메뉴 건너뛰기




Volumn 43, Issue 7, 1999, Pages 1743-1746

Class C β-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin substrates

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE; CEFALORIDINE; CEFEPIME; CEPHALOSPORIN C; CEPHALOSPORIN DERIVATIVE; MACROGOL 8000; PENICILLIN G; SUCROSE;

EID: 0032803407     PISSN: 00664804     EISSN: None     Source Type: Journal    
DOI: 10.1128/aac.43.7.1743     Document Type: Article
Times cited : (35)

References (40)
  • 1
    • 0017058392 scopus 로고
    • Evolution of enzyme function and the development of catalytic efficiency
    • Albery, W. J., and J. R. Knowles. 1976. Evolution of enzyme function and the development of catalytic efficiency. Biochemistry 15:5631-5540.
    • (1976) Biochemistry , vol.15 , pp. 5631-15540
    • Albery, W.J.1    Knowles, J.R.2
  • 2
    • 0022493194 scopus 로고
    • Fractional diffusion-limited component of reactions catalyzed by acetylcholiesterase
    • Bazelyansky, M., E. Robey, and J. F. Kirsch. 1986. Fractional diffusion-limited component of reactions catalyzed by acetylcholiesterase. Biochemistry 25:125-130.
    • (1986) Biochemistry , vol.25 , pp. 125-130
    • Bazelyansky, M.1    Robey, E.2    Kirsch, J.F.3
  • 3
    • 0344487552 scopus 로고
    • Diffusion measurements in aqueous solutions of different viscosity
    • Biancheria, A., and G. J. Kegeles. 1957. Diffusion measurements in aqueous solutions of different viscosity. J. Am. Chem. Soc. 79:5908-5912.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 5908-5912
    • Biancheria, A.1    Kegeles, G.J.2
  • 4
    • 0026766628 scopus 로고
    • Coordinate regulation of murein peptidase activity and AmpC β-lactamase synthesis in Escherichia coli
    • Bishop, R. E., and J. H. Wiener. 1992. Coordinate regulation of murein peptidase activity and AmpC β-lactamase synthesis in Escherichia coli. FEBS Lett. 304:103-108.
    • (1992) FEBS Lett. , vol.304 , pp. 103-108
    • Bishop, R.E.1    Wiener, J.H.2
  • 6
    • 0020484823 scopus 로고
    • Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation
    • Brouwer, A. C., and J. F. Kirsch. 1982. Investigation of diffusion-limited rates of chymotrypsin reactions by viscosity variation. Biochemistry 21:1302-1307.
    • (1982) Biochemistry , vol.21 , pp. 1302-1307
    • Brouwer, A.C.1    Kirsch, J.F.2
  • 7
    • 0029071785 scopus 로고
    • A functional classification scheme for β-lactamases and its correlation with molecular structure
    • Bush, K., G. A. Jacoby, and A. A. Medeiros. 1995. A functional classification scheme for β-lactamases and its correlation with molecular structure. Antimicrob. Agents Chemother. 39:1211-1233.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1211-1233
    • Bush, K.1    Jacoby, G.A.2    Medeiros, A.A.3
  • 8
    • 0032226545 scopus 로고    scopus 로고
    • How β-lactamases have driven pharmaceutical discovery: From mechanistic knowledge to classical circumvention
    • B. P. Rosen and S. Mobashery (ed.), Plenum Press, New York, N.Y.
    • Bush, K., and S. Mobashery. 1998. How β-lactamases have driven pharmaceutical discovery: from mechanistic knowledge to classical circumvention, p. 71-98. In B. P. Rosen and S. Mobashery (ed.), Resolving the antibiotic paradox: progress in understanding drug resistance and development of new antibiotics. Plenum Press, New York, N.Y.
    • (1998) Resolving the Antibiotic Paradox: Progress in Understanding Drug Resistance and Development of New Antibiotics , pp. 71-98
    • Bush, K.1    Mobashery, S.2
  • 9
    • 0021763813 scopus 로고
    • Purification of β-lactamases by affinity chromatography on phenylboronic acid-agarose
    • Cartwright, S. J., and S. G. Waley. 1984. Purification of β-lactamases by affinity chromatography on phenylboronic acid-agarose. Biochem. J. 221: 505-512.
    • (1984) Biochem. J. , vol.221 , pp. 505-512
    • Cartwright, S.J.1    Waley, S.G.2
  • 10
    • 0025270942 scopus 로고
    • Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism
    • Christensen, H., M. T. Martin, and S. G. Waley. 1990. Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism. Biochem. J. 246:853-861.
