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Volumn 439, Issue 1, 2013, Pages 37-43

Continuous fluorescence anisotropy-based assay of BOCILLIN FL penicillin reaction with penicillin binding protein 3

Author keywords

BOCILLINFL; Fluorescence anisotropy; Lactamase; Penicillin binding protein

Indexed keywords

ACYLATION; ANISOTROPY; FLUORESCENCE; PROTEINS;

EID: 84885116586     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.04.009     Document Type: Article
Times cited : (28)

References (30)
  • 1
    • 39149088656 scopus 로고    scopus 로고
    • The penicillin-binding proteins: Structure and role in peptidoglycan biosynthesis
    • DOI 10.1111/j.1574-6976.2008.00105.x
    • E. Sauvage, F. Kerff, M. Terrak, J.A. Ayala, P. Charlier, The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis, FEMS Microbiol. Rev. 32 (2008) 234-258. (Pubitemid 351257821)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.2 , pp. 234-258
    • Sauvage, E.1    Kerff, F.2    Terrak, M.3    Ayala, J.A.4    Charlier, P.5
  • 2
    • 33746891446 scopus 로고    scopus 로고
    • Penicillin binding proteins: Key players in bacterial cell cycle and drug resistance processes
    • DOI 10.1111/j.1574-6976.2006.00024.x
    • P. Macheboeuf, C. Contreras-Martel, V. Job, O. Dideberg, A. Dessen, Penicillin binding proteins: key players in bacterial cell cycle and drug resistance processes, FEMS Microbiol. Rev. 30 (2006) 673-691. (Pubitemid 44199345)
    • (2006) FEMS Microbiology Reviews , vol.30 , Issue.5 , pp. 673-691
    • Macheboeuf, P.1    Contreras-Martel, C.2    Job, V.3    Dideberg, O.4    Dessen, A.5
  • 3
    • 0017327167 scopus 로고
    • Properties of the penicillin binding proteins of Escherichia coli K12
    • DOI 10.1111/j.1432-1033.1977.tb11258.x
    • B.G. Spratt, Properties of the penicillin-binding proteins of Escherichia coli K- 12, Eur. J. Biochem. 72 (1977) 341-352. (Pubitemid 8022233)
    • (1977) European Journal of Biochemistry , vol.72 , Issue.2 , pp. 341-352
    • Spratt, B.G.1
  • 4
    • 0029956443 scopus 로고    scopus 로고
    • Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli
    • T.J. Dougherty, K. Kennedy, R.E. Kessler, M.J. Pucci, Direct quantitation of the number of individual penicillin-binding proteins per cell in Escherichia coli, J. Bacteriol. 178 (1996) 6110-6115. (Pubitemid 26365687)
    • (1996) Journal of Bacteriology , vol.178 , Issue.21 , pp. 6110-6115
    • Dougherty, T.J.1    Kennedy, K.2    Kessler, R.E.3    Pucci, M.J.4
  • 5
    • 0029025744 scopus 로고
    • Kinetic properties of the bacillus licheniformis penicillin-binding protein
    • S. Lepage, M. Galleni, B. Lakaye, B. Joris, I. Thamm, J.-M. Frère, Kinetic properties of the Bacillus licheniformis penicillin-binding protein, Biochem. J. 309 (1995) 49-53.
    • (1995) Biochem. J. , vol.309 , pp. 49-53
    • Lepage, S.1    Galleni, M.2    Lakaye, B.3    Joris, B.4    Thamm, I.5    Frère, J.-M.6
  • 6
    • 0028231058 scopus 로고
    • Use of biotinylated lactams and chemiluminescence for study and purification of penicillin-binding proteins in bacteria
