| Range |
Q10 non-enzymatic 3.4: Q10 enzymatic 1.8 unitless
|
| Organism |
Unspecified |
| Reference |
Elias M, Wieczorek G, Rosenne S, Tawfik DS. The universality of enzymatic rate-temperature dependency. Trends Biochem Sci. 2014 Jan39(1):1-7. doi: 10.1016/j.tibs.2013.11.001. p.2 right column bottom paragraphPubMed ID24315123
|
| Method |
P.1 right column bottom paragraph:"Here, [investigators] jointly address the rate–temperature dependencies of all enzyme classes, and compare them to the dependency of nonenzymatic reactions. [They] challenge the generally accepted paradigm that thermophilic, mesophilic, and psychrophilic enzymes have distinct rate–temperature dependencies, and that temperature–rate dependencies relate, by default, to enzyme dynamics. [They] suggest a common theme that underlines the temperature–rate dependency of all enzymes as long as they maintain their folded state. Also, [they] re-examine the generally assumed linkage between the overall rigidity of the fold and active site of an enzyme." |
| Comments |
P.2 right column bottom paragraph:"As is obvious from the average Q10non (3.4) versus Q10enz (1.8) values, the rates of the nonenzymatic reactions increase faster than the enzymatic reactions with temperature. Consequently, the rate enhancements (i.e., the ratio of the catalyzed versus uncatalyzed reaction rates, kcat/knon) exhibited by enzymes from all three classes consistently decrease with increasing temperature (Figure 2)." |
| Entered by |
Uri M |
| ID |
112397 |