Why does ribonuclease irreversibly inactivate at high temperatures?
BiochemistryPublished 23 September 1986
Stephen E. Zale, Alexander M. Klibanov
Citations274
SJR quartileQ1
SJR score1.18
SNIP0.73
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TL;DR
The mechanism of irreversible thermoinactivation of bovine pancreatic ribonuclease A in the pH range relevant to enzymatic catalysis has been elucidated and four processes appear to demarcate the upper limit of thermostability of enzymes.
Abstract
The mechanism of irreversible thermoinactivation of bovine pancreatic ribonuclease A in the pH range relevant to enzymatic catalysis has been elucidated. At 90 degrees C and pH 4, the enzyme inactivation is caused by hydrolysis of peptide bonds at aspartic acid residues (the main process) and deamidation of asparagine and/or glutamine residues. At 90 degrees C and neutral pH (pH 6 and 8), the enzyme inactivation is caused by a combination of disulfide interchange (the main process), beta-elimination of cystine residues, and deamidation of asparagine and/or glutamine residues. These four processes appear to demarcate the upper limit of thermostability of enzymes.
Keywords
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