{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T11:44:00Z","timestamp":1792496640861,"version":"4.5.0"},"reference-count":55,"publisher":"American Chemical Society (ACS)","issue":"20","license":[{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T00:00:00Z","timestamp":1790640000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-045"}],"funder":[{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["2003946"],"award-info":[{"award-number":["2003946"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"publisher","award":["2048875"],"award-info":[{"award-number":["2048875"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2026,10,20]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Acetohydroxyacid synthase (AHAS) is the first enzyme in the branched-chain amino acid biosynthesis pathway and is the target for more than 50 commercially deployed herbicides. This enzyme has also been suggested as a target for the discovery of novel antimicrobial and antifungal therapeutics. Dehydrophos, a natural product antibiotic, is a potential new lead inhibitor of AHASs for drug development, whereby the biologically active component is proposed to be methyl acetylphosphonate (MAP). MAP has been suggested as a pyruvate analog that inhibits ThDP-dependent enzymes, including AHAS. Here, the crystal structure of Saccharomyces cerevisiae AHAS in complex with MAP has been determined to 2.22 \u00c5 resolution, showing that it binds covalently with ThDP. We have also shown that MAP alone is effective in inhibiting the growth of uropathogenic Escherichia coli (UPEC) in cell susceptibility assays and that this activity is lost when exogenous branched-chain amino acids (BCAAs) are added. This suggests that AHAS is a target for the antibiotic activity of MAP and dehydrophos. Our crystal structure provides a starting point for the rational design of ThDP covalently bound AHAS inhibitors that are also structurally different from those that have been developed previously as commercial herbicides that inhibit AHAS.<\/jats:p>","DOI":"10.1021\/acs.biochem.6c00555","type":"journal-article","created":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T20:03:25Z","timestamp":1790712205000},"page":"3286-3298","source":"Crossref","is-referenced-by-count":0,"title":["The Active Component\nof Dehydrophos Covalently Binds\nto Acetohydroxyacid Synthase and Inhibits the Growth of Uropathogenic\n                    <i>Escherichia coli<\/i>"],"prefix":"10.1021","volume":"65","author":[{"given":"Xin","family":"Lin","sequence":"first","affiliation":[{"name":"The University of Queensland , , ,","place":["Brisbane, Australia, 4072 QLD"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sharon","family":"Chow","sequence":"additional","affiliation":[{"name":"The University of Queensland , , ,","place":["Brisbane, Australia, 4072 QLD"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul Malek","family":"Mirzayans","sequence":"additional","affiliation":[{"name":"The University of Queensland , , ,","place":["Brisbane, Australia, 4072 QLD"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jiahui","family":"Tng","sequence":"additional","affiliation":[{"name":"The University of Queensland , , ,","place":["Brisbane, Australia, 4072 QLD"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8619-0631","authenticated-orcid":true,"given":"Gerhard","family":"Schenk","sequence":"additional","affiliation":[{"name":"The University of Queensland , , ,","place":["Brisbane, Australia, 4072 QLD"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3834-7398","authenticated-orcid":true,"given":"Craig M.","family":"Williams","sequence":"additional","affiliation":[{"name":"The University of Queensland , , ,","place":["Brisbane, Australia, 4072 QLD"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8204-8408","authenticated-orcid":true,"given":"Luke W.","family":"Guddat","sequence":"additional","affiliation":[{"name":"The University of Queensland , , ,","place":["Brisbane, Australia, 4072 QLD"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"316","published-online":{"date-parts":[[2026,9,29]]},"reference":[{"key":"2026102007170879400_cit1","doi-asserted-by":"publisher","first-page":"929","DOI":"10.1099\/mic.0.034348-0","article-title":"Cytocidal amino acid starvation of Saccharomyces cerevisiae and Candida albicans acetolactate synthase (ilv2\u0394) mutants is influenced by the\ncarbon source and rapamycin","volume":"156","author":"Kingsbury","year":"2010","journal-title":"Microbiology"},{"key":"2026102007170879400_cit2","doi-asserted-by":"publisher","first-page":"1547","DOI":"10.1099\/mic.0.26928-0","article-title":"Cryptococcus neoformans Ilv2p confers resistance\nto sulfometuron methyl and is required for survival at 37 \u00b0C\nand in vivo","volume":"150","author":"Kingsbury","year":"2004","journal-title":"Microbiology"},{"key":"2026102007170879400_cit3","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1002251","article-title":"High-resolution\nphenotypic profiling defines genes\nessential for mycobacterial growth and cholesterol catabolism","volume":"7","author":"Griffin","year":"2011","journal-title":"PLoS Pathog."},{"key":"2026102007170879400_cit4","doi-asserted-by":"publisher","first-page":"E1091","DOI":"10.1073\/pnas.1616142114","article-title":"Comprehensive understanding\nof acetohydroxyacid synthase inhibition by different herbicide families","volume":"114","author":"Garcia","year":"2017","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026102007170879400_cit5","doi-asserted-by":"crossref","first-page":"1865","DOI":"10.1016\/B978-0-12-374367-1.00087-2","article-title":"Toxicology\nof triazolopyrimidine herbicides","volume-title":"Hayes\u2019\nHandbook of Pesticide Toxicology","author":"Billington","year":"2010"},{"key":"2026102007170879400_cit6","doi-asserted-by":"crossref","first-page":"1853","DOI":"10.1016\/B978-0-12-374367-1.00086-0","article-title":"Imidazolinones","volume-title":"Hayes\u2019 Handbook\nof Pesticide Toxicology","author":"Hess","year":"2010"},{"key":"2026102007170879400_cit7","doi-asserted-by":"publisher","first-page":"2330","DOI":"10.1021\/bi047980a","article-title":"Elucidating\nthe\nspecificity of binding of sulfonylurea herbicides to acetohydroxyacid\nsynthase","volume":"44","author":"McCourt","year":"2005","journal-title":"Biochemistry"},{"key":"2026102007170879400_cit8","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1006\/jmbi.2001.5419","article-title":"Crystal\nstructure of yeast acetohydroxyacid\nsynthase: a target for herbicidal inhibitors","volume":"317","author":"Pang","year":"2002","journal-title":"J. Mol. Biol."},{"key":"2026102007170879400_cit9","doi-asserted-by":"publisher","first-page":"7639","DOI":"10.1074\/jbc.M211648200","article-title":"Molecular basis of sulfonylurea herbicide\ninhibition of acetohydroxyacid synthase","volume":"278","author":"Pang","year":"2003","journal-title":"J.\nBiol. Chem."},{"key":"2026102007170879400_cit10","doi-asserted-by":"publisher","first-page":"569","DOI":"10.1073\/pnas.0508701103","article-title":"Herbicide-binding\nsites revealed in the structure of plant acetohydroxyacid synthase","volume":"103","author":"McCourt","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2026102007170879400_cit11","doi-asserted-by":"publisher","first-page":"2037","DOI":"10.1111\/febs.14102","article-title":"Crystal structure\nof plant acetohydroxyacid synthase, the target for several commercial\nherbicides","volume":"284","author":"Garcia","year":"2017","journal-title":"FEBS J."},{"key":"2026102007170879400_cit12","doi-asserted-by":"publisher","first-page":"4247","DOI":"10.1002\/anie.201511985","article-title":"Commercial\nherbicides can trigger\nthe oxidative inactivation of acetohydroxyacid synthase","volume":"55","author":"Lonhienne","year":"2016","journal-title":"Angew. Chem., Int. Ed."},{"key":"2026102007170879400_cit13","doi-asserted-by":"publisher","first-page":"E9649","DOI":"10.1073\/pnas.1809422115","article-title":"Commercial AHAS-inhibiting\nherbicides are promising drug leads for the treatment of human fungal\npathogenic infections","volume":"115","author":"Garcia","year":"2018","journal-title":"Proc. Natl. Acad. Sci.\nU.S.A."},{"key":"2026102007170879400_cit14","doi-asserted-by":"publisher","first-page":"71","DOI":"10.1021\/cb300631k","article-title":"Transition\nstates, analogues, and drug development","volume":"8","author":"Schramm","year":"2013","journal-title":"ACS\nChem. Biol."},{"key":"2026102007170879400_cit15","doi-asserted-by":"publisher","first-page":"18289","DOI":"10.1002\/chem.201704481","article-title":"Crystal\nstructures of Staphylococcus aureus ketol-acid reductoisomerase in complex with two transition state\nanalogues that have biocidal activity","volume":"23","author":"Patel","year":"2017","journal-title":"Chem.\n\u2013 Eur. J."},{"key":"2026102007170879400_cit16","unstructured":"Johnson, R. D.; Kastner, R. M.; Larsen, S. H.; Ose, E. E. 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Chem."},{"key":"2026102007170879400_cit22","doi-asserted-by":"publisher","first-page":"2895","DOI":"10.1046\/j.1432-1033.2003.03671.x","article-title":"Systematic characterization\nof mutations in yeast acetohydroxyacid synthase. Interpretation of\nherbicide-resistance data","volume":"270","author":"Duggleby","year":"2003","journal-title":"Eur. J. Biochem."},{"key":"2026102007170879400_cit23","doi-asserted-by":"crossref","DOI":"10.1002\/9781118540398","volume-title":"Evaluation of Enzyme\nInhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists","author":"Copeland","year":"2013"},{"key":"2026102007170879400_cit24","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1016\/0003-2697(89)90213-3","article-title":"Rapid measurement\nof binding constants and heats of binding using a new titration calorimeter","volume":"179","author":"Wiseman","year":"1989","journal-title":"Anal. 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D:Struct.\nBiol."},{"key":"2026102007170879400_cit27","doi-asserted-by":"publisher","first-page":"11981","DOI":"10.1002\/slct.201702128","article-title":"High resolution\ncrystal structures\nof the acetohydroxyacid synthase-pyruvate complex provide new insights\ninto its catalytic mechanism","volume":"2","author":"Lonhienne","year":"2017","journal-title":"ChemistrySelect"},{"key":"2026102007170879400_cit28","doi-asserted-by":"publisher","first-page":"5298","DOI":"10.1128\/IAI.00652-07","article-title":"Roles of\nserine accumulation and catabolism in the colonization of the murine\nurinary tract by Escherichia coli CFT073","volume":"75","author":"Anfora","year":"2007","journal-title":"Infect. Immun."},{"key":"2026102007170879400_cit29","doi-asserted-by":"publisher","first-page":"784","DOI":"10.1046\/j.1365-2672.2000.01017.x","article-title":"Susceptibility testing: accurate and reproducible minimum\ninhibitory concentration (MIC) and non-inhibitory concentration (NIC)\nvalues","volume":"88","author":"Lambert","year":"2000","journal-title":"J. Appl. Microbiol."},{"key":"2026102007170879400_cit30","doi-asserted-by":"publisher","first-page":"411","DOI":"10.1021\/ci960402j","article-title":"GraphPad\nPrism, data analysis, and scientific graphing","volume":"37","author":"Swift","year":"1997","journal-title":"J. Chem. Inf. Comput. Sci."},{"key":"2026102007170879400_cit31","doi-asserted-by":"publisher","first-page":"1035","DOI":"10.1016\/j.plantsci.2004.11.020","article-title":"Cyclopropane-1,1-dicarboxylate is\na slow-, tight-binding inhibitor of rice ketol-acid reductoisomerase","volume":"168","author":"Lee","year":"2005","journal-title":"Plant Sci."},{"key":"2026102007170879400_cit32","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1002\/9780470123072.ch5","article-title":"The behavior and\nsignificance of slow-binding enzyme\ninhibitors","volume":"61","author":"Morrison","year":"1988","journal-title":"Adv. Enzymol. Relat. Areas Mol.