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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1990-5-29
pubmed:abstractText
The herbicide suphometuron methyl inhibits the utilization of pyruvate and 2-ketobutyrate by the branched-chain amino acid biosynthetic enzyme acetolactate synthase. Eighteen insertions of the transposon Tn10 into the genome of Salmonella typhimurium LT2 caused hypersensitivity to this herbicide. Five of these insertions conferred a partial auxotrophic requirement. Concurrent herbicide sensitivity and heat-labile pantothenate auxotrophy was due to panD::Tn10 mutations, while coincident sulphometuron methyl sensitivity and thiamin auxotrophy was attributable to thiA::Tn10 mutations. The phenotypes of these mutations suggested that coenzyme A and thiamin pyrophosphate availability modulated the cells' response to sulphometuron methyl. A model suggesting a key role for 2-ketobutyrate accumulation in herbicide action is supported by the function of thiamin pyrophosphate in 2-ketoacid metabolism and the known role of a 2-ketoacid in coenzyme A synthesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-1287
pubmed:author
pubmed:issnType
Print
pubmed:volume
135
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2209-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Leaky pantothenate and thiamin mutations of Salmonella typhimurium conferring suphometuron methyl sensitivity.
pubmed:affiliation
Central Research and Development Department, E. I. du Pont de Nemours and Company, Wilmington, DE 19880-0328.
pubmed:publicationType
Journal Article