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

The universality of enzymatic rate-temperature dependency.

Author information

1
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: mikael.elias@weizmann.ac.il.
2
Department of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel.
3
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
4
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. Electronic address: tawfik@weizmann.ac.il.

Erratum in

  • Trends Biochem Sci. 2014 Jun;39(6):299.

Abstract

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

PMID:
24315123
DOI:
10.1016/j.tibs.2013.11.001
[Indexed for MEDLINE]

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