| Range |
~8х10^-10 Sec^-1
|
| Organism |
Unspecified |
| Reference |
Monika Fuxreiter and Arieh Warshel, Origin of the Catalytic Power of Acetylcholinesterase:? Computer Simulation Studies, J. Am. Chem. Soc., 1998, 120 (1), pp 183–194
DOI: 10.1021/ja972326m p.186 right column bottom paragraph |
| Primary Source |
Schowen, R. L. In Transition States of Biochemical Processes Gandour, R. D., Schowen, R. L., Eds. Plenum: New York, 1978 p 77. |
| Comments |
"A
useful definition of the catalytic effect can be obtained when
one compares kcat for the hydrolysis of acetylcholine by water
~8?10^-10s-1 (e.g. see primary source) to kcat in the enzyme active
site ~1.6?10^4 s-1 [BNID 109216]. By this definition we
have a rate enhancement of 2?10^13." |
| Entered by |
Uri M |
| ID |
109218 |