    • M. Dargis, F. Malouin, Use of biotinylated b-lactams and chemiluminescence for study and purification of penicillin binding proteins in bacteria, Antimicrob. Agents Chemother. 38 (1994) 973-980. (Pubitemid 24150824)
    • (1994) Antimicrobial Agents and Chemotherapy , vol.38 , Issue.5 , pp. 973-980
    • Dargis, M.1    Malouin, F.2
  • 7
    • 0032908481 scopus 로고    scopus 로고
    • BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins
    • G. Zhao, T.I. Meier, S.D. Kahl, K.R. Gee, L.C. Blaszczak, BOCILLIN FL, a sensitive and commercially available reagent for detection of penicillin-binding proteins, Antimicrob. Agents Chemother. 43 (1999) 1124-1128. (Pubitemid 29214735)
    • (1999) Antimicrobial Agents and Chemotherapy , vol.43 , Issue.5 , pp. 1124-1128
    • Zhao, G.1    Meier, T.I.2    Kahl, S.D.3    Gee, K.R.4    Blaszczak, L.C.5
  • 8
    • 0035044203 scopus 로고    scopus 로고
    • Fluorescent Bocillins: Synthesis and application in the detection of penicillin-binding proteins
    • DOI 10.1002/1522-2683()22:5<960::AID-ELPS9603.0.CO;2-9
    • K.R. Gee, H.C. Kang, T.I. Meier, G. Zhao, L.C. Blaszcak, Fluorescent BOCILLINs: synthesis and application in the detection of penicillin-binding proteins, Electrophoresis 22 (2001) 960-965. (Pubitemid 32318417)
    • (2001) Electrophoresis , vol.22 , Issue.5 , pp. 960-965
    • Gee, K.R.1    Kang, H.C.2    Meier, T.I.3    Zhao, G.4    Blaszcak, L.C.5
  • 10
    • 0031974583 scopus 로고
    • Soluble penicillin-binding protein 2a: B-lactam binding and inhibition by non- b-lactams using a 96-well format
    • J.H. Toney, G.G. Hammond, B. Leiting, K.D. Pryor, J.K. Wu, G.C. Cuca, D.L. Pompliano, Soluble penicillin-binding protein 2a: b-lactam binding and inhibition by non- b-lactams using a 96-well format, Anal. Biochem. 255 (1988) 113-119.
    • (1988) Anal. Biochem. , vol.255 , pp. 113-119
    • Toney, J.H.1    Hammond, G.G.2    Leiting, B.3    Pryor, K.D.4    Wu, J.K.5    Cuca, G.C.6    Pompliano, D.L.7
  • 11
    • 70449627031 scopus 로고    scopus 로고
    • A microtiter plate-based b-lactam binding assay for inhibitors of high-molecular-mass penicillin-binding proteins
    • M. Stefanova, S. Bobba, W.G. Gutheil, A microtiter plate-based b-lactam binding assay for inhibitors of high-molecular-mass penicillin-binding proteins, Anal. Biochem. 396 (2010) 164-166.
    • (2010) Anal. Biochem. , vol.396 , pp. 164-166
    • Stefanova, M.1    Bobba, S.2    Gutheil, W.G.3
  • 12
    • 79956298875 scopus 로고    scopus 로고
    • Microtiter plate-based assay for inhibitors of penicillin-binding protein 2a from methicillin-resistant staphylococcus aureus
    • S. Bobba, V.K.C. Ponnaluri, M. Mukherji, W.G. Gutheil, Microtiter plate-based assay for inhibitors of penicillin-binding protein 2a from methicillin-resistant Staphylococcus aureus, Antimicrob. Agents Chemother. 55 (2011) 2783-2787.
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 2783-2787
    • Bobba, S.1    Ponnaluri, V.K.C.2    Mukherji, M.3    Gutheil, W.G.4
  • 14
    • 85031081507 scopus 로고    scopus 로고
    • Kinetics of b-lactamases in theory and practice
    • J.-M. Frère (Ed.), Nova Science, Hauppauge, NY
