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A Multiperspective Approach to Solvent Regulation of Enzymatic Activity: HMG‐CoA Reductase
Author(s) -
Dirkmann Michael,
IglesiasFernández Javier,
Muñoz Victor,
Sokkar Pandian,
Rumancev Christoph,
von Gundlach Andreas,
Krenczyk Oktavian,
Vöpel Tobias,
Nowack Julia,
Schroer Martin A.,
Ebbinghaus Simon,
Herrmann Christian,
Rosenhahn Axel,
SanchezGarcia Elsa,
Schulz Frank
Publication year - 2018
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700596
Subject(s) - reductase , chemistry , enzyme , solvent , hmg coa reductase , active center , cofactor , molecular dynamics , kinetic energy , enzyme catalysis , coenzyme a , stereochemistry , combinatorial chemistry , biochemistry , computational chemistry , physics , quantum mechanics
3‐Hydroxy‐3‐methylglutaryl–coenzyme A (HMG‐CoA) reductase was investigated in different organic cosolvents by means of kinetic and calorimetric measurements, molecular dynamics simulations, and small‐angle X‐ray scattering. The combined experimental and theoretical techniques were essential to complement each other's limitations in the investigation of the complex interaction pattern between the enzyme, different solvent types, and concentrations. In this way, the underlying mechanisms for the loss of enzyme activity in different water‐miscible solvents could be elucidated. These include direct inhibitory effects onto the active center and structural distortions.