| Value |
1E+17
times
|
| Organism |
Unspecified |
| Reference |
Zavada SR, Battsengel T, Scott TF. Radical-Mediated Enzymatic Polymerizations. Int J Mol Sci. 2016 Feb 2 17(2). pii: E195. doi: 10.3390/ijms17020195 p.1 bottom paragraphPubMed ID26848652
|
| Primary Source |
Radzicka A, Wolfenden R. A proficient enzyme. Science. 1995 Jan 6 267(5194):90-3.PubMed ID7809611
|
| Method |
Primary source abstract: "Reactions in quartz tubes at elevated temperatures." |
| Comments |
P.1 bottom paragraph: "Enzymes are proteins that catalyze biochemical reactions. By binding a substrate to the active site of an enzyme, the activation energy of the reaction can be decreased, resulting in a substantial reaction rate increase. For example, the enzyme orotidine 5’-phosphate decarboxylase accelerates the orotidine 5’-monophosphate decarboxylation rate by 10^17 times the uncatalyzed reaction rate [primary source]." |
| Entered by |
Uri M |
| ID |
113722 |