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- W3021189985 abstract "Publisher SummaryThis chapter describes the activity, specificity and structural chemistry of Sulfolobus carboxypeptidase. S. carboxypeptidase was subsequently purified to electrophoretic homogeneity and extensively characterized. In particular, specificity studies confirmed that it was able to cleave an N-blocked tripeptide. The S. solfataricus enzyme is completely stable up to 80°C, whereas at higher temperatures it undergoes first-order irreversible thermal inactivation, with half-lives of 131 and 13.5 min at 85°C and 90°C, respectively. First-order kinetics demonstrates that autolytic cleavage is not responsible for the inactivation, but that it is more a case of thermal unfolding, as also supported by the fact that no proteolyzed form of the enzyme can be detected. At 70°C, S. solfataricus carboxypeptidase is completely stable in the pH range 5.8–8.0, whereas it is abruptly destabilized beyond these values. At 40°C, the enzyme withstands 50% methanol, 50% acetonitrile and 99% ethanol, and at 70°C, it undergoes extensive inactivation in the presence of the organic solvents. The capacity to withstand extreme pressure and solvent conditions might make it suitable as a catalyst for organic syntheses under these unusual physiochemical conditions. S. solfataricus carboxypeptidase is obtained from strain MT-4 using a 5-step procedure." @default.
- W3021189985 created "2020-05-13" @default.
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- W3021189985 date "2004-01-01" @default.
- W3021189985 modified "2023-10-05" @default.
- W3021189985 title "Sulfolobus carboxypeptidase" @default.
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- W3021189985 doi "https://doi.org/10.1016/b978-0-12-079611-3.50295-0" @default.
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