A broad inhibitor of acyl-acyl carrier protein synthetases
The acyl-acyl carrier protein synthetase enzyme enables some bacteria to scavenge free fatty acids from the environment for direct use in lipids. This fatty acid recycling pathway can help pathogens circumvent fatty acid synthase (FAS) inhibition with established antibiotics and those in clinical de...
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| Veröffentlicht in: | Biochemistry and biophysics reports Jg. 35; S. 101549 |
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01.09.2023
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| Abstract | The acyl-acyl carrier protein synthetase enzyme enables some bacteria to scavenge free fatty acids from the environment for direct use in lipids. This fatty acid recycling pathway can help pathogens circumvent fatty acid synthase (FAS) inhibition with established antibiotics and those in clinical development. AasS enzymes are surprisingly hard to identify as they show high sequence similarity to other adenylate forming enzymes, and only a handful have been correctly annotated to date. Four recently discovered AasS enzymes from Gram negative bacteria, Chlamydia trachomatis, Neisseria gonorrhoeae, and Alistipes finegoldii, form distinct clusters in protein sequence similarity networks and have varying substrate preferences. We previously synthesized C10-AMS, an inhibitor of AasS that mimics the acyl-AMP reaction intermediate. Here we tested its ability to be broadly applicable to enzymes in this class, and found it inhibits all four newly annotated AasS enzymes. C10-AMS therefore provides a tool to study the role of AasS in fatty acid recycling in pathogenic bacteria as well as offers a platform for antibiotic development.
[Display omitted]
•Four recently annotated acyl-acyl carrier protein synthetases were tested in vitro.•These AasSs group in distinct clusters suggesting significant differences.•All AasSs were active with EcACP and C10 substrates.•C10-AMS inhibited all four AasS enzymes. |
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| AbstractList | The acyl-acyl carrier protein synthetase enzyme enables some bacteria to scavenge free fatty acids from the environment for direct use in lipids. This fatty acid recycling pathway can help pathogens circumvent fatty acid synthase (FAS) inhibition with established antibiotics and those in clinical development. AasS enzymes are surprisingly hard to identify as they show high sequence similarity to other adenylate forming enzymes, and only a handful have been correctly annotated to date. Four recently discovered AasS enzymes from Gram negative bacteria, Chlamydia trachomatis, Neisseria gonorrhoeae, and Alistipes finegoldii, form distinct clusters in protein sequence similarity networks and have varying substrate preferences. We previously synthesized C10-AMS, an inhibitor of AasS that mimics the acyl-AMP reaction intermediate. Here we tested its ability to be broadly applicable to enzymes in this class, and found it inhibits all four newly annotated AasS enzymes. C10-AMS therefore provides a tool to study the role of AasS in fatty acid recycling in pathogenic bacteria as well as offers a platform for antibiotic development. The acyl-acyl carrier protein synthetase enzyme enables some bacteria to scavenge free fatty acids from the environment for direct use in lipids. This fatty acid recycling pathway can help pathogens circumvent fatty acid synthase (FAS) inhibition with established antibiotics and those in clinical development. AasS enzymes are surprisingly hard to identify as they show high sequence similarity to other adenylate forming enzymes, and only a handful have been correctly annotated to date. Four recently discovered AasS enzymes from Gram negative bacteria, Chlamydia trachomatis, Neisseria gonorrhoeae, and Alistipes finegoldii, form distinct clusters in protein sequence similarity networks and have varying substrate preferences. We previously synthesized C10-AMS, an inhibitor of AasS that mimics the acyl-AMP reaction intermediate. Here we tested its ability to be broadly applicable to enzymes in this class, and found it inhibits all four newly annotated AasS enzymes. C10-AMS therefore provides a tool to study the role of AasS in fatty acid recycling in pathogenic bacteria as well as offers a platform for antibiotic development. [Display omitted] •Four recently annotated acyl-acyl carrier protein synthetases were tested in vitro.