Activity and molecular dynamics relationship within the family of human cholinesterases.
Phys Chem Chem Phys
; 14(19): 6764-70, 2012 May 21.
Article
em En
| MEDLINE
| ID: mdl-22395795
ABSTRACT
The temperature dependence of the dynamics of recombinant human acetylcholinesterase (hAChE) and plasma human butyrylcholinesterase (hBChE) is examined using elastic incoherent neutron scattering. These two enzymes belong to the same family and present 50% amino acid sequence identity. However, significantly higher flexibility and catalytic activity of hAChE when compared to the ones of hBChE are measured. At the same time, the average height of the potential barrier to the motions is increased in the hBChE, e.g. more thermal energy is needed to cross it in the latter case, which might be the origin of the increase in activation energy and the reduction in the catalytic rate of hBChE observed experimentally. These results suggest that the motions on the picosecond timescale may act as a lubricant for those associated with activity occurring on a slower millisecond timescale.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Acetilcolinesterase
/
Butirilcolinesterase
Limite:
Humans
Idioma:
En
Ano de publicação:
2012
Tipo de documento:
Article