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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
Author(s) -
Hjelmqvist Lars,
Hackett Murray,
Shafqat Jawed,
Danielsson Olle,
Iida Junko,
Hendrickson Ronald C.,
Michel Hanspeter,
Shabanowitz Jeffrey,
Hunt Donald F.,
Jönvall Hans
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00572-q
Subject(s) - acetylation , alcohol dehydrogenase , alcohol , vertebrate , biochemistry , enzyme , biology , peptide , chemistry , stereochemistry , gene
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.