Halftime of spontaneous protein (peptide bond) hydrolysis at 25°C

Value 400 years
Organism Generic
Reference Wolfenden R, Snider MJ. The depth of chemical time and the power of enzymes as catalysts. Acc Chem Res. 2001 Dec34(12):938-45. p.940 table 1 Table - link PubMed ID11747411
Primary Source Radzicka, A. Wolfenden, R. Rates of Uncatalyzed Peptide Bond Hydrolysis in Neutral Solution and the Transition State Affinities of Proteases. J. Am. Chem. Soc. 1996, 118, 6105-6109.
Method Carboxypeptidase, endopeptidase and dipeptide cleavage reactions were modeled by a suitable derivative of glycylglycine, and could be followed by proton NMR in the temperature range near 150 °C. In each case, the linear Arrhenius plot yielded a half-time of approximately 400 years at 25 °C (primary source).
Comments These results are comparable with those for hydrolysis of the exocyclic amino groups of cytidine and adenosine. Halftime at 100°C is 5.5 weeks. See Table. For halftime of spontaneous peptide hydrolysis (int, C-terminus, dipeptide) of 450 years see p.941 fig.4 Figure link - link
Entered by Uri M
ID 105352