Peptide bond cis/trans isomerases: a biocatalysis perspective of conformational dynamics in proteins.
Top Curr Chem
; 328: 35-67, 2013.
Article
em En
| MEDLINE
| ID: mdl-21598101
ABSTRACT
Peptide bond cis/trans isomerases (PCTIases) catalyze an intrinsically slow rotational motion taking part in the conformational dynamics of a protein backbone in all of its folding states. In this way, PCTIases assist other proteins to shape their functionally active structure. They have been associated with viral, bacterial, and parasitic infection, signal transduction, cell differentiation, altered metabolic activity, apoptosis, and many other physiological and pathophysiological processes. The need to understand, characterize, and control biochemical steps which contribute to the folding of proteins is a problem being addressed in many laboratories today. This review discusses the biochemical basis that the peptidyl prolyl cis/trans isomerase (PPIase) family of PCTIases uses for the control of bioactivity. Special emphasis is given to recent developments in the field of biocatalytic features of PPIases, the mechanism of catalysis, and enzyme inhibition.
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Cis-trans-Isomerases
Idioma:
En
Revista:
Top Curr Chem
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
Alemanha