| Range |
Table - link
|
| Organism |
Microbes |
| 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 pp.6-7 table S2PubMed 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.4 right column 2nd paragraph:"[Investigators] also note that the loss of rate acceleration with temperature varies significantly between enzymes, and the L10 values (Box 1) range from ∼1 up to nearly 5. The variation, however, shows no correlation with the different classes. Rather, enzymes among the most proficient characterized so far, such as cytidine deaminase or orotidine 5′-monophosphate decarboxylase [ref 32], exhibit the largest loss factor (L10) values (Table S2)." See notes beneath table |
| Entered by |
Uri M |
| ID |
112398 |