| Range |
4х10^8 M^-1×sec^-1
|
| Organism |
Unspecified |
| Reference |
Blacklow SC, Raines RT, Lim WA, Zamore PD, Knowles JR. Triosephosphate isomerase catalysis is diffusion controlled. Appendix: Analysis of triose phosphate equilibria in aqueous solution by 31P NMR. Biochemistry. 1988 Feb 23 27(4):1158-67. p.1162 left column 2nd paragraphPubMed ID3365378
|
| Primary Source |
Albery WJ, Knowles JR. Free-energy profile of the reaction catalyzed by triosephosphate isomerase. Biochemistry. 1976 Dec 14 15(25):5627-31.PubMed ID999838
|
| Comments |
"...[researchers] report the application of the viscosity variation
method to the reaction catalyzed by triosephosphate isomerase,
an enzyme that has a value of kcat/Kmin the thermodynamically
downhill direction of 4×10^8M^-1×s^-1 (primary source) and seems a likely candidate for a reaction
that proceeds at the diffusion limit." |
| Entered by |
Uri M |
| ID |
109296 |