Mechanism of biotin carboxylase inhibition by ethyl 4-[[2-chloro-5-(phenylcarbamoyl)phenyl]sulphonylamino]benzoate

References

• Organization WH. Global antimicrobial resistance surveillance system (glass) report: early implementation 2020. In. Global antimicrobial resistance surveillance system (glass) report: early implementation 2020; Geneva; 2020.
   Google Scholar
• CDC. Antibiotic resistance threats in the United States. In: Antibiotic resistance threats in the United States. Atlanta (GA): U.S. Department of Health and Human Services; 2019.
   Google Scholar
• CDC. Antibiotic resistance threats in the United States, 2013. In: Antibiotic resistance threats in the United States. Atlanta (GA): U.S. Centers for Disease Control and Prevention; 2013.
   Google Scholar
• Cassini A, Högberg LD, Plachouras D, et al. Attributable deaths and disability-adjusted life-years caused by infections with antibiotic-resistant bacteria in the eu and the European economic area in 2015: a population-level modelling analysis. Lancet Infect Dis 2019;19:56–66.
   PubMed Web of Science ®Google Scholar
• Renner LD, Zan J, Hu LI, et al. Detection of eskape bacterial pathogens at the point of care using isothermal DNA-based assays in a portable degas-actuated microfluidic diagnostic assay platform. Appl Environ Microbiol 2017;83:e02449–02416.
   PubMed Web of Science ®Google Scholar
• Pendleton JN, Gorman SP, Gilmore BF. Clinical relevance of the eskape pathogens. Expert Rev Anti Infect Ther 2013;11:297–308.
   PubMed Web of Science ®Google Scholar
• Rice LB. Federal funding for the study of antimicrobial resistance in nosocomial pathogens: no eskape. J Infect Dis 2008:197:1079–81.
   PubMed Web of Science ®Google Scholar
• Santajit S, Indrawattana N. Mechanisms of antimicrobial resistance in eskape pathogens. BioMed Res Int 2016:2016:2475067.
   PubMed Web of Science ®Google Scholar
• Delcour AH. Outer membrane permeability and antibiotic resistance. Biochimica et biophysica acta 2009:1794:808–16.
   PubMed Web of Science ®Google Scholar
• Miller SI. Antibiotic resistance and regulation of the gram-negative bacterial outer membrane barrier by host innate immune molecules. mBio 2016;7:e01541–01516.
   PubMed Web of Science ®Google Scholar
• Breijyeh Z, Jubeh B, Karaman R. Resistance of gram-negative bacteria to current antibacterial agents and approaches to resolve it. Molecules 2020;25:1340.
   PubMed Web of Science ®Google Scholar
• Aslam B, Wang W, Arshad MI, et al. Antibiotic resistance: a rundown of a global crisis. Infect drug Resist 2018:11;1645–58.
   PubMed Web of Science ®Google Scholar
• Coates ARM, Halls G, Hu Y. Novel classes of antibiotics or more of the same? Br J Pharmacol 2011:163:184–94.
   PubMed Web of Science ®Google Scholar
• Infectious Diseases Society of A. The 10 × 20 initiative: pursuing a global commitment to develop 10 new antibacterial drugs by 2020. Clin Infect Dis 2010;50:1081–83.
   PubMed Web of Science ®Google Scholar
• Talbot GH, Jezek A, Murray BE, et al. The infectious diseases society of America’s 10 × ‘20 initiative (10 new systemic antibacterial agents us food and drug administration approved by 2020): is 20 × 20 a possibility? Clin Infect Dis 2019;69:1–11.
   PubMed Web of Science ®Google Scholar
• Yao J, Rock CO. How bacterial pathogens eat host lipids: implications for the development of fatty acid synthesis therapeutics. J Biol Chem 2015:290:5940–5946.
   PubMed Web of Science ®Google Scholar
• Parsons JB, Rock CO. Is bacterial fatty acid synthesis a valid target for antibacterial drug discovery? Curr Opin Microbiol 2011;14:544–49.
