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Volumn 44, Issue 34, 2005, Pages 11581-11591

Enzyme-substrate interactions with an antibiotic resistance enzyme: Aminoglycoside nucleotidyltransferase(2″)-Ia characterized by kinetic and thermodynamic methods

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; BACTERIA; BIOCHEMISTRY; CATALYSIS; ENTHALPY; ENTROPY; PARAMAGNETIC RESONANCE; TEMPERATURE DISTRIBUTION;

EID: 23944495538     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050797c     Document Type: Article
Times cited : (27)

References (62)
  • 1
    • 0015694583 scopus 로고
    • Mechanisms of antibiotic resistance in bacteria
    • Benveniste, R., and Davies, J. (1973) Mechanisms of antibiotic resistance in bacteria, Annu. Rev. Biochem. 42, 471-506.
    • (1973) Annu. Rev. Biochem. , vol.42 , pp. 471-506
    • Benveniste, R.1    Davies, J.2
  • 2
    • 0030956372 scopus 로고    scopus 로고
    • MdfA, an Escherichia coli multidrug resistance protein with an extraordinarily broad spectrum of drug recognition [erratum: (1997) J. Bacteriol. 179 (17), 5654]
    • Edgar, R., and Bibi, E. (1997) MdfA, an Escherichia coli multidrug resistance protein with an extraordinarily broad spectrum of drug recognition [erratum: (1997) J. Bacteriol. 179 (17), 5654], J. Bacteriol. 179, 2274-2280.
    • (1997) J. Bacteriol. , vol.179 , pp. 2274-2280
    • Edgar, R.1    Bibi, E.2
  • 3
    • 0035986724 scopus 로고    scopus 로고
    • Aminoglycoside antibiotic resistance by enzymatic deactivation
    • Smith, C. A., and Baker, E. N. (2002) Aminoglycoside antibiotic resistance by enzymatic deactivation, Curr. Drug Targets: Infect. Disord. 2, 143-160.
    • (2002) Curr. Drug Targets: Infect. Disord. , vol.2 , pp. 143-160
    • Smith, C.A.1    Baker, E.N.2
  • 4
    • 0034426097 scopus 로고    scopus 로고
    • Aminoglycosides: Perspectives on mechanisms of action and resistance and strategies to counter resistance
    • Kotra, L. P., Haddad, J., and Mobashery, S. (2000) Aminoglycosides: perspectives on mechanisms of action and resistance and strategies to counter resistance, Antimicrob. Agents Chemother. 44, 3249-3256.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 3249-3256
    • Kotra, L.P.1    Haddad, J.2    Mobashery, S.3
  • 5
    • 0036237683 scopus 로고    scopus 로고
    • Aminoglycosides modified by resistance enzymes display diminished binding to the bacterial ribosomal aminoacyl-tRNA site
    • Llano-Sotelo, B., Azucena, E. F., Jr., Kotra, L. P., Mobashery, S., and Chow, C. S. (2002) Aminoglycosides modified by resistance enzymes display diminished binding to the bacterial ribosomal aminoacyl-tRNA site, Chem. Biol. 9, 455-463.
    • (2002) Chem. Biol. , vol.9 , pp. 455-463
    • Llano-Sotelo, B.1    Azucena Jr., E.F.2    Kotra, L.P.3    Mobashery, S.4    Chow, C.S.5
  • 6
    • 0027478123 scopus 로고
    • Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes
    • Shaw, K. J., Rather, P. N., Hare, R. S., and Miller, G. H. (1993) Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes, Microbiol. Rev. 57, 138-163.
    • (1993) Microbiol. Rev. , vol.57 , pp. 138-163
    • Shaw, K.J.1    Rather, P.N.2    Hare, R.S.3    Miller, G.H.4
  • 7
    • 0242365248 scopus 로고
    • R-factor mediated gentamicin resistance: A new enzyme which modifies aminoglycoside antibiotics
    • Benveniste, R., and Davies, J. (1971) R-factor mediated gentamicin resistance: A new enzyme which modifies aminoglycoside antibiotics, FEBS Lett. 14, 293-296.
    • (1971) FEBS Lett. , vol.14 , pp. 293-296
    • Benveniste, R.1    Davies, J.2
  • 8
  • 10
    • 0016367512 scopus 로고
    • Gentamicin:adenine mononucleotide transferase: Partial purification, characterization, and use in the clinical quantitation of gentamicin
    • Smith, A. L., and Smith, D. H. (1974) Gentamicin:adenine mononucleotide transferase: partial purification, characterization, and use in the clinical quantitation of gentamicin, J. Infect. Dis. 129, 391-401.
    • (1974) J. Infect. Dis. , vol.129 , pp. 391-401
    • Smith, A.L.1    Smith, D.H.2
  • 11
    • 0021349419 scopus 로고
    • Relation between aminoglycoside 2″-O-nucleotidyltransferase activity and aminoglycoside resistance
    • Bongaerts, G. P., and Molendijk, L. (1984) Relation between aminoglycoside 2″-O-nucleotidyltransferase activity and aminoglycoside resistance, Antimicrob. Agents Chemother. 25, 234-237.
    • (1984) Antimicrob. Agents Chemother. , vol.25 , pp. 234-237
    • Bongaerts, G.P.1    Molendijk, L.2
  • 12
    • 0017717867 scopus 로고
    • Resistance of bacteria to the newer aminoglycoside antibiotics: An epidemiological and enzymatic study