•These AasSs group in distinct clusters suggesting significant differences.•All AasSs were active with EcACP and C10 substrates.•C10-AMS inhibited all four AasS enzymes. The acyl-acyl carrier protein synthetase enzyme enables some bacteria to scavenge free fatty acids from the environment for direct use in lipids. This fatty acid recycling pathway can help pathogens circumvent fatty acid synthase (FAS) inhibition with established antibiotics and those in clinical development. AasS enzymes are surprisingly hard to identify as they show high sequence similarity to other adenylate forming enzymes, and only a handful have been correctly annotated to date. Four recently discovered AasS enzymes from Gram negative bacteria, Chlamydia trachomatis, Neisseria gonorrhoeae, and Alistipes finegoldii, form distinct clusters in protein sequence similarity networks and have varying substrate preferences. We previously synthesized C10-AMS, an inhibitor of AasS that mimics the acyl-AMP reaction intermediate. Here we tested its ability to be broadly applicable to enzymes in this class, and found it inhibits all four newly annotated AasS enzymes. C10-AMS therefore provides a tool to study the role of AasS in fatty acid recycling in pathogenic bacteria as well as offers a platform for antibiotic development.The acyl-acyl carrier protein synthetase enzyme enables some bacteria to scavenge free fatty acids from the environment for direct use in lipids. This fatty acid recycling pathway can help pathogens circumvent fatty acid synthase (FAS) inhibition with established antibiotics and those in clinical development. AasS enzymes are surprisingly hard to identify as they show high sequence similarity to other adenylate forming enzymes, and only a handful have been correctly annotated to date. Four recently discovered AasS enzymes from Gram negative bacteria, Chlamydia trachomatis, Neisseria gonorrhoeae, and Alistipes finegoldii, form distinct clusters in protein sequence similarity networks and have varying substrate preferences. We previously synthesized C10-AMS, an inhibitor of AasS that mimics the acyl-AMP reaction intermediate. Here we tested its ability to be broadly applicable to enzymes in this class, and found it inhibits all four newly annotated AasS enzymes. C10-AMS therefore provides a tool to study the role of AasS in fatty acid recycling in pathogenic bacteria as well as offers a platform for antibiotic development. The acyl-acyl carrier protein synthetase enzyme enables some bacteria to scavenge free fatty acids from the environment for direct use in lipids. This fatty acid recycling pathway can help pathogens circumvent fatty acid synthase (FAS) inhibition with established antibiotics and those in clinical development. AasS enzymes are surprisingly hard to identify as they show high sequence similarity to other adenylate forming enzymes, and only a handful have been correctly annotated to date. Four recently discovered AasS enzymes from Gram negative bacteria, Chlamydia trachomatis, Neisseria gonorrhoeae, and Alistipes finegoldii, form distinct clusters in protein sequence similarity networks and have varying substrate preferences. We previously synthesized C10-AMS, an inhibitor of AasS that mimics the acyl-AMP reaction intermediate. Here we tested its ability to be broadly applicable to enzymes in this class, and found it inhibits all four newly annotated AasS enzymes. C10-AMS therefore provides a tool to study the role of AasS in fatty acid recycling in pathogenic bacteria as well as offers a platform for antibiotic development. Image 1 • Four recently annotated acyl-acyl carrier protein synthetases were tested in vitro. • These AasSs group in distinct clusters suggesting significant differences. • All AasSs were active with EcACP and C10 substrates. • C10-AMS inhibited all four AasS enzymes. |