    • J.-M. Frère, Kinetics of b-lactamases in theory and practice, in: J.-M. Frère (Ed.), b-Lactamases, Nova Science, Hauppauge, NY, 2012.
    • (2012) B-Lactamases
    • Frère, J.-M.1
  • 15
    • 0016753853 scopus 로고
    • Kinetics of interaction between the exocellular dd-carboxypeptidase- transpeptidase from streptomyces r61 and b-lactam antibiotics
    • J.-M. Frère, J.-M. Ghuysen, M. Iwatsubo, Kinetics of interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and b-lactam antibiotics, Eur. J. Biochem. 57 (1975) 343-351.
    • (1975) Eur. J. Biochem. , vol.57 , pp. 343-351
    • Frère, J.-M.1    Ghuysen, J.-M.2    Iwatsubo, M.3
  • 18
    • 84859588905 scopus 로고    scopus 로고
    • Sitesaturation mutagenesis of position v117 in oxa-1 b-lactamase: Effect of side chain polarity on enzyme carboxylation and substrate turnover
    • J.S. Buchman, K.D. Schneider, A.R. Lloyd, S.L. Pavlish, D.A. Leonard, Sitesaturation mutagenesis of position V117 in OXA-1 b-lactamase: effect of side chain polarity on enzyme carboxylation and substrate turnover, Biochemistry 51 (2012) 3143-3150.
    • (2012) Biochemistry , vol.51 , pp. 3143-3150
    • Buchman, J.S.1    Schneider, K.D.2    Lloyd, A.R.3    Pavlish, S.L.4    Leonard, D.A.5
  • 19
    • 71549171706 scopus 로고    scopus 로고
    • Fitting enzyme kinetic data with kintek global kinetic explorer
    • K.A. Johnson, Fitting enzyme kinetic data with KinTek Global Kinetic Explorer, Methods Enzymol. 467 (2009) 601-626.
    • (2009) Methods Enzymol , vol.467 , pp. 601-626
    • Johnson, K.A.1
  • 20
    • 0032880709 scopus 로고    scopus 로고
    • Homogeneous fluorescence readouts for miniaturized high-throughput screening: Theory and practice
    • DOI 10.1016/S1359-6446(99)01340-9, PII S1359644699013409
    • A.J. Pope, U.M. Haupts, K.J. Moore, Homogeneous fluorescence readouts for miniaturized high-throughput screening: theory and practice, Drug Discov. Technol. 4 (1999) 350-362. (Pubitemid 29457485)
    • (1999) Drug Discovery Today , vol.4 , Issue.8 , pp. 350-362
    • Pope, A.J.1    Haupts, U.M.2    Moore, K.J.3
  • 22
    • 77952538407 scopus 로고    scopus 로고
    • Fluorescence polarization/anisotropy in diagnostics and imaging
    • D.M. Jameson, J.A. Ross, Fluorescence polarization/anisotropy in diagnostics and imaging, Chem. Rev. 110 (2010) 2685-2708.
    • (2010) Chem. Rev. , vol.110 , pp. 2685-2708
    • Jameson, D.M.1    Ross, J.A.2
  • 23
    • 0030921172 scopus 로고    scopus 로고
    • The bimodular G57-V577 polypeptide chain of the class B penicillin- binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate
    • M. Adam, C. Fraipont, N. Rhazi, M. Nguyen-Distèche, B. Lakaye, J.-M. Frère, B. Devreese, J. van Beeumen, Y. vanHeijenoort, J. vanHeijenoort, J.M. Ghuysen, The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate, J. Bacteriol. 179 (1997) 6005-6009. (Pubitemid 27419021)
    • (1997) Journal of Bacteriology , vol.179 , Issue.19 , pp. 6005-6009
    • Adam, M.1    Fraipont, C.2    Rhazi, N.3    Nguyen-Disteche, M.4    Lakaye, B.5    Frere, J.-M.6    Devreese, B.7    Van Beeumen, J.8    Van Heijenoort, Y.9    Van Heijenoort, J.10    Ghuysen, J.-M.11
  • 25
    • 67650095721 scopus 로고    scopus 로고