   PubMed Web of Science ®Google Scholar
• Turner KH, Wessel AK, Palmer GC, et al. Essential genome of pseudomonas aeruginosa in cystic fibrosis sputum. Proc Natl Acad Sci USA 2015:112:4110–15.
   PubMed Web of Science ®Google Scholar
• Parsons JB, Frank MW, Subramanian C, et al. Metabolic basis for the differential susceptibility of gram-positive pathogens to fatty acid synthesis inhibitors. Proc Natl Acad Sci USA 2011:108:15378–83.
   PubMed Web of Science ®Google Scholar
• Raetz CRH, Reynolds CM, Trent MS, Bishop RE. Lipid a modification systems in gram-negative bacteria. Ann Rev Biochem 2007;76:295–329.
   PubMed Web of Science ®Google Scholar
• Parsons JB, Rock CO. Bacterial lipids: metabolism and membrane homeostasis. Prog Lipid Res 2013;52:249–76.
   PubMed Web of Science ®Google Scholar
• Cronan JE, Waldrop GL. Multi-subunit acetyl-coa carboxylases. Prog Lipid Res 2002;41:407–35.
   PubMed Web of Science ®Google Scholar
• Campbell JW, John E. Cronan J. Bacterial fatty acid biosynthesis: targets for antibacterial drug discovery. Ann Rev Microbiol 2001;55:305–32.
   PubMed Web of Science ®Google Scholar
• Freiberg C, Brunner NA, Schiffer G, et al. Identification and characterization of the first class of potent bacterial acetyl-coa carboxylase inhibitors with antibacterial activity. J Biol Chem 2004:279:26066–73.
   PubMed Web of Science ®Google Scholar
• Mochalkin I, Miller JR, Narasimhan L, et al. Discovery of antibacterial biotin carboxylase inhibitors by virtual screening and fragment-based approaches. ACS Chem Biol 2009;4:473–83.
   PubMed Web of Science ®Google Scholar
• Cheng CC, Shipps GW, Yang Z, et al. Discovery and optimization of antibacterial accc inhibitors. Bioorg Med Chem Lett 2009;19:6507–14.
   PubMedGoogle Scholar
• Miller JR, Dunham S, Mochalkin I, et al. A class of selective antibacterials derived from a protein kinase inhibitor pharmacophore. Proc Natl Acad Sci USA 2009:106:1737–42.
   PubMed Web of Science ®Google Scholar
• Wallace J, Bowlin NO, Mills DM, et al. Discovery of bacterial fatty acid synthase type II inhibitors using a novel cellular bioluminescent reporter assay. Antimicrob Agents Chemother 2015;59:5775–87.
   PubMed Web of Science ®Google Scholar
• Blanchard CZ, Lee YM, Frantom PA, Waldrop GL. Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin. Biochemistry 1999;38:3393–400.
   PubMed Web of Science ®Google Scholar
• Broussard TC, Price AE, Laborde SM, Waldrop GL. Complex formation and regulation of Escherichia coli acetyl-coa carboxylase. Biochemistry 2013;52:3346–57.
   PubMed Web of Science ®Google Scholar
• Blanchard CZ, Waldrop GL. Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-coa carboxylase. J Biol Chem 1998:273:19140–45.
   PubMed Web of Science ®Google Scholar
• Webb MR. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc Natl Acad Sci USA 1992;89:4884–87.
   PubMed Web of Science ®Google Scholar
• Cleland WW. Statistical analysis of enzyme kinetic data. Methods Enzymol 1979:63;103–38.
   PubMedGoogle Scholar
• Leatherbarrow RJ. Enzfitter: a non-linear regression data analysis program for the IBM PC and true compatibles; manuel. Biosoft 1987.
   Google Scholar
• Sterling T, Irwin JJ. Zinc 15-ligand discovery for everyone. J Chem Inform Model 2015;55:2324–37.
   PubMed Web of Science ®Google Scholar
• Morris GM, Huey R, Lindstrom W, et al. Autodock4 and autodocktools4: automated docking with selective receptor flexibility. J Comput Chem 2009;30:2785–91.
