Linked Life Data

9020976

Source:http://linkedlifedata.com/resource/pubmed/id/9020976

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-2-27
pubmed:abstractText
The nucleophilic attack by cysteine 12 in the low-molecular-weight protein tyrosine phosphatase is believed to be carried out by the thiolate anion form of this residue. We here study the energetics of proton transfer between the thiol group of cysteine 12 and a substrate phosphate oxygen atom, to examine the effects of the enzymic environment on the stability of the thiolate nucleophile. This is done by molecular dynamics and free energy perturbation simulations, utilizing the empirical valence bond method to describe the potential surface of the system. The calculations show that the protein environment significantly stabilizes the thiolate ion, thereby setting the stage for the nucleophilic attack. We compare these results with those from further simulations of a mutant enzyme, and demonstrate the importance of serine 19 in thiolate stabilization.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
118-27
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Energetics of nucleophile activation in a protein tyrosine phosphatase.
pubmed:affiliation
Department of Molecular Biology, Uppsala University Biomedical Centre, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't