(Q59074354)

English

Origin of the herbicide binding site of acetolactate synthase

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Origin of the herbicide binding site of acetolactate synthase (English)

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John V. Schloss

1

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Lawrence M. Ciskanik

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2

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Drew E.Van Dyk

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3

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language of work or name

English

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publication date

January 1988

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published in

Nature

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volume

331

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issue

6154

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page(s)

360-362

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exact match

https://scigraph.springernature.com/pub.10.1038/331360a0

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cites work

Acetolactate synthase is the site of action of two sulfonylurea herbicides in higher plants.

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7 January 2021

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Site of action of chlorsulfuron: inhibition of valine and isoleucine biosynthesis in plants

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7 January 2021

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Imidazolinones: potent inhibitors of acetohydroxyacid synthase

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7 January 2021

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Imidazolinones and acetohydroxyacid synthase from higher plants: properties of the enzyme from maize suspension culture cells and evidence for the binding of imazapyr to acetohydroxyacid synthase in vivo

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Nucleotide sequence and deduced amino acid sequence of Escherichia coli pyruvate oxidase, a lipid-activated flavoprotein

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The nucleotide sequence of the ilvBN operon of Escherichia coli: sequence homologies of the acetohydroxy acid synthase isozymes

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The ilvB locus of Escherichia coli K-12 is an operon encoding both subunits of acetohydroxyacid synthase I.

1 reference

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Molecular basis of valine resistance in Escherichia coli K-12

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Molecular structure ofilvIHand its evolutionary relationship toilvGinEscherichia coliK12

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7 January 2021

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Nucleotide sequence of the yeast ILV2 gene which encodes acetolactate synthase

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7 January 2021

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Isolation and characterization of plant genes coding for acetolactate synthase, the target enzyme for two classes of herbicides.

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7 January 2021

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Reconstitution of the membrane-bound, ubiquinone-dependent pyruvate oxidase respiratory chain of Escherichia coli with the cytochrome d terminal oxidase

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7 January 2021

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Purification and properties of Salmonella typhimurium acetolactate synthase isozyme II from Escherichia coli HB101/pDU9.

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Reconstitution of the lipid-depleted pyruvate oxidase system of Escherichia coli: the palmitic acid effect

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7 January 2021

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In vivo function of Escherichia coli pyruvate oxidase specifically requires a functional lipid binding site

1 reference

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reference URL

https://api.crossref.org/works/10.1038%2F331360A0

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7 January 2021

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Identifiers

DOI

10.1038/331360A0

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Dimensions Publication ID

1007795469

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(Q59074354)

Origin of the herbicide binding site of acetolactate synthase

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