    • Mutation of the active site lysine (k70) of oxa-1 b-lactamase results in a deacylation-deficient enzyme
    • K.D. Schneider, C.R. Bethel, A.M. Distler, A.M. Hujer, R.A. Bonomo, D.A. Leonard, Mutation of the active site lysine (K70) of OXA-1 b-lactamase results in a deacylation-deficient enzyme, Biochemistry 48 (2009) 6136-6145.
    • (2009) Biochemistry , vol.48 , pp. 6136-6145
    • Schneider, K.D.1    Bethel, C.R.2    Distler, A.M.3    Hujer, A.M.4    Bonomo, R.A.5    Leonard, D.A.6
  • 26
    • 70349642091 scopus 로고    scopus 로고
    • Mechanismbased inhibition: Deriving ki and kinact directly from time-dependent ic50 values
    • B.-F. Krippendorff, R. Neuhaus, P. Lienau, A. Reichel, W. Huisinga, Mechanismbased inhibition: deriving Ki and kinact directly from time-dependent IC50 values, J. Biomol. Screen. 14 (2009) 913-923.
    • (2009) J. Biomol. Screen. , vol.14 , pp. 913-923
    • Krippendorff, B.-F.1    Neuhaus, R.2    Lienau, P.3    Reichel, A.4    Huisinga, W.5
  • 27
    • 0024996497 scopus 로고
    • Chromogenic depsipeptide substrates for - Lactamases and penicillin-sensitive DD-peptidases
    • M. Adam, C. Damblon, B. Plaitin, L. Chistiaens, J.-M. Frere, Chromogenic depsipeptide substrates for b-lactamases and penicillin-sensitive DDpeptidases, Biochem. J. 270 (1990) 525-529. (Pubitemid 20273499)
    • (1990) Biochemical Journal , vol.270 , Issue.2 , pp. 525-529
    • Adam, M.1    Damblon, C.2    Plaitin, B.3    Christiaens, L.4    Frere, J.-M.5
  • 28
    • 33845958152 scopus 로고    scopus 로고
    • Reactivity of penicillin-binding proteins with peptidoglycan-mimetic lactams: What's wrong with these enzymes
    • DOI 10.1021/bi061804f
    • H.R. Josephine, P. Charlier, C. Davies, R.A. Nicholas, R.F. Pratt, Reactivity of penicillin-binding proteins with peptidoglycan-mimetic b-lactams: what's wrong with these enzymes?, Biochemistry 45 (2006) 15873-15883. (Pubitemid 46032508)
    • (2006) Biochemistry , vol.45 , Issue.51 , pp. 15873-15883
    • Josephine, H.R.1    Charlier, P.2    Davies, C.3    Nicholas, R.A.4    Pratt, R.F.5
  • 29
    • 34447254695 scopus 로고    scopus 로고
    • Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae
    • DOI 10.1128/AAC.00029-07
    • T.A. Davies, M.G.P. Page, W. Shang, T. Andrew, M. Kania, K. Bush, Binding of ceftobiprole and comparators to the penicillin-binding proteins of Escherichia coli, Pseudomonas aeruginosa, Staphylococcus aureus, and Streptococcus pneumoniae, Antimicrob. Agents Chemother. 51 (2007) 2621-2624. (Pubitemid 47047351)
    • (2007) Antimicrobial Agents and Chemotherapy , vol.51 , Issue.7 , pp. 2621-2624
    • Davies, T.A.1    Page, M.G.P.2    Shang, W.3    Andrew, T.4    Kania, M.5    Bush, K.6
  • 30
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (ki) and the concentration of inhibitor which causes 50 per cent inhibition (i50) of an enzymatic reaction
    • Y. Cheng, W.H. Prusoff, Relationship between the inhibition constant (KI) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction, Biochem. Pharmacol. 22 (1973) 3099-3108.
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2


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