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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1995-7-5
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pubmed:abstractText |
A comparison is made of the kinetic characteristics of acetolactate synthase (EC 4.1.3.18) in extracts from Columbia wild type and four near-isogenic, herbicide-resistant mutants of Arabidopsis thaliana (L.) Heynh. The mutants used were the chlorsulfuron-resistant GH50 (csr1-1), the imazapyr-resistant GH90 (csr1-2), the triazolopyrimidine-resistant Tzp5 (csr1-3) and the multiherbicide-resistant, double mutant GM4.8 (csr1-4), derived from csr1-1 and csr1-2 by intragenic recombination (G. Mourad et al. 1994, Mol. Gen. Genet. 243, 178-184). Kmapp and Vmax values for the substrate pyruvate were unaffected by any of the mutations giving rise to herbicide resistance. Feedback inhibition by L-valine (L-Val), L-leucine (L-Leu) and L-isoleucine (L-Ile) of acetolactate synthase extracted from wild type and mutants fitted a mixed competitive pattern most closely. Ki values for L-Val, L-Leu and L-Ile inhibition were not significantly different from wild type in extracts from csr1-1, csr1-2, and csr1-3. Ki values were significantly higher than wild type by two- and five-fold, respectively, for csr1-4 with L-Val and L-Leu but not L-Ile. GM4.8 (csr1-4) plants were also highly resistant in their growth to added L-Val and L-Leu.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
B
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetolactate Synthase,
http://linkedlifedata.com/resource/pubmed/chemical/Isoleucine,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Pyruvates,
http://linkedlifedata.com/resource/pubmed/chemical/Pyruvic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Valine
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pubmed:status |
MEDLINE
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pubmed:issn |
0032-0935
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
196
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
64-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7767237-Acetolactate Synthase,
pubmed-meshheading:7767237-Alleles,
pubmed-meshheading:7767237-Arabidopsis,
pubmed-meshheading:7767237-Isoleucine,
pubmed-meshheading:7767237-Kinetics,
pubmed-meshheading:7767237-Leucine,
pubmed-meshheading:7767237-Mutation,
pubmed-meshheading:7767237-Pyruvates,
pubmed-meshheading:7767237-Pyruvic Acid,
pubmed-meshheading:7767237-Valine
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pubmed:year |
1995
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pubmed:articleTitle |
A double mutant allele, csr1-4, of Arabidopsis thaliana encodes an acetolactate synthase with altered kinetics.
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pubmed:affiliation |
Department of Biology, Indiana-Purdue University, Fort Wayne 46805-1499, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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