jönvall, Hans¹  Michel, Hanspeter²  Hendrickson, Ronald C.²  Iida, Junko²  Hackett, Murray²  Danielsson, Olle¹ 

[1] Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden;Department of Chemistry, University of Virginia, Charlottesville, VI 22901, USA

关键词: Enzyme family;    Alcohol dehydrogenase;    Mass spectrometry;    N-terminus;    Acetyl group;   

DOI  :  10.1016/0014-5793(95)00572-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown