Linked Life Data

19100283

Source:http://linkedlifedata.com/resource/pubmed/id/19100283

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-2-3
pubmed:abstractText
Arginine kinase (AK; EC 2.7.3.3) is a key enzyme in the cellular energy metabolism of insects. Screening on potential effective inhibitors of AK may provide a pathway for novel, environmentally friendly insecticides. The results in this study indicated that rutin, as a noncompetitive inhibitor, interacts with AK mainly by a hydrophobic force forming an intermolecular complex with AK, which is according to the thermodynamic parameters obtained. Using a flexible docking method (AutoDock) the interaction between rutin and AK were further analyzed, which suggested in order to screen effective inhibitors, flexible active sites of AK (Ser63, Gly64, Val65, Tyr68) should be taken in account.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1879-0003
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
149-55
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
The effect of rutin on arginine kinase: inhibition kinetics and thermodynamics merging with docking simulation.
pubmed:affiliation
College of Life Science, Shandong Agricultural University, Tai'an, Shandong 271018, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't