Table - link unitless
||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. Supplementary data p.14 table S5PubMed ID24315123
||See refs beneath table
||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."
||P.2 right column 2nd paragraph:"How do the rate–temperature dependencies of enzyme reactions compare to those of nonenzymatic reactions (Q10non)? A direct comparison (i.e., having both the enzymatic and nonenzymatic Q10 values) is available for only a small set (n=9) that exhibits an average Q10non of 3.4. A larger set of reactions (n=18) indicates an average Q10non of ∼4.4 (Table S5). The prevailing rule of thumb is that reaction rates double per 10°C increase. [Investigators] could not, however, find any systematic exploration of this rule. As previously noticed [ref 17], the Q10non values for enzyme-catalyzed reactions appear to be much higher than 2. It thus remains unclear whether the rule of thumb should become Q10 = 3, or possibly 4, or whether the current sample of Q10non is biased, particularly for reactions in water, where dramatic changes in water properties such as density and ionic concentration occur at high temperatures [ref 18]." See note beneath table