Impact of intra-subunit domain-domain interactions on creatine kinase activity and stability.
FEBS Lett
; 580(16): 3835-40, 2006 Jul 10.
Article
em En
| MEDLINE
| ID: mdl-16797013
ABSTRACT
Creatine kinase (CK) is a key enzyme in vertebrate excitable tissues. In this research, five conserved residues located on the intra-subunit domain-domain interface were mutated to explore their role in the activity and structural stability of CK. The mutations of Val72 and Gly73 decreased both the activity and stability of CK. The mutations of Cys74 and Val75, which had no significant effect on CK activity and structure, gradually decreased the stability and reactivation of CK. Our results suggested that the mutations might modify the correct positioning of the loop contributing to domain-domain interactions, and result in decreased stability against denaturation.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Subunidades Proteicas
/
Creatina Quinase Forma MM
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article