    • (1990) Biochem. J. , vol.246 , pp. 853-861
    • Christensen, H.1    Martin, M.T.2    Waley, S.G.3
  • 11
    • 0015516331 scopus 로고
    • Effect of glycerol on some kinetic parameters of phosphorylase b
    • Damjanovich, S., J. Bot, B. Somogyi, and J. Sumegi. 1972. Effect of glycerol on some kinetic parameters of phosphorylase b. Biochim. Biophys. Acta 284:345-348.
    • (1972) Biochim. Biophys. Acta , vol.284 , pp. 345-348
    • Damjanovich, S.1    Bot, J.2    Somogyi, B.3    Sumegi, J.4
  • 12
    • 0028944605 scopus 로고
    • Steady-state kinetics of the binding of β-lactams and penicilloates to the second binding site of the Enterobacter cloacae P99 β-lactamase
    • Dryjanski, M., and R. F. Pratt. 1995. Steady-state kinetics of the binding of β-lactams and penicilloates to the second binding site of the Enterobacter cloacae P99 β-lactamase. Biochemistry 34:3561-3568.
    • (1995) Biochemistry , vol.34 , pp. 3561-3568
    • Dryjanski, M.1    Pratt, R.F.2
  • 13
    • 0029817551 scopus 로고    scopus 로고
    • The roles of residues Tyr150, Glu272, and His314 in class C beta-lactamases
    • Dubus, A., P. Ledent, J. Lamotte-Brasseur, and J.-M. Frère. 1996. The roles of residues Tyr150, Glu272, and His314 in class C beta-lactamases. Proteins 25:473-485.
    • (1996) Proteins , vol.25 , pp. 473-485
    • Dubus, A.1    Ledent, P.2    Lamotte-Brasseur, J.3    Frère, J.-M.4
  • 14
    • 0017670157 scopus 로고
    • Effect of mixed solvents on the formation of horseradish peroxidase compound I. the importance of diffusion-controlled reactions
    • Dunford, B. H., and W. D. Hewson. 1977. Effect of mixed solvents on the formation of horseradish peroxidase compound I. The importance of diffusion-controlled reactions. Biochemistry 16:2949-2957.
    • (1977) Biochemistry , vol.16 , pp. 2949-2957
    • Dunford, B.H.1    Hewson, W.D.2
  • 15
    • 0023278709 scopus 로고
    • Kinetics and mechanism of the serine β-lactamase catalyzed hydrolysis of depsipeptides
    • Govardhan, C. P., and R. F. Pratt. 1987. Kinetics and mechanism of the serine β-lactamase catalyzed hydrolysis of depsipeptides. Biochemistry 26: 3385-3395.
    • (1987) Biochemistry , vol.26 , pp. 3385-3395
    • Govardhan, C.P.1    Pratt, R.F.2
  • 16
    • 0021403736 scopus 로고
    • Diffusion-limited component of reactions catalyzed by Bacillus cereus β-lactamase I
    • Hardy, L. W., and J. F. Kirsch. 1984. Diffusion-limited component of reactions catalyzed by Bacillus cereus β-lactamase I. Biochemistry 23:1275-1282.
    • (1984) Biochemistry , vol.23 , pp. 1275-1282
    • Hardy, L.W.1    Kirsch, J.F.2
  • 17
    • 0021484926 scopus 로고
    • Kinetics of carbonic anhydrase catalysis in solvents of increased viscosity: A partially diffusion-controlled reaction
    • Hasinoff, B. B. 1984. Kinetics of carbonic anhydrase catalysis in solvents of increased viscosity: a partially diffusion-controlled reaction. Arch. Biochem. Biophys. 233:676-681.
    • (1984) Arch. Biochem. Biophys. , vol.233 , pp. 676-681
    • Hasinoff, B.B.1
  • 18
    • 0020400743 scopus 로고
    • Viscosity dependence of the kinetics of the diffusion-controlled reaction of carbon monoxide and myoglobin
    • Hasinoff, B. B., and S. B. Chisthi. 1982. Viscosity dependence of the kinetics of the diffusion-controlled reaction of carbon monoxide and myoglobin. Biochemistry 21:4275-4278.
    • (1982) Biochemistry , vol.21 , pp. 4275-4278
    • Hasinoff, B.B.1    Chisthi, S.B.2
  • 19
    • 0343632366 scopus 로고    scopus 로고
    • Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in gram-negative bacteria
    • Jacobs, C., J.-M. Frère, and S. Normark. 1997. Cytosolic intermediates for cell wall biosynthesis and degradation control inducible β-lactam resistance in gram-negative bacteria. Cell 88:823-832.
