Co-solvent effects on reaction rate and reaction equilibrium of an enzymatic peptide hydrolysis-Reference-Cited by-同舟云学术

Co-solvent effects on reaction rate and reaction equilibrium of an enzymatic peptide hydrolysis

Published:2018 Issue:16 Volume:20 Page:11317-11326
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Wangler A.¹²³⁴,Canales R.¹²³⁴⁵^ORCID,Held C.¹²³⁴^ORCID,Luong T. Q.⁶²³⁴,Winter R.⁶²³⁴^ORCID,Zaitsau D. H.⁷⁸⁹¹⁰⁴^ORCID,Verevkin S. P.⁷⁸⁹¹⁰⁴^ORCID,Sadowski G.¹²³⁴^ORCID

Affiliation:

1. Department BCI, Laboratory of Thermodynamics

2. TU Dortmund University

3. 44227 Dortmund

4. Germany

5. Departamento de Ingeniería Química y Bioprocesos

6. Department of Chemistry and Chemical Biology

7. Department of Physical Chemistry

8. Institute of Chemistry

9. University of Rostock

10. 18059 Rostock

Abstract

This work presents an approach that expresses the Michaelis constant KaM and the equilibrium constant K_th of an enzymatic peptide hydrolysis based on thermodynamic activities instead of concentrations.

Funder

Russian Foundation for Basic Research

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CP/C7CP07346A

Reference47 articles.

1. Conformer Selection and Intensified Dynamics During Catalytic Turnover in Chymotrypsin

2. Influence of modulated structural dynamics on the kinetics of ?-chymotrypsin catalysis.