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Volumn 43, Issue 22, 2004, Pages 7046-7053

Toward better antibiotics: Crystallographic studies of a novel class of DD-peptidase/β-lactamase inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; BACTERIOLOGY; CELLS; CRYSTALLOGRAPHY; ENZYMES; PATIENT TREATMENT;

EID: 2642588180     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049612c     Document Type: Article
Times cited : (18)

References (40)
  • 1
    • 77956796844 scopus 로고
    • (Ghuysen, J.-M., and Hakenbeck, R., Eds.). Elsevier, Amsterdam, The Netherlands
    • Spratt, B. G. (1994) in Bacterial Cell Wall (Ghuysen, J.-M., and Hakenbeck, R., Eds.) pp 517-534, Elsevier, Amsterdam, The Netherlands.
    • (1994) Bacterial Cell Wall , pp. 517-534
    • Spratt, B.G.1
  • 2
    • 0024561489 scopus 로고
    • Enzymes in the D-alanine branch of bacterial cell wall peptidoglycan assembly
    • Walsh, C. T. (1989) Enzymes in the D-alanine branch of bacterial cell wall peptidoglycan assembly, J. Biol. Chem. 264, 2393-2396.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2393-2396
    • Walsh, C.T.1
  • 3
    • 0026880575 scopus 로고
    • Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: Enzymology, antibiotics, and antibiotic resistance
    • Bugg, T. D., and Walsh, C. T. (1992) Intracellular steps of bacterial cell wall peptidoglycan biosynthesis: enzymology, antibiotics, and antibiotic resistance, Nat. Prod. Rep. 9, 199-215.
    • (1992) Nat. Prod. Rep. , vol.9 , pp. 199-215
    • Bugg, T.D.1    Walsh, C.T.2
  • 5
    • 0021943163 scopus 로고
    • Penicillin-sensitive enzymes in peptidoglycan biosynthesis
    • Frère J. M., and Joris, B. (1985) Penicillin-sensitive enzymes in peptidoglycan biosynthesis, CRC Crit. Rev. Microbiol. 11, 299-396.
    • (1985) CRC Crit. Rev. Microbiol. , vol.11 , pp. 299-396
    • Frère, J.M.1    Joris, B.2
  • 6
    • 0034515505 scopus 로고    scopus 로고
    • Penicillin binding proteins, β-lactams, and β-lactamases: Offensives, attacks, and defensive countermeasures
    • Koch, A. L. (2000) Penicillin binding proteins, β-lactams, and β-lactamases: offensives, attacks, and defensive countermeasures, Crit. Rev. Microbiol. 26, 205-220.
    • (2000) Crit. Rev. Microbiol. , vol.26 , pp. 205-220
    • Koch, A.L.1
  • 7
    • 0036014011 scopus 로고    scopus 로고
    • Functional evolution of the serine β-lactamase active site
    • Pratt, R. F. (2002) Functional evolution of the serine β-lactamase active site, J. Chem. Soc., Perkin Trans. 2, 851-861.
    • (2002) J. Chem. Soc., Perkin Trans. , vol.2 , pp. 851-861
    • Pratt, R.F.1
  • 8
    • 0020972419 scopus 로고
    • Penicillin-binding proteins and the mechanism of action of β-lactam antibiotics
    • Waxman, D. J., and Strominger, J. L. (1983) Penicillin-binding proteins and the mechanism of action of β-lactam antibiotics, Annu. Rev. Biochem. 52, 825-869.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 825-869
    • Waxman, D.J.1    Strominger, J.L.2
  • 9
    • 0013808622 scopus 로고
    • Mechanism of action of penicillins: A proposal based on their structural similarity to acyl-D-alanyl-D-alanine
    • Tipper, D. J., and Strominger, J. L. (1965) Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine, Proc. Natl. Acad. Sci. U.S.A. 54, 1133-1141.
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 1133-1141
    • Tipper, D.J.1    Strominger, J.L.2
  • 10
    • 0021991655 scopus 로고
    • Mode of action of β-lactam antibiotics
    • Tipper, D. J. (1985) Mode of action of β-lactam antibiotics, Pharmacol. Ther. 27, 1-35.
    • (1985) Pharmacol. Ther. , vol.27 , pp. 1-35
    • Tipper, D.J.1
  • 12
    • 33845379247 scopus 로고
    • Penicillin resistance: The chemistry of β-lactamase inhibition
    • Knowles, J. R. (1985) Penicillin resistance: the chemistry of β-lactamase inhibition, Acc. Chem. Res. 18, 97-104.
    • (1985) Acc. Chem. Res. , vol.18 , pp. 97-104
    • Knowles, J.R.1
  • 13
    • 0023870553 scopus 로고
    • β-lactamases as the main resistance factor to penicillin-related antibiotics
    • Frère, J. M., and Joris, B. (1988) β-lactamases as the main resistance factor to penicillin-related antibiotics, Ann. Biol. Clin. 46, 151-156.
