Effects of High-Pressure on the Activity and Spectroscopic Properties of Carboxypeptidase Y
Author:
Publisher
The Chemical Society of Japan
Subject
General Chemistry
Link
https://www.jstage.jst.go.jp/article/bcsj/70/6/70_6_1459/_pdf
Reference32 articles.
1. [48] Carboxypeptidase Y
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3. The Activity of Carboxypeptidase Y toward Substrates with Basic P1 Amino Acid Residues Is Drastically Increased by Mutational Replacement of Leucine 178
4. Mechanistic study on carboxypeptidase Y-catalyzed transacylation reactions. Mutationally altered enzymes for peptide synthesis
5. Site-directed mutagenesis on (serine) carboxypeptidase Y. A hydrogen bond network stabilizes the transition state by interaction with the C-terminal carboxylate group of the substrate
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1. Pressure and temperature as tools for investigating the role of individual non-covalent interactions in enzymatic reactions;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2006-03
2. Sínteses química e enzimática de peptídeos: princípios básicos e aplicações;Química Nova;2004-10
3. The propeptide in the precursor form of carboxypeptidase Y ensures cooperative unfolding and the carbohydrate moiety exerts a protective effect against heat and pressure;European Journal of Biochemistry;2003-11
4. Pressure-driven Cold Denaturation of Proteins and Structure Formation of Water-soluble Polymers;Advances in High Pressure Bioscience and Biotechnology II;2003
5. Cold denaturation of proteins under high pressure;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2002-03
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