Linked Life Data

15134347

Source:http://linkedlifedata.com/resource/pubmed/id/15134347

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
2004-5-11
pubmed:abstractText
Copper amine oxidase from lentil (Lens esculenta) seedlings was shown to catalyze the oxidative deamination of tyramine and three similar aromatic monoamines, benzylamine, phenylethylamine and 4-methoxyphenylethylamine. Tyramine, an important plant intermediate, was found to be both a substrate and an irreversible inhibitor of the enzyme whereas the other amines were not inhibitory. In the course of tyramine oxidation the enzyme gradually became inactivated with the concomitant appearance of a new absorption at 560 nm due to the formation of a stable adduct. Inactivation took place only in the presence of oxygen and was probably due to the reaction of the enzyme with the oxidation product of tyramine, p-hydroxyphenylacetaldehyde. The kinetic data obtained in this study indicate that tyramine represents a new interesting type of physiological mechanism-based inhibitor for plant copper amine oxidases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1431-6730
pubmed:author
pubmed:issnType
Print
pubmed:volume
385
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
323-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Inhibition of lentil copper/TPQ amine oxidase by the mechanism-based inhibitor derived from tyramine.
pubmed:affiliation
Department of Applied Sciences in Biosystems, University of Cagliari, 1-09042 Monserrato, CA, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't