Linked Life Data

998041

Source:http://linkedlifedata.com/resource/pubmed/id/998041

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1977-1-25
pubmed:abstractText
The phenylurea herbicide linuron is hydrolyzed by Bacillus sphaericus ATCC 12123 quantitatively forming 3,4-dichloroaniline, CO2, and N,O-dimethylhydroxylamine. The inducible enzyme responsible for this hydrolysis was purified to homogeneity as judged by polyacrylamide gel electrophoresis. Its molecular weight was 75 000 +/- 10%. Studies on its substrate specificity showed that either whole cells as the linuron-induced enzyme hydrolyze a large number of herbicidal and fungicidal acylanilides, the methoxysubstituted phenylureas and the phenylcarbamate propham at the carbonyl-aniline bond. This would classify the enzyme as an aryl acylamidase (E.C. 3.5.1). Hydrolysis of phenylamides by whole cells and by the enzyme is inhibited by different methylcarbamate and organophosphorus insecticides. Inhibition of hydrolysis of linuron by the aryl acylamidase by methylcarbamates is a competitive one.
pubmed:language
ger
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0300-9661
pubmed:author
pubmed:issnType
Print
pubmed:volume
162
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
138-44
pubmed:dateRevised
2009-6-5
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
[Hydrolysis of methoxysubstituted phenylureas, acylanilides and phenylcarbamates by a microbial aryl acylamidase (author's transl)].
pubmed:publicationType
Journal Article, English Abstract