Linked Life Data

15134652

Source:http://linkedlifedata.com/resource/pubmed/id/15134652

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-5-11
pubmed:abstractText
F(1)-ATPase catalyses ATP hydrolysis and converts the cellular chemical energy into mechanical rotation. The hydrolysis reaction in F(1)-ATPase does not follow the widely believed Michaelis-Menten mechanism. Instead, the hydrolysis mechanism behaves in an ATP-dependent manner. We develop a model for enzyme kinetics and hydrolysis cooperativity of F(1)-ATPase which involves the binding-state changes to the coupling catalytic reactions. The quantitative analysis and modeling suggest the existence of complex cooperative hydrolysis between three different catalysis sites of F(1)-ATPase. This complexity may be taken into account to resolve the arguments on the binding change mechanism in F(1)-ATPase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
1698
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
197-202
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Complex cooperativity of ATP hydrolysis in the F(1)-ATPase molecular motor.
pubmed:affiliation
Centre for Molecular Simulation, Swinburne University of Technology, PO Box 218, Hawthorn, Melbourne, Victoria 3122, Australia. ming@it.swin.edu.au
pubmed:publicationType
Journal Article