    • (1997) Cell , vol.88 , pp. 823-832
    • Jacobs, C.1    Frère, J.-M.2    Normark, S.3
  • 20
    • 0000283648 scopus 로고
    • Perfection in enzyme catalysis: The energetics of triosephosphate isomerase
    • Knowles, J. R., and W. J. Albery. 1977. Perfection in enzyme catalysis: the energetics of triosephosphate isomerase. Acc. Chem. Res. 10:105-111.
    • (1977) Acc. Chem. Res. , vol.10 , pp. 105-111
    • Knowles, J.R.1    Albery, W.J.2
  • 21
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • Amsterdam
    • Kramers, H. A. 1940. Brownian motion in a field of force and the diffusion model of chemical reactions. Physica (Amsterdam) 7:284-304.
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 22
    • 0023160841 scopus 로고
    • Adenosine deaminase: Viscosity studies and the mechanism of binding of substrate and of ground-and transition-state analogue inhibitors
    • Kurz, L. C., E. Weitkamp, and C. Frieden. 1987. Adenosine deaminase: viscosity studies and the mechanism of binding of substrate and of ground-and transition-state analogue inhibitors. Biochemistry 26:3027-3032.
    • (1987) Biochemistry , vol.26 , pp. 3027-3032
    • Kurz, L.C.1    Weitkamp, E.2    Frieden, C.3
  • 23
    • 0031973490 scopus 로고    scopus 로고
    • Kinship and diversification of bacterial penicillin-binding proteins and β-lactamases
    • Massova, I., and S. Mobashery. 1998. Kinship and diversification of bacterial penicillin-binding proteins and β-lactamases. Antimicrob. Agents Chemother. 42:1-17.
    • (1998) Antimicrob. Agents Chemother. , vol.42 , pp. 1-17
    • Massova, I.1    Mobashery, S.2
  • 24
    • 0033082703 scopus 로고    scopus 로고
    • The beta-lactamase cycle: A tale of selective pressure and bacterial ingenuity
    • Matagné, A., A. Dubus, M. Galleni, and J.-M. Frère. 1999. The beta-lactamase cycle: a tale of selective pressure and bacterial ingenuity. Nat. Prod. Rep. 16:1-19.
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 1-19
    • Matagné, A.1    Dubus, A.2    Galleni, M.3    Frère, J.-M.4
  • 25
    • 0029941909 scopus 로고    scopus 로고
    • Catalytic mechanism of enteroccoccal kanamycin kinase (APH(3′)-IIIa): Viscosity, thio, and solvent isotope effects support a Theorell-Chance mechanism
    • McKay, G. A., and G. D. Wright 1996. Catalytic mechanism of enteroccoccal kanamycin kinase (APH(3′)-IIIa): viscosity, thio, and solvent isotope effects support a Theorell-Chance mechanism. Biochemistry 35:8680-8685.
    • (1996) Biochemistry , vol.35 , pp. 8680-8685
    • McKay, G.A.1    Wright, G.D.2
  • 26
    • 0031029659 scopus 로고    scopus 로고
    • Evolution and dissemination of β-lactamases accelerated by generation of β-lactam antibiotics
    • Medeiros, A. A. 1997. Evolution and dissemination of β-lactamases accelerated by generation of β-lactam antibiotics. Clin. Infect. Dis. 24(Suppl. 1): S19-S45.
    • (1997) Clin. Infect. Dis. , vol.24 , Issue.1 SUPPL.
    • Medeiros, A.A.1
  • 27
    • 0021699812 scopus 로고
    • Effect of water activity on enzyme action and stability
    • Monsan, P., and D. Combes. 1984. Effect of water activity on enzyme action and stability. Ann. N. Y. Acad. Sci. 434:48-60.
    • (1984) Ann. N. Y. Acad. Sci. , vol.434 , pp. 48-60
    • Monsan, P.1    Combes, D.2
  • 28
    • 0020163001 scopus 로고
    • Diffusion in gels
    • Muhr, A. H., and J. M. V. Blanshard. 1982. Diffusion in gels. Polymer 23:1012-1026.
    • (1982) Polymer , vol.23 , pp. 1012-1026
    • Muhr, A.H.1    Blanshard, J.M.V.2
  • 29
    • 0029311691 scopus 로고
    • β-Lactamase induction in gram-negative bacteria is intimately linked to peptidoglycan recycling
    • Normark, S. 1995. β-Lactamase induction in gram-negative bacteria is intimately linked to peptidoglycan recycling. Microb. Drug Res. 1:111-114.
