The branched-chain amino acids are synthesized by plants, fungi and microorganisms, but not by animals. Therefore, the enzymes of this pathway are potential target sites for the development of antifungal agents, antimicrobials and herbicides. Most research has focused upon the first enzyme in this biosynthetic pathway, acetohydroxyacid synthase (AHAS) largely because it is the target site for many commercial herbicides. In this review we provide a brief overview of the important properties of each enzyme within the pathway and a detailed summary of the most recent AHAS research, against the perspective of work that has been carried out over the past 50 years.
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http://dx.doi.org/10.1007/s00726-005-0297-3 | DOI Listing |
Bioorg Med Chem
December 2024
Key Laboratory of Medical Laboratory Diagnostics of the Education Ministry, College of Laboratory Medicine, Chongqing Medical University, No. 1, Yixueyuan Road, Yuzhong Dist, Chongqing 400016, China. Electronic address:
Acetohydroxy acid synthase (AHAS) is a key enzyme that catalyzes the synthesis of branched-chain amino acids, which is indispensable for the survival and growth of Mycobacterium tuberculosis (Mtb). Aim to discover new AHAS inhibitors from natural products, here we performed computer assistant target-based screening for Mtb-AHAS inhibitors using Discovery Studio on TCMSP and SELLECK libraries. Mtb-AHAS structure was first simulated and verified for docking, and 80 compounds with top LIBDOCK and CDDOCK scores were obtained.
View Article and Find Full Text PDFPlanta
December 2024
AgResearch, Christchurch, New Zealand.
Herbicide application to plants heterozygous for herbicide resistance results in distorted segregation favoring resistant allele transmission resulting in a conditional gene drive. Brassica napus plants heterozygous for an allele conferring sulfonylurea resistance at a single locus exhibit normal Mendelian inheritance. However, following application of the herbicide, highly distorted segregation of herbicide resistance occurs among progeny.
View Article and Find Full Text PDFJ Antibiot (Tokyo)
December 2024
Department of Microbiology, College of Medicine, Chungnam National University, 266 Munhwa-ro, Jung-gu, Daejeon, 35015, South Korea.
Acetohydroxyacid synthase (AHAS), exclusively present in microorganisms and plants, is a promising target for several herbicides due to its catalytic role in the branched-chain amino acid biosynthetic pathway. Previous studies have shown that K13787, a pyrazolopyrimidine sulfonamide AHAS inhibitor, was moderately effective against pulmonary infection caused by M. tuberculosis and nontuberculous mycobacteria (NTM).
View Article and Find Full Text PDFAnal Bioanal Chem
December 2024
Botanical Institute and Botanic Gardens, Kiel University, D-24098, Kiel, Germany.
Acetohydroxyacid synthase (AHAS, EC 2.2.1.
View Article and Find Full Text PDFPest Manag Sci
February 2025
IFEVA - CONICET - Faculty of Agronomy, Department of Ecology, University of Buenos Aires (UBA), Buenos Aires, Argentina.
Background: Chlorsulfuron resistance and genetic dominance was evaluated in Raphanus raphanistrum genotypes homozygous (122-RR, 376-RR), heterozygous (122-RS, 376-RS) and compound heterozygous (122-R/376-R) for the target-site resistance mutations Ala-122-Tyr and Asp-376-Glu in the AHAS (acetohydroxyacid synthase) gene.
Results: At the AHAS level, 122-RR and 122-RS plants exhibited significantly higher I values than 376-RR and 376-RS plants, respectively. However, plants of the compound heterozygous genotype (122-R/376-R), showed no difference in AHAS activity compared to the 122-RS genotype but lower activity than the 122-RR genotype, and showed a nearly 400-fold greater I value than both genotypes (376-RR and 376-RS) carrying the 376-Glu allele.
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