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• W2171466907 abstract "Acetolactate synthase (ALS) is the first common enzyme in the biosynthesis of L-leucine, L-isoleucine, and L-valine. The wild-type ALS gene fromNicotiana tabacumwas cloned into the bacterial expression vector pGEX-2T. The resulting recombinant plasmid pGEX-ALS2 was used to transformEscherichia colistrain XL1-Blue, and the wild-type tobacco ALS (wALS) was expressed in the bacteria as a protein fused with glutathioneS-transferase (GST). The fusion product GST-wALS was purified in a single step on a glutathione-Sepharose column. The purified GST-wALS was sensitive to a sulfonylurea herbicide, and was lost its sensitivity to end products, L-valine, L-leucine and L-isoleucine. These results suggest that the purified recombinant tobacco ALS was functionally active, and that the sulfonylureas may not bind to the feedback regulatory site on the plant ALS." @default.
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• W2171466907 date "1997-05-01" @default.
• W2171466907 modified "2023-09-26" @default.
• W2171466907 title "Soluble Overexpression inEscherichia coli,and Purification and Characterization of Wild-Type Recombinant Tobacco Acetolactate Synthase" @default.
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• W2171466907 doi "https://doi.org/10.1006/bbrc.1997.6678" @default.
• W2171466907 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9175749" @default.
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