메뉴 건너뛰기




Volumn 1780, Issue 5, 2008, Pages 848-853

Examination of intrinsic sulfonamide resistance in Bacillus anthracis: A novel assay for dihydropteroate synthase

Author keywords

6 Hydroxymethyl 7,8 dihydropterin diphosphate; Coupled spectrophotometric assay; Dihydropteroate; Dihydropteroate synthase; para Aminobenzoic acid; Sulfonamide

Indexed keywords

4 AMINOBENZOIC ACID; 6 HYDROXYMETHYL 7,8 DIHYDROPTERIN DIPHOSPHATE; 6 PHOSPHOFRUCTOKINASE; DAPSONE; DIHYDROPTEROATE SYNTHASE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; MAGNESIUM; PTERIN DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SULFADIAZINE; SULFAFURAZOLE; SULFAMETHIZOLE; SULFAMETHOXAZOLE; SULFATHIAZOLE; SULFONAMIDE; TRIOSE;

EID: 45049086683     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2008.02.003     Document Type: Article
Times cited : (25)

References (23)
  • 1
    • 0027737508 scopus 로고
    • Molecular aspects and mechanism of action of dihydrofolate reductase inhibitors
    • Hartman P.G. Molecular aspects and mechanism of action of dihydrofolate reductase inhibitors. J. Chemother. 5 (1993) 369-376
    • (1993) J. Chemother. , vol.5 , pp. 369-376
    • Hartman, P.G.1
  • 2
    • 0033674845 scopus 로고    scopus 로고
    • Mechanism of the antimicrobial drug trimethoprim revisited
    • Quinlivan E.P., McPartlin J., Weir D.G., and Scott J. Mechanism of the antimicrobial drug trimethoprim revisited. FASEB J. 14 (2000) 2519-2524
    • (2000) FASEB J. , vol.14 , pp. 2519-2524
    • Quinlivan, E.P.1    McPartlin, J.2    Weir, D.G.3    Scott, J.4
  • 3
    • 0033853659 scopus 로고    scopus 로고
    • Sulfonamide resistance: mechanisms and trends
    • Skold O. Sulfonamide resistance: mechanisms and trends. Drug Resist. Updat. 3 (2000) 155-160
    • (2000) Drug Resist. Updat. , vol.3 , pp. 155-160
    • Skold, O.1
  • 4
    • 0000478463 scopus 로고
    • The biosynthesis of folic acid. II. Inhibition by sulfonamides
    • Brown G.M. The biosynthesis of folic acid. II. Inhibition by sulfonamides. J. Biol. Chem. 237 (1962) 536-540
    • (1962) J. Biol. Chem. , vol.237 , pp. 536-540
    • Brown, G.M.1
  • 5
    • 0018567923 scopus 로고
    • The characteristics and significance of sulfonamides as substrates for Escherichia coli dihydropteroate synthase
    • Roland S., Ferone R., Harvey R.J., Styles V.L., and Morrison R.W. The characteristics and significance of sulfonamides as substrates for Escherichia coli dihydropteroate synthase. J. Biol. Chem 254 (1979) 10337-10345
    • (1979) J. Biol. Chem , vol.254 , pp. 10337-10345
    • Roland, S.1    Ferone, R.2    Harvey, R.J.3    Styles, V.L.4    Morrison, R.W.5
  • 6
    • 0018341925 scopus 로고
    • Characterization of mutationally altered dihydropteroate synthase and its ability to form a sulfonamide-containing dihydrofolate analog
    • Swedberg G., Castensson S., and Skold O. Characterization of mutationally altered dihydropteroate synthase and its ability to form a sulfonamide-containing dihydrofolate analog. J. Bacteriol. 137 (1979) 129-136
    • (1979) J. Bacteriol. , vol.137 , pp. 129-136
    • Swedberg, G.1    Castensson, S.2    Skold, O.3
  • 7
    • 0002009389 scopus 로고
    • The relation of p-aminobenzoic acid to the mechanism of action of sulphanilamide
    • Woods D.D. The relation of p-aminobenzoic acid to the mechanism of action of sulphanilamide. Br. J. Exp. Pathol. 21 (1940) 74-90
