Linked Life Data

17401532

Source:http://linkedlifedata.com/resource/pubmed/id/17401532

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-5-23
pubmed:abstractText
We and others have observed that substrates for copper-containing amine oxidases cause substrate inhibition at high concentrations. Through use of a novel "pseudoquantitative" rapid equilibrium approach, kinetic analyses with human and bovine enzymes indicate that these effects are consistent with substrates binding to oxidised and reduced enzyme forms. Small cations compete with binding of substrates to oxidised and reduced enzyme, influencing both substrate turnover and substrate inhibition patterns. Cations reduce affinity of the resting bovine enzyme for spermidine, but not benzylamine, indicating that the predominant effect of cations on substrate oxidation results from binding to an anionic site outside the active site. However, binding of cations to the active site of the reduced form of both enzymes attenuates substrate inhibition with both spermidine and benzylamine. Our observations have significant practical implications for researchers assaying kinetic behaviour of these enzymes, and particularly those developing novel inhibitors of human copper-containing amine oxidases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-9564
pubmed:author
pubmed:issnType
Print
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
733-41
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
The effects of buffer cations on interactions between mammalian copper-containing amine oxidases and their substrates.
pubmed:affiliation
Department of Pharmacology, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Canada. aholt@pmcol.ualberta.ca
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't