| ArticleNumber | 101549 |
| Author | Todorinova, Magdalena Beld, Joris Jaremko, Kara L. |
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| Cites_doi | 10.1016/j.chembiol.2014.08.015 10.1073/pnas.73.12.4374 10.1016/0167-4838(91)90138-P 10.1007/s00253-021-11546-x 10.1016/j.tim.2021.06.002 10.1074/jbc.M115.671008 10.3390/ph16030425 10.1016/j.sbi.2009.09.004 10.1111/mmi.14445 10.1016/S0021-9258(18)52372-3 10.2174/156802612799984571 10.1186/s12879-020-05307-w 10.1021/ml500475n 10.1016/S0960-894X(00)00360-7 10.1016/j.bmcl.2008.07.130 10.1074/jbc.M113.532804 10.1016/j.biochi.2017.06.015 10.1179/1973947812Y.0000000060 10.1074/jbc.M115.699462 10.1016/j.bbapap.2015.04.015 10.1101/gr.1239303 10.1042/BCJ20230161 10.1038/s41598-020-74731-4 10.1002/cmdc.201300209 10.1021/bi9719861 10.1021/bi060842w 10.1371/journal.pone.0143304 10.1038/nmeth.2089 10.1038/nature07772 10.1139/o90-154 |
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| Keywords | Fatty acid synthase Inhibitor Acyl-acyl carrier protein synthetase Acyl carrier protein Fatty acid recycling |
| Language | English |
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| References | Currie, Persaud, Rana, Platt, Beld, Jaremko (bib7) 2020; 10 Yao, Rock (bib1) 2017; 141 Schiebel, Chang, Shah, Lu, Liu, Pan, Hirschbeck, Tareilus, Eltschkner, Yu, Cummings, Knudson, Bommineni, Walker, Slayden, Sotriffer, Tonge, Kisker (bib4) 2014; 289 Cronan (bib29) 2023; 480 Schneider, Rasband, Eliceiri (bib27) 2012; 9 Yao, Bruhn, Frank, Lee, Rock (bib16) 2016; 291 Beld, Finzel, Burkart (bib11) 2014; 21 Newman, Rowley, Vander Hoorn, Wijesooriya, Unemo, Low, Stevens, Gottlieb, Kiarie, Temmerman (bib20) 2015; 10 Lu, Zhang, Tonge, Tan (bib15) 2008; 18 Bibens, Becker, Dassonville-Klimpt, Sonnet (bib5) 2023; 16 Jiang, Chan, Cronan (bib12) 2006; 45 Duckworth, Nelson, Aldrich (bib30) 2012; 12 Kengmo Tchoupa, Eijkelkamp, Peschel (bib2) 2022; 30 Radka, Frank, Rock, Yao (bib17) 2020; 113 Ueda (bib13) 1991; 1080 Yao, Dodson, Frank, Rock (bib18) 2015; 290 Byers, Holmes (bib10) 1990; 68 Post-Beittenmiller, Jaworski, Ohlrogge (bib24) 1991; 266 Ray, Cronan (bib9) 1976; 73 Brinster, Lamberet, Staels, Trieu-Cuot, Gruss, Poyart (bib6) 2009; 458 Tieu, Polyak, Paparella, Yap, Soares da Costa, Ng, Wang, Lumb, Bell, Turnidge, Wilce, Booker, Abell (bib26) 2015; 6 Gerlt, Bouvier, Davidson, Imker, Sadkhin, Slater, Whalen (bib21) 2015; 1854 Huai, Li, Chu, Liu, Liu, Zhang (bib19) 2020; 20 Tsuji, Harigaya, Lesse, Forrest, Ngo (bib28) 2013; 25 Forrest, Jarvest, Mensah, O'Hanlon, Pope, Sheppard (bib14) 2000; 10 Jones, Jarboe, Majer, Ma, Beld (bib23) 2021; 105 Schmelz, Naismith (bib8) 2009; 19 Shannon, Markiel, Ozier, Baliga, Wang, Ramage, Amin, Schwikowski, Ideker (bib22) 2003; 13 Quadri, Weinreb, Lei, Nakano, Zuber, Walsh (bib25) 1998; 37 Wang, Ma (bib3) 2013; 8 Quadri (10.1016/j.bbrep.2023.101549_bib25) 1998; 37 Kengmo Tchoupa (10.1016/j.bbrep.2023.101549_bib2) 2022; 30 Huai (10.1016/j.bbrep.2023.101549_bib19) 2020; 20 Shannon (10.1016/j.bbrep.2023.101549_bib22) 2003; 13 Radka (10.1016/j.bbrep.2023.101549_bib17) 2020; 113 Yao (10.1016/j.bbrep.2023.101549_bib18) 2015; 290 Yao (10.1016/j.bbrep.2023.101549_bib1) 2017; 141 Tieu (10.1016/j.bbrep.2023.101549_bib26) 2015; 6 Cronan (10.1016/j.bbrep.2023.101549_bib29) 2023; 480 Forrest (10.1016/j.bbrep.2023.101549_bib14) 2000; 10 Lu (10.1016/j.bbrep.2023.101549_bib15) 2008; 18 Byers (10.1016/j.bbrep.2023.101549_bib10) 