Kinetic View of Enzyme Catalysis from Enhanced Sampling QM/MM Simulations.
J Chem Inf Model
; 64(9): 3953-3958, 2024 May 13.
Article
in En
| MEDLINE
| ID: mdl-38607669
ABSTRACT
The rate constants of enzyme-catalyzed reactions (kcat) are often approximated from the barrier height of the reactive step. We introduce an enhanced sampling QM/MM approach that directly calculates the kinetics of enzymatic reactions, without introducing the transition-state theory assumptions, and takes into account the dynamical equilibrium between the reactive and non-reactive conformations of the enzyme/substrate complex. Our computed kcat values are in order-of-magnitude agreement with the experimental data for two representative enzymatic reactions.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Quantum Theory
/
Biocatalysis
Language:
En
Journal:
J Chem Inf Model
Journal subject:
INFORMATICA MEDICA
/
QUIMICA
Year:
2024
Document type:
Article
Affiliation country: