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Cover Feature: Thermal Adaptation of Enzymes: Impacts of Conformational Shifts on Catalytic Activation Energy and Optimum Temperature (Chem. Eur. J. 44/2020)
Author(s) -
Maffucci Irene,
Laage Damien,
Sterpone Fabio,
Stirnemann Guillaume
Publication year - 2020
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.202003018
Subject(s) - melting temperature , enzyme , activation energy , work (physics) , cover (algebra) , thermal , catalysis , chemistry , thermodynamics , molecular dynamics , materials science , computational chemistry , biochemistry , physics , mechanical engineering , engineering , composite material
Evolution has led to conserved enzyme families that efficiently catalyze the same chemical reaction but in radically different thermal environments. In particular, some enzymes need to be stable and to work in very hot conditions that usually lead to protein melting. Using atomistic simulations and analytic modeling, it is shown that the temperature‐dependence of the enzyme accessible conformations plays a key role in the determination of its optimum working temperature, that cannot be predicted from its melting temperature alone. More information can be found in the Full Paper by D. Laage, F. Sterpone, G. Stirnemann et al. on page 10045.