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Extreme biophysics: Enzymes under pressure
Author(s) -
Huang Qi,
Rodgers Jocelyn M.,
Hemley Russell J.,
Ichiye Toshiko
Publication year - 2017
Publication title -
journal of computational chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.907
H-Index - 188
eISSN - 1096-987X
pISSN - 0192-8651
DOI - 10.1002/jcc.24737
Subject(s) - flexibility (engineering) , enzyme , mesophile , escherichia coli , adaptation (eye) , function (biology) , molecular dynamics , chemistry , psychrophile , biology , biophysics , biochemistry , microbiology and biotechnology , genetics , gene , bacteria , computational chemistry , statistics , mathematics , neuroscience
A critical question about piezophilic (pressure‐loving) microbes is how their constituent molecules maintain function under high pressure. Here, factors are examined that may lead to the increased activity under pressure in dihydrofolate reductase from the piezophilic Moritella profunda compared to the homologous enzyme from the mesophilic Escherichia coli . Molecular dynamics simulations are performed at various temperatures and pressures to examine how pressure affects the flexibility of the enzymes from these two microbes, since both stability and flexibility are necessary for enzyme activity. The results suggest that collective motions on the 10‐ns timescale are responsible for the flexibility necessary for “corresponding states” activity at the growth conditions of the parent organism. In addition, the results suggest that while the lower stability of many enzymes from deep‐sea microbes may be an adaptation for greater flexibility at low temperatures, high pressure may enhance their adaptation to low temperatures. © 2017 Wiley Periodicals, Inc.