    • (1995) Microb. Drug Res. , vol.1 , pp. 111-114
    • Normark, S.1
  • 30
    • 0020339538 scopus 로고
    • Identification of a novel ampC β-lactamase promoter in a clinical isolate of Escherichia coli
    • Olson, O., S. Bergstrom, and S. Normark. 1982. Identification of a novel ampC β-lactamase promoter in a clinical isolate of Escherichia coli. EMBO J. 1:1411-1416.
    • (1982) EMBO J. , vol.1 , pp. 1411-1416
    • Olson, O.1    Bergstrom, S.2    Normark, S.3
  • 31
    • 0023234281 scopus 로고
    • Enzyme kinetics in solvents of increased viscosity. Dynamic aspects of carbonic anhydrase catalysis
    • Pocker, Y., and N. Yanjic. 1987. Enzyme kinetics in solvents of increased viscosity. Dynamic aspects of carbonic anhydrase catalysis. Biochemistry 26:2597-2606.
    • (1987) Biochemistry , vol.26 , pp. 2597-2606
    • Pocker, Y.1    Yanjic, N.2
  • 32
    • 0014202840 scopus 로고
    • Origin and function of penicillinase: A problem in biochemical evolution
    • Pollock, M. R. 1967. Origin and function of penicillinase: a problem in biochemical evolution. Br. Med. J. 4:71-77.
    • (1967) Br. Med. J. , vol.4 , pp. 71-77
    • Pollock, M.R.1
  • 33
    • 0000107082 scopus 로고
    • Diffusion-controlled reaction rate to a buried active site
    • Samson, R., and J. M. Deutch. 1978. Diffusion-controlled reaction rate to a buried active site. J. Chem. Phys. 68:285-290.
    • (1978) J. Chem. Phys. , vol.68 , pp. 285-290
    • Samson, R.1    Deutch, J.M.2
  • 34
    • 0014913797 scopus 로고
    • An introspective view of penicillinase
    • Saz, A. K. 1970. An introspective view of penicillinase. J. Cell. Physiol. 76:397-404.
    • (1970) J. Cell. Physiol. , vol.76 , pp. 397-404
    • Saz, A.K.1
  • 35
    • 33847797897 scopus 로고
    • Orientation constrains and rotational diffusion in bimolecular solution kinetics. Simplification
    • Schurr, J. H., and J. Schmitz. 1976. Orientation constrains and rotational diffusion in bimolecular solution kinetics. Simplification. J. Phys. Chem. 80:1934-1936.
    • (1976) J. Phys. Chem. , vol.80 , pp. 1934-1936
    • Schurr, J.H.1    Schmitz, J.2
  • 36
    • 84986793930 scopus 로고
    • Kinetics of diffusion-controlled reaction between chemically asymmetric molecules. II. Approximate steady-state solution
    • Solc, K., and W. H. Stockmayer. 1973. Kinetics of diffusion-controlled reaction between chemically asymmetric molecules. II. Approximate steady-state solution. Int. J. Chem. Kinet. 5:733-752.
    • (1973) Int. J. Chem. Kinet. , vol.5 , pp. 733-752
    • Solc, K.1    Stockmayer, W.H.2
  • 38
    • 0013787826 scopus 로고
    • Penicillin: Its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis
    • Wise, E. M., and J. T. Park. 1965. Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell wall mucopeptide synthesis. Proc. Natl. Acad. Sci. USA 54:75-81.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 75-81
    • Wise, E.M.1    Park, J.T.2
  • 39
    • 0028167838 scopus 로고
    • β-Lactam-recognizing enzymes exhibit different structural specificity in acyclic amide and ester substrates: A starting point in β-lactamase evolution?
    • Xu, Y., and R. F. Pratt. 1994. β-Lactam-recognizing enzymes exhibit different structural specificity in acyclic amide and ester substrates: a starting point in β-lactamase evolution? Bioorg. Med. Chem. Lett. 4:2291-2296.
    • (1994) Bioorg. Med. Chem. Lett. , vol.4 , pp. 2291-2296
    • Xu, Y.1    Pratt, R.F.2
  • 40
    • 0028001382 scopus 로고
    • Relative specificities of a series of β-lactam-recognizing enzymes towards side-chain of penicillins and of acyclic thioldepsipeptides
    • Xu, Y., G. Soto, H. Adachi, M. P. G. van der Linden, W. Keck, and R. F. Pratt. 1994. Relative specificities of a series of β-lactam-recognizing enzymes towards side-chain of penicillins and of acyclic thioldepsipeptides. Biochem. J. 302:851-856.
    • (1994) Biochem. J. , vol.302 , pp. 851-856
    • Xu, Y.1    Soto, G.2    Adachi, H.3    Van Der Linden, M.P.G.4    Keck, W.5    Pratt, R.F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.