Acetylated N‐terminal structures of class III alcohol dehydrogenases Differences among the three enzyme classes

FEBS Letters

Holmquist, Barton²  Fairwell, Thomas¹  Parés, Xavier³  Vallee, Bert L.²  Kaiser, Rudolf⁴  Julià, Pere³  Jörnvall, Hans⁴ 

[1] Molecular Disease Branch, NHLBI, NIH, Bethesda, MD 20892, USA;Center for Biochemical and Biophysical Sciences and Medicine, Harvard Medical School, Boston, MA 02115, USA;Departament de Bioquimica i Biologia Molecular, Facultat de Ciències, Universitat Autònoma de Barcelona, Bellaterra, Spain;Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden

关键词: Alcohol dehydrogenase;    Isozyme;    Acetylation;    Sequence homology;    Amino acid sequence;    N-terminal analysis;   

DOI  :  10.1016/0014-5793(87)80199-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protein chains of mammalian alcohol dehydrogenases typically lack free α-amino groups. The blocked N-terminal regions of the class III type of the rat (ADH-2), human (χχ) and horse enzymes were isolated by digestions with proteases, and characterized by mass-spectrometry supplemented with chemical analysis of the peptides and their redigestion fragments. Results were confirmed by synthesis of the corresponding peptides, followed by chromatographic comparisons of the native and synthetic products. The N-terminal regions of the three class III alcohol dehydrogenase subunits are homologous but differ from the class I and II enzymes in both the exact start position and the amino acid sequence, which suggests that different N-terminal structures are typical for each of the three classes.

【 授权许可】

Unknown