\nBiol."},{"key":"2026102007170879400_cit33","doi-asserted-by":"publisher","first-page":"317","DOI":"10.1038\/s41586-020-2514-3","article-title":"Structures of fungal and plant acetohydroxyacid\nsynthases","volume":"586","author":"Lonhienne","year":"2020","journal-title":"Nature"},{"key":"2026102007170879400_cit34","doi-asserted-by":"publisher","first-page":"857","DOI":"10.1104\/pp.109.141622","article-title":"Quantitative proteomics\nof seed filling\nin castor: comparison with soybean and rapeseed reveals differences\nbetween photosynthetic and nonphotosynthetic seed metabolism","volume":"151","author":"Houston","year":"2009","journal-title":"Plant Physiol."},{"key":"2026102007170879400_cit35","doi-asserted-by":"publisher","DOI":"10.1038\/msb.2011.48","article-title":"A dynamic model of proteome changes\nreveals new roles for transcript alteration in yeast","volume":"7","author":"Lee","year":"2011","journal-title":"Mol. Syst. Biol."},{"key":"2026102007170879400_cit36","doi-asserted-by":"publisher","first-page":"482","DOI":"10.1038\/nchembio.2077","article-title":"Metabolite\nconcentrations, fluxes\nand free energies imply efficient enzyme usage","volume":"12","author":"Park","year":"2016","journal-title":"Nat. Chem. Biol."},{"key":"2026102007170879400_cit37","doi-asserted-by":"publisher","first-page":"6368","DOI":"10.1021\/acs.analchem.4c04003","article-title":"Mechanistic characterization of covalent\nenzyme inhibition by isothermal titration calorimetry kinetic competition\n(ITC-KC)","volume":"97","author":"Hennecker","year":"2025","journal-title":"Anal. Chem."},{"key":"2026102007170879400_cit38","doi-asserted-by":"publisher","DOI":"10.1016\/j.bpj.2019.11.440","article-title":"The enthalpy of protein-ligand\ninteraction","volume":"118","author":"Zubrien","year":"2020","journal-title":"Biophys. 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Biochem."},{"key":"2026102007170879400_cit41","doi-asserted-by":"publisher","first-page":"872","DOI":"10.1126\/science.1101030","article-title":"A molecular\nswitch and proton wire synchronize the active sites in thiamine enzymes","volume":"306","author":"Frank","year":"2004","journal-title":"Science"},{"key":"2026102007170879400_cit42","doi-asserted-by":"publisher","first-page":"15296","DOI":"10.1074\/jbc.M600656200","article-title":"A thiamin-bound, pre-decarboxylation\nreaction intermediate analogue in the pyruvate dehydrogenase E1 subunit\ninduces large scale disorder-to-order transformations in the enzyme\nand reveals novel structural features in the covalently bound adduct","volume":"281","author":"Arjunan","year":"2006","journal-title":"J. Biol. Chem."},{"key":"2026102007170879400_cit43","doi-asserted-by":"publisher","first-page":"324","DOI":"10.1038\/nchembio788","article-title":"The catalytic cycle of a thiamin diphosphate enzyme\nexamined by cryocrystallography","volume":"2","author":"Wille","year":"2006","journal-title":"Nat. Chem.\nBiol."},{"key":"2026102007170879400_cit44","doi-asserted-by":"publisher","first-page":"E1945","DOI":"10.1073\/pnas.1714392115","article-title":"Structural insights into the mechanism of inhibition\nof AHAS by herbicides","volume":"115","author":"Lonhienne","year":"2018","journal-title":"Proc. Natl. Acad. Sci.\nU.S.A."},{"key":"2026102007170879400_cit45","doi-asserted-by":"publisher","first-page":"22487","DOI":"10.1021\/acs.jafc.4c04990","article-title":"Crystal\nstructures of Arabidopsis thaliana acetohydroxyacid\nsynthase in complex with the herbicide triasulfuron and two analogues\nwith herbicidal activity in field trials","volume":"72","author":"Cheng","year":"2024","journal-title":"J.\nAgric. Food Chem."},{"key":"2026102007170879400_cit46","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-022-31023-x","article-title":"Structural basis\nof resistance to herbicides that target acetohydroxyacid synthase","volume":"13","author":"Lonhienne","year":"2022","journal-title":"Nat. Commun."