1990; 68 Duckworth (10.1016/j.bbrep.2023.101549_bib30) 2012; 12 Schmelz (10.1016/j.bbrep.2023.101549_bib8) 2009; 19 Yao (10.1016/j.bbrep.2023.101549_bib16) 2016; 291 Newman (10.1016/j.bbrep.2023.101549_bib20) 2015; 10 Post-Beittenmiller (10.1016/j.bbrep.2023.101549_bib24) 1991; 266 Currie (10.1016/j.bbrep.2023.101549_bib7) 2020; 10 Jiang (10.1016/j.bbrep.2023.101549_bib12) 2006; 45 Schiebel (10.1016/j.bbrep.2023.101549_bib4) 2014; 289 Gerlt (10.1016/j.bbrep.2023.101549_bib21) 2015; 1854 Ueda (10.1016/j.bbrep.2023.101549_bib13) 1991; 1080 Beld (10.1016/j.bbrep.2023.101549_bib11) 2014; 21 Tsuji (10.1016/j.bbrep.2023.101549_bib28) 2013; 25 Wang (10.1016/j.bbrep.2023.101549_bib3) 2013; 8 Bibens (10.1016/j.bbrep.2023.101549_bib5) 2023; 16 Ray (10.1016/j.bbrep.2023.101549_bib9) 1976; 73 Jones (10.1016/j.bbrep.2023.101549_bib23) 2021; 105 Schneider (10.1016/j.bbrep.2023.101549_bib27) 2012; 9 Brinster (10.1016/j.bbrep.2023.101549_bib6) 2009; 458 |
| References_xml | – volume: 141 start-page: 30 year: 2017 end-page: 39 ident: bib1 article-title: Exogenous fatty acid metabolism in bacteria publication-title: Biochimie – volume: 480 start-page: 855 year: 2023 end-page: 873 ident: bib29 article-title: The acyl carrier proteins of lipid synthesis are busy having other affairs publication-title: Biochem. J. – volume: 13 start-page: 2498 year: 2003 end-page: 2504 ident: bib22 article-title: Cytoscape: a software environment for integrated models of biomolecular interaction networks publication-title: Genome Res. – volume: 266 start-page: 1858 year: 1991 end-page: 1865 ident: bib24 article-title: In vivo pools of free and acylated acyl carrier proteins in spinach. Evidence for sites of regulation of fatty acid biosynthesis publication-title: J. Biol. Chem. – volume: 12 start-page: 766 year: 2012 end-page: 796 ident: bib30 article-title: Adenylating enzymes in Mycobacterium tuberculosis as drug targets publication-title: Curr. Top. Med. Chem. – volume: 25 start-page: 32 year: 2013 end-page: 35 ident: bib28 article-title: Activity of AFN-1252, a novel FabI inhibitor, against Staphylococcus aureus in an in vitro pharmacodynamic model simulating human pharmacokinetics publication-title: J. Chemother. – volume: 289 start-page: 15987 year: 2014 end-page: 16005 ident: bib4 article-title: Rational design of broad spectrum antibacterial activity based on a clinically relevant enoyl-acyl carrier protein (ACP) reductase inhibitor publication-title: J. Biol. Chem. – volume: 113 start-page: 807 year: 2020 end-page: 825 ident: bib17 article-title: Fatty acid activation and utilization by Alistipes finegoldii, a representative Bacteroidetes resident of the human gut microbiome publication-title: Mol. Microbiol. – volume: 45 start-page: 10008 year: 2006 end-page: 10019 ident: bib12 article-title: The soluble acyl-acyl carrier protein synthetase of publication-title: Biochemistry – volume: 68 start-page: 1045 year: 1990 end-page: 1051 ident: bib10 article-title: A soluble fatty acyl - acyl carrier protein synthetase from the bioluminescent bacterium publication-title: Biochem. Cell. Biol. – volume: 30 start-page: 241 year: 2022 end-page: 253 ident: bib2 article-title: Bacterial adaptation strategies to host-derived fatty acids publication-title: Trends Microbiol. – volume: 10 year: 2015 ident: bib20 article-title: Global estimates of the prevalence and incidence of four curable sexually transmitted infections in 2012 based on systematic review and global reporting publication-title: PLoS One – volume: 19 start-page: 666 year: 2009 end-page: 671 ident: bib8 article-title: Adenylate-forming enzymes publication-title: Curr. Opin. Struct. Biol. – volume: 6 start-page: 216 year: 2015 end-page: 220 ident: bib26 article-title: Improved synthesis of biotinol-5’-AMP: implications for antibacterial discovery publication-title: ACS Med. Chem. Lett. – volume: 10 start-page: 1871 