    • (1940) Br. J. Exp. Pathol. , vol.21 , pp. 74-90
    • Woods, D.D.1
  • 8
    • 9644254239 scopus 로고    scopus 로고
    • Functional cloning of Bacillus anthracis DHFR and confirmation of natural resistance to trimethoprim
    • Barrow E.W., Bourne P.C., and Barrow W.W. Functional cloning of Bacillus anthracis DHFR and confirmation of natural resistance to trimethoprim. Antimicrob. Agents Chemother. 48 (2004) 4643-4649
    • (2004) Antimicrob. Agents Chemother. , vol.48 , pp. 4643-4649
    • Barrow, E.W.1    Bourne, P.C.2    Barrow, W.W.3
  • 9
    • 34250223080 scopus 로고    scopus 로고
    • Cloning and molecular characterization of three arylamine N-acetyltransferase genes from Bacillus anthracis: identification of unusual enzymatic properties and their contribution to sulfamethoxazole resistance
    • Pluvinage B., Dairou J., Possot O.M., Martins M., Fouet A., Dupret J.-M., and Rodrigues-Lima F. Cloning and molecular characterization of three arylamine N-acetyltransferase genes from Bacillus anthracis: identification of unusual enzymatic properties and their contribution to sulfamethoxazole resistance. Biochemistry 46 (2007) 7069-7078
    • (2007) Biochemistry , vol.46 , pp. 7069-7078
    • Pluvinage, B.1    Dairou, J.2    Possot, O.M.3    Martins, M.4    Fouet, A.5    Dupret, J.-M.6    Rodrigues-Lima, F.7
  • 10
    • 34249751709 scopus 로고    scopus 로고
    • Genetic basis for sulfonamide resistance in Bacillus anthracis
    • Valderas M.W., and Barrow W.W. Genetic basis for sulfonamide resistance in Bacillus anthracis. Microb. Drug Resist. 13 (2007) 11-20
    • (2007) Microb. Drug Resist. , vol.13 , pp. 11-20
    • Valderas, M.W.1    Barrow, W.W.2
  • 11
    • 0018812881 scopus 로고
    • 7,8-Dihydropteroate-synthesizing enzyme from Plasmodium chabaudi
    • Walter R.D., and Konigk E. 7,8-Dihydropteroate-synthesizing enzyme from Plasmodium chabaudi. Methods enzymol. 66 (1980) 564-570
    • (1980) Methods enzymol. , vol.66 , pp. 564-570
    • Walter, R.D.1    Konigk, E.2
  • 12
    • 0036605892 scopus 로고    scopus 로고
    • The molecular basis of sulfonamide resistance in Toxoplasma gondii and implications for the clinical management of toxoplasmosis
    • Aspinall T.V., Joynson D.H., Guy E., Hyde J.E., and Sims P.F. The molecular basis of sulfonamide resistance in Toxoplasma gondii and implications for the clinical management of toxoplasmosis. J. Infect. Dis. 185 (2002) 1637-1643
    • (2002) J. Infect. Dis. , vol.185 , pp. 1637-1643
    • Aspinall, T.V.1    Joynson, D.H.2    Guy, E.3    Hyde, J.E.4    Sims, P.F.5
  • 13
    • 0021772471 scopus 로고
    • Kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii
    • Bertagnolli B.L., and Cook P.F. Kinetic mechanism of pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii. Biochemistry 23 (1984) 4101-4108
    • (1984) Biochemistry , vol.23 , pp. 4101-4108
    • Bertagnolli, B.L.1    Cook, P.F.2
  • 14
    • 0025774861 scopus 로고
    • Existence of two d-alanine:d-alanine ligases in Escherichia coli: cloning and sequencing of the ddlA gene and purification and characterization of the Ddl and DdlB enzymes
    • Zawadzke L.E., Timothy D.H., and Walsh C.T. Existence of two d-alanine:d-alanine ligases in Escherichia coli: cloning and sequencing of the ddlA gene and purification and characterization of the Ddl and DdlB enzymes. Biochemistry 30 (1991) 1673-1682
