The temperature dependence of enzyme rate enhancements [8]

Journal of the American Chemical Society

Volumn 121, Issue 32, 1999, Pages 7419-7420

  Wolfenden, Richard ^a   Snider, Mark ^a   Ridgway, Caroline ^a   Miller, Brian ^a  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GLUCOSIDASE; BACTERIAL ENZYME; CARBOXYLYASE; CHORISMATE MUTASE; CHYMOTRYPSIN; FUNGAL PROTEIN; GLYCOSIDE; NUCLEASE; UREASE;

BACTERIUM; BINDING AFFINITY; ENZYME BINDING; ENZYME KINETICS; ENZYME SUBSTRATE; LETTER; NONHUMAN; TEMPERATURE DEPENDENCE; YEAST;

EID: 0033581167     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja991280p     Document Type: Letter

References (22)

1. Wolfenden, R. Nature 1969, 223, 704-705.
2. 14-fold) arise from variations in the rate of the uncatalyzed reactions, the rates of most enzyme reactions remaining relatively invariant (Radzicka, A.; Wolfenden, R. Science 1995, 267, 90-93).
3. 2 (Harcourt, A. V. J. Chem. Soc. 1867, 20, 460-495), that tendency has since been observed for so many reactions that it is offered as a rule of thumb by most textbooks that have anything to say about the temperature dependence of reaction rates in water (see, for example: Pauling, L. College Chemistry; Freeman: New York, 1950; p 410).
4. 2 (Harcourt, A. V. J. Chem. Soc. 1867, 20, 460-495), that tendency has since been observed for so many reactions that it is offered as a rule of thumb by most textbooks that have anything to say about the temperature dependence of reaction rates in water (see, for example: Pauling, L. College Chemistry; Freeman: New York, 1950; p 410).
5. Laidler, K. J.; Peterman, B. K. Methods Enzymol. 1979, 63, 234-257.
6. ‡ vary within a relatively narrow range.
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9. Wolfenden, R.; Ridgway, C.; Young, G. J. Am. Chem. Soc. 1998, 120, 6814-6815.
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15. This work.
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19. Each of these reactions involves a single substrate, or water is the second substrate and its concentration is very high. In reactions that involve multiple substrates, or in which ground states and transition states differ markedly in their free energies of interaction with solvent water, entropic contributions might be expected to be more pronounced (Westheimer, F. H. Adv. Enzymol. 1962, 24, 441-482). That possibility remains to be examined experimentally.
20. Kati, W. M.; Wolfenden, R. Biochemistry 1989, 28, 7919-7927.
21. Nonpolar interactions also play a role in some reactions that involve charge delocalization, but their use in enzyme catalysts appears to be relatively uncommon (for a review, see: Radzicka, A.; Wolfenden, R. Methods Enzymol. 1995, 249, 284-312).
22. 8