year: 2000 end-page: 1874 ident: bib14 article-title: Aminoalkyl adenylate and aminoacyl sulfamate intermediate analogues differing greatly in affinity for their cognate Staphylococcus aureus aminoacyl TRNA synthetases publication-title: Bioorg. Med. Chem. Lett. – volume: 290 start-page: 22163 year: 2015 end-page: 22173 ident: bib18 article-title: Chlamydia trachomatis scavenges host fatty acids for phospholipid synthesis via an acyl-acyl carrier protein synthetase publication-title: J. Biol. Chem. – volume: 291 start-page: 171 year: 2016 end-page: 181 ident: bib16 article-title: Activation of exogenous fatty acids to acyl-acyl carrier protein cannot bypass FabI inhibition in publication-title: J. Biol. Chem. – volume: 1080 start-page: 126 year: 1991 end-page: 134 ident: bib13 article-title: X-ray crystallographic conformational study of 5′-O-[N-(L-Alanyl)-Sulfamoyl] adenosine, a substrate analogue for alanyl-TRNA synthetase publication-title: Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. – volume: 20 start-page: 589 year: 2020 ident: bib19 article-title: Prevalence of genital Chlamydia trachomatis infection in the general population: a meta-analysis publication-title: BMC Infect. Dis. – volume: 16 year: 2023 ident: bib5 article-title: A review of fatty acid biosynthesis enzyme inhibitors as promising antimicrobial drugs publication-title: Pharmaceuticals – volume: 105 start-page: 7785 year: 2021 end-page: 7799 ident: bib23 article-title: Escherichia coli nissle 1917 secondary metabolism: aryl polyene biosynthesis and phosphopantetheinyl transferase crosstalk publication-title: Appl. Microbiol. Biotechnol. – volume: 18 start-page: 5963 year: 2008 end-page: 5966 ident: bib15 article-title: Mechanism-based inhibitors of MenE, an acyl-CoA synthetase involved in bacterial menaquinone biosynthesis publication-title: Bioorg. Med. Chem. Lett – volume: 8 start-page: 1589 year: 2013 end-page: 1608 ident: bib3 article-title: Recent advances in inhibitors of bacterial fatty acid synthesis type II (FASII) system enzymes as potential antibacterial agents publication-title: ChemMedChem – volume: 37 start-page: 1585 year: 1998 end-page: 1595 ident: bib25 article-title: Characterization of Sfp, a publication-title: Biochemistry – volume: 458 start-page: 83 year: 2009 end-page: 86 ident: bib6 article-title: Type II fatty acid synthesis is not a suitable antibiotic target for gram-positive pathogens publication-title: Nature – volume: 73 start-page: 4374 year: 1976 end-page: 4378 ident: bib9 article-title: Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl acyl carrier protein synthetase, in publication-title: Proc. Natl. Acad. Sci. U. S. A. – volume: 9 start-page: 671 year: 2012 end-page: 675 ident: bib27 article-title: NIH image to ImageJ: 25 Years of image analysis publication-title: Nat. Methods – volume: 1854 start-page: 1019 year: 2015 end-page: 1037 ident: bib21 article-title: Enzyme function initiative-enzyme similarity tool (EFI-EST): a web tool for generating protein sequence similarity networks publication-title: Biochim. Biophys. Acta – volume: 10 year: 2020 ident: bib7 article-title: Synthesis of an acyl-acyl carrier protein synthetase inhibitor to study fatty acid recycling publication-title: Sci. Rep. – volume: 21 start-page: 1293 year: 2014 end-page: 1299 ident: bib11 article-title: Versatility of acyl-acyl carrier protein synthetases publication-title: Chem. Biol. – volume: 21 start-page: 1293 issue: 10 year: 2014 ident: 10.1016/j.bbrep.2023.101549_bib11 article-title: Versatility of acyl-acyl carrier protein synthetases publication-title: Chem. Biol. doi: 10.1016/j.chembiol.2014.08.015 – volume: 73 start-page: 4374 issue: 12 year: 1976 ident: 10.1016/j.bbrep.2023.101549_bib9 article-title: Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl acyl carrier protein synthetase, in Escherichia coli publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.73.12.4374 – volume: 1080 start-page: 126 year: 1991 ident: 10.1016/j.bbrep.2023.101549_bib13 article-title: X-ray crystallographic conformational study of 5′-O-[N-(L-Alanyl)-Sulfamoyl] adenosine, a substrate analogue for alanyl-TRNA synthetase publication-title: Biochim. Biophys. Acta Protein Struct. Mol. Enzymol. doi: 10.1016/0167-4838(91)90138-P – volume: 105 start-page: 7785 issue: 20 year: 2021 ident: 10.1016/j.bbrep.2023.101549_bib23 article-title: Escherichia coli nissle 1917 secondary metabolism: aryl polyene biosynthesis and phosphopantetheinyl transferase crosstalk publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-021-11546-x – volume: 30 start-page: 241 issue: 3 year: 2022 ident: 10.1016/j.bbrep.2023.101549_bib2 article-title: Bacterial adaptation strategies to host-derived fatty acids publication-title: Trends Microbiol. doi: 10.1016/j.tim.2021.06.002 – volume: 290 start-page: 22163 issue: 36 year: 2015 ident: 10.1016/j.bbrep.2023.101549_bib18 article-title: Chlamydia trachomatis scavenges host fatty acids for phospholipid synthesis via an acyl-acyl carrier protein synthetase publication-title: J. Biol. Chem. doi: 10.1074/jbc.M115.671008 – volume: 16 issue: 3 year: 2023 ident: 10.1016/j.bbrep.2023.101549_bib5 article-title: A review of fatty acid biosynthesis enzyme inhibitors as promising antimicrobial drugs publication-title: Pharmaceuticals doi: 10.3390/ph16030425 – volume: 19 start-page: 666 issue: 6 year: 2009 ident: 10.1016/j.bbrep.2023.101549_bib8 article-title: Adenylate-forming enzymes publication-title: Curr. Opin. Struct. Biol. doi: 10.1016/j.sbi.2009.09.004 – volume: 113 start-page: 807 issue: 4 year: 2020 ident: 10.1016/j.bbrep.2023.101549_bib17 article-title: Fatty acid activation and utilization by Alistipes finegoldii, a representative Bacteroidetes resident of the human gut microbiome publication-title: Mol. Microbiol. doi: 10.1111/mmi.14445 – volume: 266 start-page: 1858 issue: 3 year: 1991 ident: 10.1016/j.bbrep.2023.101549_bib24 article-title: In vivo pools of free and acylated acyl carrier proteins in spinach. Evidence for sites of regulation of fatty acid biosynthesis publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)52372-3 – volume: 12 start-page: 766 issue: 7 year: 2012 ident: 10.1016/j.bbrep.2023.101549_bib30 article-title: Adenylating enzymes in Mycobacterium tuberculosis as drug targets publication-title: Curr. Top. Med. Chem. doi: 10.2174/156802612799984571 – volume: 20 start-page: 589 issue: 1 year: 2020 ident: 10.1016/j.bbrep.2023.101549_bib19 article-title: Prevalence of genital Chlamydia trachomatis infection in the general population: a meta-analysis publication-title: BMC Infect. Dis. doi: 10.1186/s12879-020-05307-w – volume: 6 start-page: 216 issue: 2 year: 2015 ident: 10.1016/j.bbrep.2023.101549_bib26 article-title: Improved synthesis of biotinol-5’-AMP: implications for antibacterial discovery publication-title: ACS Med. Chem. Lett. doi: 10.1021/ml500475n – volume: 10 start-page: 1871 issue: 16 year: 2000 ident: 10.1016/j.bbrep.2023.101549_bib14 article-title: Aminoalkyl adenylate and aminoacyl sulfamate intermediate analogues differing greatly in affinity for their cognate Staphylococcus aureus aminoacyl TRNA synthetases publication-title: Bioorg. Med. Chem. Lett. doi: 10.1016/S0960-894X(00)00360-7 – volume: 18 start-page: 5963 issue: 22 year: 2008 ident: 10.1016/j.bbrep.2023.101549_bib15 article-title: Mechanism-based inhibitors of MenE, an acyl-CoA synthetase involved in bacterial menaquinone biosynthesis publication-title: Bioorg. Med. Chem. Lett doi: 10.1016/j.bmcl.2008.07.130 – volume: 289 start-page: 15987 issue: 23 year: 2014 ident: 10.1016/j.bbrep.2023.101549_bib4 article-title: Rational design of broad spectrum antibacterial activity based on a clinically relevant enoyl-acyl carrier protein (ACP) reductase inhibitor publication-title: J. Biol. Chem. doi: 