    • (1988) Ann. Biol. Clin. , vol.46 , pp. 151-156
    • Frère, J.M.1    Joris, B.2
  • 14
    • 0019782527 scopus 로고
    • Inhibition of β-lactamases from Gram-negative bacteria by clavulanic acid
    • Reading, C., and Farmer, T. (1981) Inhibition of β-lactamases from Gram-negative bacteria by clavulanic acid, Biochem. J. 199, 779-787.
    • (1981) Biochem. J. , vol.199 , pp. 779-787
    • Reading, C.1    Farmer, T.2
  • 15
    • 0024582859 scopus 로고
    • Characterization of β-lactamases
    • Bush, K. (1989) Characterization of β-lactamases, Antimicrob. Agents Chemother. 33, 259-263.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 259-263
    • Bush, K.1
  • 16
    • 0001817705 scopus 로고
    • (Page, M. I., Ed.). Blackie Academic & Professional, London, U.K
    • Waley, S. G. (1992) in The Chemistry of β-Lactams (Page, M. I., Ed.) pp 198-228, Blackie Academic & Professional, London, U.K.
    • (1992) The Chemistry of β-Lactams , pp. 198-228
    • Waley, S.G.1
  • 17
    • 0032495765 scopus 로고    scopus 로고
    • Salicyloyl cyclic phosphate, a "penicillin-like" inhibitor of β-lactamases
    • Pratt, R. F., and Hammar, N. J. (1998) Salicyloyl cyclic phosphate, a "penicillin-like" inhibitor of β-lactamases, J. Am. Chem. Soc. 120, 3004-3006.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3004-3006
    • Pratt, R.F.1    Hammar, N.J.2
  • 18
    • 0035980397 scopus 로고    scopus 로고
    • Mechanism of inhibition of the class C β-lactamase of enterobacter cloacae P99 by cyclic acyl phosph(on)ates: Rescue by return
    • Kaur, K., Lan, M. J., and Pratt, R. F. (2001) Mechanism of Inhibition of the Class C β-Lactamase of Enterobacter cloacae P99 by Cyclic Acyl Phosph(on)ates: Rescue by Return, J. Am. Chem. Soc. 123, 10436-10443.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 10436-10443
    • Kaur, K.1    Lan, M.J.2    Pratt, R.F.3
  • 19
    • 0037452523 scopus 로고    scopus 로고
    • Inhibition of β-lactamases by monocyclic acyl phosph(on)ates
    • Kaur, K., Adediran, S. A., Lan, M. J., and Pratt, R. F. (2003) Inhibition of β-lactamases by monocyclic acyl phosph(on)ates, Biochemistry 42, 1529-1536.
    • (2003) Biochemistry , vol.42 , pp. 1529-1536
    • Kaur, K.1    Adediran, S.A.2    Lan, M.J.3    Pratt, R.F.4
  • 20
    • 0033543182 scopus 로고    scopus 로고
    • On the importance of a methyl group in β-lactamase evolution: Free energy profiles and molecular modeling
    • Bernstein, N. J., and Pratt, R. (1999) On the importance of a methyl group in β-lactamase evolution: Free energy profiles and molecular modeling, Biochemistry 38, 10499-10510.
    • (1999) Biochemistry , vol.38 , pp. 10499-10510
    • Bernstein, N.J.1    Pratt, R.2
  • 21
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. (1996) Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase, Anal. Biochem. 237, 260-273.
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 22
    • 0024450592 scopus 로고
    • Crystallographic mapping of β-lactams bound to a DD-peptidase
    • Kelly, J. A., Knox, J. R., Zhao, H., Frère, J.-M., and Ghuysen, J.-M. (1989) Crystallographic mapping of β-lactams bound to a DD-peptidase, J. Mol. Biol. 209, 281-295.
    • (1989) J. Mol. Biol. , vol.209 , pp. 281-295
    • Kelly, J.A.1    Knox, J.R.2    Zhao, H.3    Frère, J.-M.4    Ghuysen, J.-M.5
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 25
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High-resolution refinement
    • Sheldrick, G. M., and Schneider, T. R. (1997) SHELXL: high-resolution refinement, Methods Enzymol. 277, 319-343.
    • (1997) Methods Enzymol. , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 26
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. E. (1999) XtalView/Xfit- -A versatile program for manipulating atomic coordinates and electron density, J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 27
    • 0028224698 scopus 로고
    • Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: Mechanistic interpretation of a β-lactamase transition-state analogue
    • Lobkovsky, E., Billings, E. M., Moews, P. C., Rahil, J., Pratt, R. F., and Knox, J. R. (1994) Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: Mechanistic interpretation of a β-lactamase transition-state analogue, Biochemistry 33, 6762-6772.
    • (1994) Biochemistry , vol.33 , pp. 6762-6772
    • Lobkovsky, E.1    Billings, E.M.2    Moews, P.C.3    Rahil, J.4    Pratt, R.F.5    Knox, J.R.6
  • 28
    • 0037432016 scopus 로고    scopus 로고
    • Crystal structure of phosphonate-inhibited D-Ala-D-Ala peptidase reveals an analogue of a tetrahedral transition state
    • Silvaggi, N. R., Anderson, J. W., Brinsmade, S. R., Pratt, R. F., Kelly, J. A. (2003) Crystal Structure of Phosphonate-Inhibited D-Ala-D-Ala Peptidase Reveals an Analogue of a Tetrahedral Transition State, Biochemistry 42, 1199-1208.
