Linked Life Data

6626248

Source:http://linkedlifedata.com/resource/pubmed/id/6626248

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
18
pubmed:dateCreated
1983-11-23
pubmed:abstractText
A non-specific N-methyltransferase was demonstrated in dog liver. This enzyme is different from other N-methylating systems, especially in terms of substrate and species specificity. The enzyme catalyzes the methylation of a variety of endogenous and exogenous amines; of the compounds studied, SK&F 64139 (7,8-dichloro-1,2,3,4-tetrahydroisoquinoline) was found to be the best substrate. The enzyme utilized S-adenosylmethionine but not 5-methyltetrahydrofolate as a methyl donor, and it had a pH optimum at 8.0. Study of SK&F 64139 with the partially purified enzyme indicated that this dog liver N-methyltransferase had very low Km and high Vmax values for SK&F 64139. Methylation of SK&F 64139 was not observed with the monkey or rat liver enzyme preparation. This finding is in accordance with the fact that SK&F 64139 is methylated extensively in the dog, but not in other species. The ability of this enzyme to methylate a number of arylalkylamines suggests its possible importance in drug biotransformation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2952
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2781-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Dog liver N-methyltransferase. A drug-metabolizing enzyme.
pubmed:publicationType
Journal Article, Comparative Study