Recombinant biotin carboxylase domains for identification of Acetyle CoA carboxylase inhibitors
AssigneeCropsolution, Inc.
InventorsTedd E. Elich, Sandra L. Volrath, Stephanie C. Weatherly
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Abstract
A peptide comprising an Acetyl CoA carboxylase (ACCase) having a deleted biotin binding domain, having a deleted carboxy transferase domain, and having a functional biotin carboxylase (BC) domain is described. A nucleic acid that encodes the peptide described above and a recombinant host cell that contains the nucleic acid and expresses the encoded peptide is also described. A method of identifying Acetyl CoA carboxylase inhibitors, fungicides, and herbicides is also described herein.
Claims8
An isolated peptide comprising an Acetyl CoA carboxylase (ACCase) having a nonfunctional biotin binding domain, having a nonfunctional carboxy transferase domain, and having a functional biotin carboxylase domain, wherein said peptide is a monomer and binds to soraphen, and wherein said ACCase is selected from the group consisting of mammal, insect, yeast, Ascomycota, Basidiomycota. and Oomycota ACCase.
An isolated peptide consisting essentially of a functional Acetyl CoA carboxylase (ACCase) biotin carboxylase domain, wherein said functional biotin carboxylase domain is a monomer and binds to soraphen and wherein said functional ACCase biotin carboxylase domain is selected from the group consisting of:
- mammal, insect, yeast, Ascomycota, Basidiomycota, and Oomycota ACCase.
Dependencies are inferred from the claim text.