Global ETD Search
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Showing 1 to 5 of 5 for “"Acetohydroxyacid synthase"”.
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Investigation of the Evolutionary Aspects of Thiamin Diphosphate-Dependent Decarboxylases
… additional cofactors such as FAD in enzymes like acetohydroxyacid synthase (AHAS) but in others, like pyruvate decarboxylase (PDC), it has lost this function completely. The work presented here focuses on ThDP-dependent decarboxylases. In this thesis, several evolutionary aspects of this group of …
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Non-target-site resistance to ALS inhibitors in waterhemp
The acetolactate synthase (ALS) enzyme, or acetohydroxyacid synthase (AHAS) enzyme, is an essential enzyme in branched-chain amino acid biosynthesis, and is the target site of five families of herbicides referred to as ALS inhibitors. Waterhemp (Amaranthus tuberculatus) is considered one of the …
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Factors affecting common lambsquarters' tolerance to imazethapyr
… and metabolism. Since acetolactate synthase (ALS, or acetohydroxyacid synthase) (EC 4.1.3.18) is the target enzyme of imazethapyr, the activity of this enzyme was also examined in vivo and in vitro. In vitro studies showed higher ALS activity in extracts from common lambsquarters …
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Synthesis and structure-activity relationship studies of novel anti-infectives for cross screening in tuberculosis and malaria disease models
… sites were designed for synthesis. Acetolactate synthase (also known as acetohydroxyacid synthase) is the enzyme which catalyzes the first step in the biosynthesis of branched chain amino acids, including valine, leucine and isoleucine. It is a target for several classes of herbicides including …
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Investigating the Double-Edged Sword of Rifampicin Resistance in Mycobacterium Tuberculosis
… the gene encoding the thiamine diphosphate (TPP) synthase, is a top collateral vulnerability in βS450L Mtb, and a top collateral invulnerability in these fast, hypo-terminating RifR mutants. We determined that the enhanced vulnerability of thiS in βS450L Mtb is due to the depletion of branch chain …