    • (2003) Biochemistry , vol.42 , pp. 1199-1208
    • Silvaggi, N.R.1    Anderson, J.W.2    Brinsmade, S.R.3    Pratt, R.F.4    Kelly, J.A.5
  • 29
    • 0028806595 scopus 로고
    • Refined crystallographic structure of a DD-peptidase penicillin target enzyme at 1.6 Å resolution
    • Kelly, J. A., and Kuzin, A. P. (1995) Refined crystallographic structure of a DD-peptidase penicillin target enzyme at 1.6 Å resolution, J. Mol. Biol. 254, 223-236.
    • (1995) J. Mol. Biol. , vol.254 , pp. 223-236
    • Kelly, J.A.1    Kuzin, A.P.2
  • 30
    • 0036965578 scopus 로고    scopus 로고
    • Structures of two kinetic intermediates reveal species specificity of penicillin-binding proteins
    • McDonough, M., Anderson, J., Silvaggi, N., Pratt, R., Knox, J., and Kelly, J. (2002) Structures of Two Kinetic Intermediates Reveal Species Specificity of Penicillin-Binding Proteins, J. Mol. Biol. 322, 111.
    • (2002) J. Mol. Biol. , vol.322 , pp. 111
    • McDonough, M.1    Anderson, J.2    Silvaggi, N.3    Pratt, R.4    Knox, J.5    Kelly, J.6
  • 31
    • 0029147002 scopus 로고
    • Binding of cephalothin and cefotaxime to D-ala-D-ala peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum β-lactamases
    • Kuzin, A. P., Liu, H., Kelly, J. A., and Knox, J. R. (1995) Binding of cephalothin and cefotaxime to D-ala-D-ala peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum β-lactamases, Biochemistry 34, 9532-9540.
    • (1995) Biochemistry , vol.34 , pp. 9532-9540
    • Kuzin, A.P.1    Liu, H.2    Kelly, J.A.3    Knox, J.R.4
  • 33
    • 0027428548 scopus 로고
    • Evolution of an enzyme activity: Crystallographic structure at 2 Å resolution of the cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase
    • Lobkovsky, E., Moews, P. C., Liu, H., Zhao, H., Frère, J.-M., and Knox, J. R. (1993) Evolution of an enzyme activity: Crystallographic structure at 2 Å resolution of the cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase, Proc. Natl. Acad. Sci. U.S.A. 90, 11257-11261.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 11257-11261
    • Lobkovsky, E.1    Moews, P.C.2    Liu, H.3    Zhao, H.4    Frère, J.-M.5    Knox, J.R.6
  • 34
    • 0043127209 scopus 로고    scopus 로고
    • Structural aspects for evolution of β-lactamases from penicillin-binding proteins
    • Meroueh, S. O., Minasov, G., Lee, W., Shoichet, B. K., and Mobashery, S. (2003) Structural aspects for evolution of β-lactamases from penicillin-binding proteins, J. Am. Chem. Soc. 125, 9612-9618.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9612-9618
    • Meroueh, S.O.1    Minasov, G.2    Lee, W.3    Shoichet, B.K.4    Mobashery, S.5
  • 35
    • 0031973490 scopus 로고    scopus 로고
    • Kinship and diversification of bacterial penicillin-binding proteins and β-lactamases
    • Massova, I., and Mobashery, S. (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
  • 37
    • 0035901551 scopus 로고    scopus 로고
    • Mechanism of reaction of acyl phosph(on)ates with the β-lactamase of Enterobacter cloacae P99
    • Kaur, K., and Pratt, R. F. (2001) Mechanism of reaction of acyl phosph(on)ates with the β-lactamase of Enterobacter cloacae P99, Biochemistry 40, 4610-4621.
    • (2001) Biochemistry , vol.40 , pp. 4610-4621
    • Kaur, K.1    Pratt, R.F.2
  • 38
    • 0034633999 scopus 로고    scopus 로고
    • Dipeptide binding to the extended active site of the Streptomyces R61 D-alanyl-D-alanine peptidase: The path to a specific substrate
    • Anderson, J. W., and Pratt, R. F. (2000) Dipeptide binding to the extended active site of the Streptomyces R61 D-alanyl-D-alanine peptidase: The path to a specific substrate, Biochemistry 39, 12200-12209.
    • (2000) Biochemistry , vol.39 , pp. 12200-12209
    • Anderson, J.W.1    Pratt, R.F.2
  • 39
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merrit, E. A., and Bacon, D. J. (1997) Raster3D: Photorealistic molecular graphics, Methods Enzymol. 277, 505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merrit, E.A.1    Bacon, D.J.2
  • 40
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1


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