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Literature summary for 3.4.16.5 extracted from

  • Kinsho, T.; Ueno, H.; Hayashi, R.; Hashizume, C.; Kimura, K.
    Sub-zero temperature inactivation of carboxypeptidase Y under high hydrostatic pressure (2002), Eur. J. Biochem., 269, 4666-4674.
    View publication on PubMed

General Stability

General Stability Organism
when the enzyme is treated at pressures higher than 300 mPa and temperatures lower than -5°C, it undergoes an irreversible inactivation in which nearly 50% of the alpha-helical structure is lost as judged by circular dichroism spectral analysis. When the applied pressure is limited to below 200 mPa, the cold inactivation process appears to be reversible. In the presence of reducing agent, this reversible phenomenon, observed at below 200 mPa, diminishes to give an inactive enzyme Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
when the enzyme is treated at pressures higher than 300 mPa and temperatures lower than -5°C, it undergoes an irreversible inactivation in which nearly 50% of the alpha-helical structure is lost as judged by circular dichroism spectral analysis. When the applied pressure is limited to below 200 mPa, the cold inactivation process appears to be reversible. In the presence of reducing agent, this reversible phenomenon, observed at below 200 mPa, diminishes to give an inactive enzyme Saccharomyces cerevisiae
-30 20 30 min, 0.1 mPa, nearly full activity is maintained Saccharomyces cerevisiae
10
-
400 mPa, 10 min, 50% loss of activity Saccharomyces cerevisiae