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Are the Catalytic Properties of Enzymes from Piezophilic Organisms Pressure Adapted?

Hay, Sam, Evans, Rhiannon Mari, Levy, Colin, Loveridge, Edric Joel, Wang, Xi, Leys, David, Allemann, Rudolf Konrad ORCID: and Scrutton, Nigel S. 2009. Are the Catalytic Properties of Enzymes from Piezophilic Organisms Pressure Adapted? ChemBioChem 10 (14) , pp. 2348-2353. 10.1002/cbic.200900367

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We report the crystal structure of dihydrofolate reductase (DHFR) from the psychropiezophilic bacterium Moritella profunda, which was isolated from the deep ocean at 2 °C and 280 bar. The structure is typical of a chromosomal DHFR and we were unable to identify any obvious structural features that would suggest pressure adaptation. In particular, the core regions of the enzyme are virtually identical to those of the DHFR from the mesophile Escherichia coli. The steady-state rate at pH 9, which is limited by hydride transfer at atmospheric pressure, is roughly constant between 1 and 750 bar, falling at higher pressures. However, the value of KM increases with increasing pressure, and as a result kcat/KM decreases over the entire pressure range studied. Isotope effect studies showed that increasing the pressure causes a change in the rate-limiting step of the reaction. We therefore see no evidence of pressure adaptation in either the structure or the activity of this enzyme.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Chemistry
Cardiff Catalysis Institute (CCI)
Subjects: Q Science > QD Chemistry
Uncontrolled Keywords: dihydrofolate reductase; enzyme catalysis; isotope effects; piezophile
Publisher: Wiley-Blackwell
ISSN: 1439-4227
Funders: BBSRC
Last Modified: 18 Oct 2022 14:25

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