A Multiperspective Approach to Solvent Regulation of Enzymatic Activity: 
HMG‐CoA Reductase

Dirkmann, Michael; Iglesias-Fernandez, 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; Sanchez-Garcia, Elsa; Schulz, Frank

doi:10.1002/cbic.201700596

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

A Multiperspective Approach to Solvent Regulation of Enzymatic Activity: HMG‐CoA Reductase

MPS-Authors

/persons/resource/persons221175

Iglesias-Fernandez, Javier
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Fakultät für Biologie, Universität Duisburg–Essen;

Muñoz, Victor
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Fakultät für Biologie, Universität Duisburg–Essen;

/persons/resource/persons146636

Sokkar, Pandian
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Fakultät für Biologie, Universität Duisburg–Essen;

/persons/resource/persons101503

Sanchez-Garcia, Elsa
Research Group Sánchez-García, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Fakultät für Biologie, Universität Duisburg–Essen;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Dirkmann, M., Iglesias-Fernandez, J., Muñoz, V., Sokkar, P., Rumancev, C., von Gundlach, A., et al. (2018). A Multiperspective Approach to Solvent Regulation of Enzymatic Activity: HMG‐CoA Reductase. Chembiochem, 19(2), 153-158. doi:10.1002/cbic.201700596.

Cite as: https://hdl.handle.net/21.11116/0000-0001-63F5-B

Abstract

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.