| 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 |