Localization of the thermosensitive X‐prolyl dipeptidyl aminopeptidase in the vacuolar membrane of Saccharomyces cerevisiae

FEBS Letters

Rendueles, Maripaz Suarez²  Schwencke, Jaime¹  Bordallo, Carmen² 

[1] Laboratoire d'Enzymologie du CNRS, Gif-sur-Yvette, France;Departamento Interfacultativo de Bioquimica, Facultad de Medicina, Universidad de Oviedo, Spain

关键词: Yeast;    Dipeptidyl aminopeptidase;    Proteinase;    Vacuole;    Membrane-bound proteinase;    Tonoplast;    Mes;    2-(N-morpholino)ethanesulfonic acid;    Mops;    3-(N-morpholino)propanesulfonic acid;    X-prolyl DPAPase;    X-prolyl dipeptidyl aminopeptidase;   

DOI  :  10.1016/0014-5793(84)81046-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Most of the X-prolyl dipeptidyl aminopeptidase activity of Saccharomyces cerevisiae was found to be associated with purified vacuolar membranes (specific activity approx. 75-times higher than in the protoplast lysate). The tonoplast-bound enzyme is thermosensitive. Another heat-resistant enzyme was found in the protoplast lysate. The tonoplast-bound thermosensitive enzyme shows an apparent K _m of 0.06 mM against L-alanyl-L-prolyl-p-nitroanilide while the heat-resistant enzyme shows an apparent K _m of 0.4 mM against the same substrate.

【 授权许可】

Unknown