Carboxypeptidase Y activity and maintenance is modulated by a large helical structure
| Autor: | Takehiko Sahara, Mai Makino, Hiroshi Ueno, Naoki Morita |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
Protein Denaturation Protein Folding Saccharomyces cerevisiae Proteins Stereochemistry Protein Conformation Mutant Cathepsin A Carboxypeptidases Saccharomyces cerevisiae General Biochemistry Genetics and Molecular Biology Catalysis Substrate Specificity 03 medical and health sciences 0302 clinical medicine Catalytic Domain Hydrolase Amino Acid Sequence lcsh:QH301-705.5 Research Articles Serine protease Binding Sites biology Chemistry Disulfide bond Active site 030104 developmental biology lcsh:Biology (General) 030220 oncology & carcinogenesis Intramolecular force serine carboxypeptidase Helix biology.protein α/β hydrolase fold Protein folding disulfide bond Research Article |
| Zdroj: | FEBS Open Bio FEBS Open Bio, Vol 9, Iss 7, Pp 1337-1343 (2019) |
| ISSN: | 2211-5463 |
| Popis: | Yeast carboxypeptidase Y (CPY) is a serine protease with broad substrate specificity. Structurally, CPY belongs to the α/β hydrolase fold family and contains characteristic large helices, termed the V-shape helix, above the active site cavity. Four intramolecular disulfide bonds are located in and around the V-shape helix. In this study, mutant CPYs were constructed in which one of these disulfide bonds was disrupted. Mutants lacking the C193-C207 bond located at the beginning of the V-shape helix aggregated easily, while mutants lacking the C262-C268 bond located at the end of the V-shape helix displayed decreased hydrolytic activity. The results indicate that the V-shape helix is involved in CPY catalysis and in maintenance of its conformation. |
| Databáze: | OpenAIRE |
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