The universality of enzymatic rate-temperature dependency

Trends Biochem Sci. 2014 Jan;39(1):1-7. doi: 10.1016/j.tibs.2013.11.001. Epub 2013 Dec 5.


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.

Keywords: active-site preorganization; enzyme dynamics; rate temperature–dependency; thermal vibrations; thermophilic enzymes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptation, Biological
  • Archaeal Proteins / chemistry
  • Bacterial Proteins / chemistry
  • Biocatalysis
  • Catalytic Domain
  • Enzyme Stability
  • Enzymes / chemistry*
  • Enzymes / genetics
  • Evolution, Molecular
  • Kinetics
  • Temperature


  • Archaeal Proteins
  • Bacterial Proteins
  • Enzymes