Mechanisms of the Aspartoacylase Catalytic Activity Regulation According to the Computer Modeling Results


Citar

Texto integral

Acesso aberto Acesso aberto
Acesso é fechado Acesso está concedido
Acesso é fechado Somente assinantes

Resumo

The results of molecular modeling allow us to associate the catalytic activity of aspartoacylase towards the hydrolysis of N-acetylaspartate with the dynamic properties of a dimeric molecule of the enzyme. The availability of the enzyme’s active site for the substrate is controlled by the conformational dynamics of the peptide loops that form a gate to the transport channel in one of the monomers. It is shown that this model explains the results of the experimental studies according to which the point mutation K213E does not affect the catalytic function of the enzyme.

Sobre autores

E. Kots

Department of Chemistry

Email: anemukhin@yahoo.com
Rússia, Moscow, 119991

M. Khrenova

Department of Chemistry

Email: anemukhin@yahoo.com
Rússia, Moscow, 119991

S. Lushchekina

Emanuel Institute of Biochemical Physics

Email: anemukhin@yahoo.com
Rússia, Moscow, 119334

A. Nemukhin

Department of Chemistry

Autor responsável pela correspondência
Email: anemukhin@yahoo.com
Rússia, Moscow, 119991

Arquivos suplementares

Arquivos suplementares
Ação
1. JATS XML

Declaração de direitos autorais © Allerton Press, Inc., 2018