Kinetic View of Enzyme Catalysis from Enhanced Sampling QM/MM Simulations.
J Chem Inf Model
; 64(9): 3953-3958, 2024 May 13.
Article
en 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.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Teoría Cuántica
/
Biocatálisis
Idioma:
En
Revista:
J Chem Inf Model
Asunto de la revista:
INFORMATICA MEDICA
/
QUIMICA
Año:
2024
Tipo del documento:
Article
País de afiliación:
Italia