    • (1991) Biochemistry , vol.30 , pp. 1673-1682
    • Zawadzke, L.E.1    Timothy, D.H.2    Walsh, C.T.3
  • 15
    • 0026132864 scopus 로고
    • The antibiotic sensitivity patterns of Bacillus anthracis isolated from the Kruger National Park
    • Odendaal M.S., Pieterson P.M., deMos V., and Botha A.D. The antibiotic sensitivity patterns of Bacillus anthracis isolated from the Kruger National Park. Onderstepoort J. Vet. Res. 58 (1991) 17-19
    • (1991) Onderstepoort J. Vet. Res. , vol.58 , pp. 17-19
    • Odendaal, M.S.1    Pieterson, P.M.2    deMos, V.3    Botha, A.D.4
  • 17
    • 0005958575 scopus 로고    scopus 로고
    • Enzyme data and metabolic information: BRENDA, a resource for research in biology, biochemistry, and medicine
    • Schomburg I., Hofmann O., Bänsch C., Chang A., and Schomburg D. Enzyme data and metabolic information: BRENDA, a resource for research in biology, biochemistry, and medicine. Gene Funct. Dis. 3-4 (2000) 109-118
    • (2000) Gene Funct. Dis. , vol.3-4 , pp. 109-118
    • Schomburg, I.1    Hofmann, O.2    Bänsch, C.3    Chang, A.4    Schomburg, D.5
  • 18
    • 4444229009 scopus 로고    scopus 로고
    • Crystal structure of 7,8-dihydropteroate synthase from Bacillus anthracis; mechanism and novel inhibitor design
    • Babaoglu K., Qi J., Lee R.E., and White S.W. Crystal structure of 7,8-dihydropteroate synthase from Bacillus anthracis; mechanism and novel inhibitor design. Structure (Camb) 12 (2004) 1705-1717
    • (2004) Structure (Camb) , vol.12 , pp. 1705-1717
    • Babaoglu, K.1    Qi, J.2    Lee, R.E.3    White, S.W.4
  • 20
    • 0022406073 scopus 로고
    • Monocyclic pteridine analogues. Inhibition of Escherichia coli dihydropteroate synthase by 6-amino-5-nitrosoisocytosines
    • Lever Jr. O.W., Bell L.N., McGuire H.M., and Ferone R. Monocyclic pteridine analogues. Inhibition of Escherichia coli dihydropteroate synthase by 6-amino-5-nitrosoisocytosines. J. Med. Chem. 28 (1985) 1870-1874
    • (1985) J. Med. Chem. , vol.28 , pp. 1870-1874
    • Lever Jr., O.W.1    Bell, L.N.2    McGuire, H.M.3    Ferone, R.4
  • 21
    • 45049083504 scopus 로고    scopus 로고
    • T. Stachyra, J. Biton, In international publication number WO 03/012132 A2 (Aventis, Pharma, Antony, France; 2003).
    • T. Stachyra, J. Biton, In international publication number WO 03/012132 A2 (Aventis, Pharma, Antony, France; 2003).
  • 22
    • 33845672238 scopus 로고    scopus 로고
    • A rapid assay for dihydropteroate synthase activity suitable for identification of inhibitors
    • Fernley R.T., Iliades P., and Macreadie I. A rapid assay for dihydropteroate synthase activity suitable for identification of inhibitors. Anal. Biochem. 360 (2007) 227-234
    • (2007) Anal. Biochem. , vol.360 , pp. 227-234
    • Fernley, R.T.1    Iliades, P.2    Macreadie, I.3
  • 23
    • 34548480436 scopus 로고    scopus 로고
    • Crystal structure of the anthrax drug target, Bacillus anthracis dihydrofolate reductase
    • Bennett B.C., Xu H., Simmerman R.F., Lee R.E., and Dealwis C.G. Crystal structure of the anthrax drug target, Bacillus anthracis dihydrofolate reductase. J. Med. Chem. 50 (2007) 4374-4381
    • (2007) J. Med. Chem. , vol.50 , pp. 4374-4381
    • Bennett, B.C.1    Xu, H.2    Simmerman, R.F.3    Lee, R.E.4    Dealwis, C.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.