| Range |
Table - link
|
| Organism |
Various |
| 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. Supplementary data p.5 table S1PubMed ID24315123
|
| Primary Source |
See refs beneath table |
| 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 left column 2nd paragraph:"Rate–temperature dependencies are compared using the empirical measure of Q10 (Box 1). [Investigators] systematically explored the existing literature, and extracted Q10 values for >150 enzymatic reactions from the three environmental classes, including reactions for which Q10 values were available for both the enzymatic and nonenzymatic reactions (Figure 1 Text S1 and Tables S1–S4 in the supplementary material online)." See note beneath table |
| Entered by |
Uri M |
| ID |
112399 |