The universality of enzymatic rate-temperature dependency

Mikael Elias, Grzegorz Wieczorek, Shaked Rosenne, Dan S. Tawfik

Research output: Contribution to journalReview articlepeer-review

145 Scopus citations


Organismal adaptation to extreme temperatures yields enzymes with distinct configurational stabilities, including thermophilic and psychrophilic enzymes, which are adapted to high and low temperatures, respectively. These enzymes are widely assumed to also have unique rate-temperature dependencies. Thermophilic enzymes, for example, are considered optimal at high temperatures and effectively inactive at low temperatures due to excess rigidity. Surveying published data, we find that thermophilic, mesophilic, and psychrophilic enzymes exhibit indistinguishable rate-temperature dependencies. Furthermore, given the nonenzymatic rate-temperature dependency, all enzymes, regardless of their operation temperatures, become >10-fold less powerful catalysts per 25°C temperature increase. Among other factors, this loss of rate acceleration may be ascribed to thermally induced vibrations compromising the active-site catalytic configuration, suggesting that many enzymes are in fact insufficiently rigid.

Original languageEnglish (US)
Pages (from-to)1-7
Number of pages7
JournalTrends in Biochemical Sciences
Issue number1
StatePublished - Jan 2014

Bibliographical note

Funding Information:
This work was inspired by review comments to [31] and illuminating discussions with Brian Shoichet. We are also grateful to Ron Milo, Arren Bar-Even, James Fraser, Nobuhiko Tokuriki, and Arieh Warshel for inspiring discussions and valuable comments. Financial support by the Israel Science Foundation is gratefully acknowledged.


  • Active-site preorganization
  • Enzyme dynamics
  • Rate temperature-dependency
  • Thermal vibrations
  • Thermophilic enzymes


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