   PubMed Web of Science ®Google Scholar
• Feinstein WP, Brylinski M. Calculating an optimal box size for ligand docking and virtual screening against experimental and predicted binding pockets. J Cheminform 2015;7:18.
   PubMed Web of Science ®Google Scholar
• Broussard TC, Pakhomova S, Neau DB, et al. Structural analysis of substrate, reaction intermediate, and product binding in haemophilus influenzae biotin carboxylase. Biochemistry 2015;54:3860–70.
   PubMed Web of Science ®Google Scholar
• Trott O, Olson AJ. Autodock vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem 2010;31:455–61.
   PubMed Web of Science ®Google Scholar
• O’Boyle NM, Banck M, James CA, et al. Open babel: an open chemical toolbox. J Cheminformatics 2011;3:33.
   PubMed Web of Science ®Google Scholar
• Schrodinger, LLC. The pymol molecular graphics system, version 1.8. In: The pymol molecular graphics system, version 1.8; November; 2015.
   Google Scholar
• Yonetani T, Theorell H. Studies on liver alcohol hydrogenase complexes. 3. Multiple inhibition kinetics in the presence of two competitive inhibitors. Arch Biochem Biophys 1964:106;243–51.
   PubMed Web of Science ®Google Scholar
• Dimroth P, Guchhait RB, Stoll E, Lane MD. Enzymatic carboxylation of biotin: molecular and catalytic properties of a component enzyme of acetyl coa carboxylase. Proc Natl Acad Sci 1970;67:1353–60.
   PubMed Web of Science ®Google Scholar
• Cleland WW. Determining the chemical mechanisms of enzyme-catalyzed reactions by kinetic studies. Adv Enzymol Relat Areas Mol Biol 1977:45;273–387.
   PubMedGoogle Scholar
• Tipton PA, Cleland WW. Catalytic mechanism of biotin carboxylase: steady-state kinetic investigations. Biochemistry 1988;27:4317–25.
   PubMed Web of Science ®Google Scholar
• Weeks G, Wakil SJ. Studies on the mechanism of fatty acid synthesis: xviii. Preparation and general properties of the enoyl acyl carrier protein reductases from Escherichia coli. J Biol Chem 1968:243:1180–9.
   PubMed Web of Science ®Google Scholar
• Quemard A, Sacchettini JC, Dessen A, et al. Enzymic characterization of the target for isoniazid in mycobacterium tuberculosis. Biochemistry 1995;34:8235–41.
   PubMed Web of Science ®Google Scholar
• Ward WHJ, Holdgate GA, Rowsell S, et al. Kinetic and structural characteristics of the inhibition of enoyl (acyl carrier protein) reductase by triclosan. Biochemistry 1999;38:12514–25.
   PubMed Web of Science ®Google Scholar
• Heath RJ, Rubin JR, Holland DR, et al. Mechanism of triclosan inhibition of bacterial fatty acid synthesis*. J Biol Chem 1999:274:11110–14.
   PubMed Web of Science ®Google Scholar
• Silvers MA, Robertson GT, Taylor CM, Waldrop GL. Design, synthesis, and antibacterial properties of dual-ligand inhibitors of acetyl-coa carboxylase. J Med Chem 2014;57:8947–59.
   PubMed Web of Science ®Google Scholar
• Vasiliou V, Vasiliou K, Nebert DW. Human ATP-binding cassette (abc) transporter family. Hum Genomics 2009;3:281–290.
   PubMedGoogle Scholar
• Umate P, Tuteja N, Tuteja R. Genome-wide comprehensive analysis of human helicases. Commun Integr Biol 2011;4:118–137.
   PubMedGoogle Scholar
• Duong-Ly KC, Peterson JR. The human kinome and kinase inhibition. Curr Protocols Pharmacol, 2013;Unit2.9:60.
   Google Scholar
• Sloane V, Waldrop GL. Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase. J Biol Chem 2004:279:15772–78.
   PubMed Web of Science ®Google Scholar
• Tong L. Structure and function of biotin-dependent carboxylases. Cell Mol Life Sci 2013;70:863–91.
   PubMed Web of Science ®Google Scholar