ArticleFEBS open bio2019
Carboxypeptidase Y activity and maintenance is modulated by a large helical structure.
Article in FEBS open bio, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Carboxypeptidases for food processing: structural characteristics, expression optimization, and advances in applications.Frontiers in nutrition · 2026Review
- Transcriptome Profiling Provides Insights Into Potential Antagonistic Mechanisms Involved inFrontiers in microbiology · 2020Article
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Authors and funding
4 authors.
Funding
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Abstract
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.
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