10.1074/jbc.M113.532804 – volume: 141 start-page: 30 year: 2017 ident: 10.1016/j.bbrep.2023.101549_bib1 article-title: Exogenous fatty acid metabolism in bacteria publication-title: Biochimie doi: 10.1016/j.biochi.2017.06.015 – volume: 25 start-page: 32 issue: 1 year: 2013 ident: 10.1016/j.bbrep.2023.101549_bib28 article-title: Activity of AFN-1252, a novel FabI inhibitor, against Staphylococcus aureus in an in vitro pharmacodynamic model simulating human pharmacokinetics publication-title: J. Chemother. doi: 10.1179/1973947812Y.0000000060 – volume: 291 start-page: 171 issue: 1 year: 2016 ident: 10.1016/j.bbrep.2023.101549_bib16 article-title: Activation of exogenous fatty acids to acyl-acyl carrier protein cannot bypass FabI inhibition in Neisseria publication-title: J. Biol. Chem. doi: 10.1074/jbc.M115.699462 – volume: 1854 start-page: 1019 issue: 8 year: 2015 ident: 10.1016/j.bbrep.2023.101549_bib21 article-title: Enzyme function initiative-enzyme similarity tool (EFI-EST): a web tool for generating protein sequence similarity networks publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbapap.2015.04.015 – volume: 13 start-page: 2498 issue: 11 year: 2003 ident: 10.1016/j.bbrep.2023.101549_bib22 article-title: Cytoscape: a software environment for integrated models of biomolecular interaction networks publication-title: Genome Res. doi: 10.1101/gr.1239303 – volume: 480 start-page: 855 issue: 12 year: 2023 ident: 10.1016/j.bbrep.2023.101549_bib29 article-title: The acyl carrier proteins of lipid synthesis are busy having other affairs publication-title: Biochem. J. doi: 10.1042/BCJ20230161 – volume: 10 issue: 1 year: 2020 ident: 10.1016/j.bbrep.2023.101549_bib7 article-title: Synthesis of an acyl-acyl carrier protein synthetase inhibitor to study fatty acid recycling publication-title: Sci. Rep. doi: 10.1038/s41598-020-74731-4 – volume: 8 start-page: 1589 issue: 10 year: 2013 ident: 10.1016/j.bbrep.2023.101549_bib3 article-title: Recent advances in inhibitors of bacterial fatty acid synthesis type II (FASII) system enzymes as potential antibacterial agents publication-title: ChemMedChem doi: 10.1002/cmdc.201300209 – volume: 37 start-page: 1585 issue: 6 year: 1998 ident: 10.1016/j.bbrep.2023.101549_bib25 article-title: Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carder protein domains in peptide synthetases publication-title: Biochemistry doi: 10.1021/bi9719861 – volume: 45 start-page: 10008 issue: 33 year: 2006 ident: 10.1016/j.bbrep.2023.101549_bib12 article-title: The soluble acyl-acyl carrier protein synthetase of Vibrio harveyi B392 is a member of the medium chain acyl-CoA synthetase family publication-title: Biochemistry doi: 10.1021/bi060842w – volume: 10 issue: 12 year: 2015 ident: 10.1016/j.bbrep.2023.101549_bib20 article-title: Global estimates of the prevalence and incidence of four curable sexually transmitted infections in 2012 based on systematic review and global reporting publication-title: PLoS One doi: 10.1371/journal.pone.0143304 – volume: 9 start-page: 671 issue: 7 year: 2012 ident: 10.1016/j.bbrep.2023.101549_bib27 article-title: NIH image to ImageJ: 25 Years of image analysis publication-title: Nat. Methods doi: 10.1038/nmeth.2089 – volume: 458 start-page: 83 issue: 7234 year: 2009 ident: 10.1016/j.bbrep.2023.101549_bib6 article-title: Type II fatty acid synthesis is not a suitable antibiotic target for gram-positive pathogens publication-title: Nature doi: 10.1038/nature07772 – volume: 68 start-page: 1045 issue: 7–8 year: 1990 ident: 10.1016/j.bbrep.2023.101549_bib10 article-title: A soluble fatty acyl - acyl carrier protein synthetase from the bioluminescent bacterium Vibrio harveyi publication-title: Biochem. Cell. Biol. doi: 10.1139/o90-154 |
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| Title | A broad inhibitor of acyl-acyl carrier protein synthetases |
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