期刊论文详细信息
FEBS Letters | |
Localization of the thermosensitive X‐prolyl dipeptidyl aminopeptidase in the vacuolar membrane of Saccharomyces cerevisiae | |
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
【 预 览 】
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RO201912020285711ZK.pdf | 520KB | download |