},{"key":"2026102007170879400_cit47","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1021\/acs.jcim.9b00863","article-title":"Catalytic\nrole of Gln202 in the carboligation reaction mechanism of yeast AHAS:\na QM\/MM study","volume":"60","author":"Mendoza","year":"2020","journal-title":"J. Chem. Inf. Model."},{"key":"2026102007170879400_cit48","doi-asserted-by":"publisher","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped\nBLAST and PSI-BLAST: a new\ngeneration of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"2026102007170879400_cit49","doi-asserted-by":"publisher","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence\nalignments using Clustal Omega","volume":"7","author":"Sievers","year":"2011","journal-title":"Mol. Syst. Biol."},{"key":"2026102007170879400_cit50","doi-asserted-by":"publisher","first-page":"1188","DOI":"10.1101\/gr.849004","article-title":"WebLogo: a sequence logo generator","volume":"14","author":"Crooks","year":"2004","journal-title":"Genome Res."},{"key":"2026102007170879400_cit51","doi-asserted-by":"crossref","unstructured":"Ortelli, M.; Prakapaite\u0301, R.; Mu\u0308ller, A.; Miele, S.; Fino, C.; Klimke, S.; Tschudin-Sutter, S.; Jenal, U.; Flores, C.; Bikard, D.\n          Genome-scale CRISPRi profiling reveals\nmetabolic vulnerabilities of uropathogenic Escherichia coli in human urine\n          bioRxiv\n          2025.","DOI":"10.1101\/2025.10.31.685768"},{"key":"2026102007170879400_cit52","doi-asserted-by":"publisher","first-page":"2439","DOI":"10.1042\/BCJ20200292","article-title":"Molecular architecture\nof the acetohydroxyacid synthase holoenzyme","volume":"477","author":"Zhang","year":"2020","journal-title":"Biochem. J."},{"key":"2026102007170879400_cit53","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1007\/BF02716867","article-title":"Growth of Mycobacterium smegmatis in minimal and complete media","volume":"2","author":"Gadagkar","year":"1980","journal-title":"J. Biosci."},{"key":"2026102007170879400_cit54","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1016\/j.chembiol.2009.11.017","article-title":"Biosynthesis of rhizocticins, antifungal\nphosphonate\noligopeptides produced by Bacillus subtilis ATCC6633","volume":"17","author":"Borisova","year":"2010","journal-title":"Chem. Biol."},{"key":"2026102007170879400_cit55","doi-asserted-by":"publisher","first-page":"1180","DOI":"10.1021\/acsinfecdis.4c01028","article-title":"Florasulam is a\npotent inhibitor of Mycobacterium tuberculosis acetohydroxyacid synthase\nand possesses in vivo antituberculosis activity","volume":"11","author":"Wun","year":"2025","journal-title":"ACS Infect. Dis."}],"container-title":["Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pubs.acs.org\/doi\/pdf\/10.1021\/acs.biochem.6c00555","content-type":"application\/pdf","content-version":"vor","intended-application":"unspecified"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/doi\/10.1021\/acs.biochem.6c00555\/68703063\/acs.biochem.6c00555.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pubs.acs.org\/bichaw\/article-pdf\/doi\/10.1021\/acs.biochem.6c00555\/68703063\/acs.biochem.6c00555.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T11:29:25Z","timestamp":1792495765000},"score":1,"resource":{"primary":{"URL":"https:\/\/pubs.acs.org\/bichaw\/article\/65\/20\/3286\/5441853\/The-Active-Component-of-Dehydrophos-Covalently"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9,29]]},"references-count":55,"journal-issue":{"issue":"20","published-online":{"date-parts":[[2026,9,29]]},"published-print":{"date-parts":[[2026,10,20]]}},"URL":"https:\/\/doi.org\/10.1021\/acs.biochem.6c00555","relation":{},"ISSN":["0006-2960","1520-4995"],"issn-type":[{"value":"0006-2960","type":"print"},{"value":"1520-4995","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,9,29]]}}}