Linked Life Data

7703233

Source:http://linkedlifedata.com/resource/pubmed/id/7703233

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
1995-5-10
pubmed:abstractText
A recent experimental study of human acetylcholinesterase has shown that the mutation of surface acidic residues has little effect on the rate constant for hydrolysis of acetylthiocholine. It was concluded, on this basis, that the reaction is not diffusion controlled and that electrostatic steering plays only a minor role in determining the rate. Here we examine this issue through Brownian dynamics simulations on Torpedo californica acetylcholinesterase in which the surface acidic residues homologous with those mutated in the human enzyme are artificially neutralized. The computed effects of the mutations on the rate constants reproduce quite well the modest effects of the mutations upon the measured encounter rates. Nonetheless, the electrostatic field of the enzyme is found to increase the rate constants by about an order of magnitude in both the wild type and the mutants. We therefore conclude that the mutation experiments do not disprove that electrostatic steering substantially affects the catalytic rate of acetylcholinesterase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
4
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4211-9
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Simulation of charge-mutant acetylcholinesterases.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla 92093-0365, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't