    • Devaud, M., Kayser, F. H., and Huber, U. (1977) Resistance of bacteria to the newer aminoglycoside antibiotics: an epidemiological and enzymatic study, J. Antibiot. 30, 655-664.
    • (1977) J. Antibiot. , vol.30 , pp. 655-664
    • Devaud, M.1    Kayser, F.H.2    Huber, U.3
  • 13
    • 0019166125 scopus 로고
    • Properties of gentamicin adenylyl transferase obtained from R-factor-resistant Escherichia coli
    • Lombardini, J. B., and Cheng-Chu, M. (1980) Properties of gentamicin adenylyl transferase obtained from R-factor-resistant Escherichia coli, Int. J. Biochem. 12, 427-431.
    • (1980) Int. J. Biochem. , vol.12 , pp. 427-431
    • Lombardini, J.B.1    Cheng-Chu, M.2
  • 14
    • 0023937023 scopus 로고
    • Substrate specificities and structure-activity relationships for the nucleotidylation of antibiotics catalyzed by aminoglycoside nucleotidyltransferase 2″-I
    • Gates, C. A., and Northrop, D. B. (1988) Substrate specificities and structure-activity relationships for the nucleotidylation of antibiotics catalyzed by aminoglycoside nucleotidyltransferase 2″-I, Biochemistiy 27, 3820-3825.
    • (1988) Biochemistiy , vol.27 , pp. 3820-3825
    • Gates, C.A.1    Northrop, D.B.2
  • 15
    • 0024290399 scopus 로고
    • Alternative substrate and inhibition kinetics of aminoglycoside nucleotidyltransferase 2″-I in support of a Theorell-Chance kinetic mechanism [erratum: (1989) Biochemistry 28 (4), 1930]
    • Gates, C. A., and Northrop, D. B. (1988) Alternative substrate and inhibition kinetics of aminoglycoside nucleotidyltransferase 2″-I in support of a Theorell-Chance kinetic mechanism [erratum: (1989) Biochemistry 28 (4), 1930], Biochemistry 27, 3826-3833.
    • (1988) Biochemistry , vol.27 , pp. 3826-3833
    • Gates, C.A.1    Northrop, D.B.2
  • 16
    • 0021268095 scopus 로고
    • Purification and properties of gentamicin nucleotidyltransferase from Escherichia coli: Nucleotide specificity, pH optimum, and the separation of two electrophoretic variants
    • Van Pelt, J. E., and Northrop, D. B. (1984) Purification and properties of gentamicin nucleotidyltransferase from Escherichia coli: nucleotide specificity, pH optimum, and the separation of two electrophoretic variants. Arch. Biochem. Biophys. 230, 250-263.
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 250-263
    • Van Pelt, J.E.1    Northrop, D.B.2
  • 17
    • 2642580087 scopus 로고    scopus 로고
    • Isolation of aminoglycoside nucleotidyltransferase(2″)-Ia from inclusion bodies as active, monomeric enzyme
    • Wright, E., and Serpersu, E. H. (2004) Isolation of aminoglycoside nucleotidyltransferase(2″)-Ia from inclusion bodies as active, monomeric enzyme, Protein Expression Purif. 35, 373-380.
    • (2004) Protein Expression Purif. , vol.35 , pp. 373-380
    • Wright, E.1    Serpersu, E.H.2
  • 19
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 21
    • 33645494328 scopus 로고    scopus 로고
    • Kinetic and thermodynamic characterization of an aminoglycoside resistance enzyme, Aminoglycoside nucleotidyltransferase(2)-Ia
    • Research Triangle Park, NC
    • Wright, E., and Serpersu, E. (2004) Kinetic and thermodynamic characterization of an aminoglycoside resistance enzyme, Aminoglycoside nucleotidyltransferase(2)-Ia, Southeastern Regional Meeting of the American Chemical Society, Research Triangle Park, NC.
    • (2004) Southeastern Regional Meeting of the American Chemical Society
    • Wright, E.1    Serpersu, E.2
  • 23
    • 0028358078 scopus 로고
    • Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: Overexpression, purification, and substrate specificity
    • McKay, G. A., Thompson, P. R., and Wright, G. D. (1994) Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: overexpression, purification, and substrate specificity, Biochemistry 33, 6936-6944.
    • (1994) Biochemistry , vol.33 , pp. 6936-6944
    • McKay, G.A.1    Thompson, P.R.2    Wright, G.D.3
  • 24
    • 0035912790 scopus 로고    scopus 로고
    • Cloning, overexpression, and purification of aminoglycoside antibiotic nucleotidyltransferase (2″)-Ia: Conformational studies with bound substrates
    • Ekman, D. R., DiGiammarino, E. L., Wright, E., Witter, E. D., and Serpersu, E. H. (2001) Cloning, overexpression, and purification of aminoglycoside antibiotic nucleotidyltransferase (2″)-Ia: conformational studies with bound substrates, Biochemistry 40, 7017-7024.
    • (2001) Biochemistry , vol.40 , pp. 7017-7024
    • Ekman, D.R.1    Digiammarino, E.L.2    Wright, E.3    Witter, E.D.4    Serpersu, E.H.5
  • 25
    • 0017821705 scopus 로고
    • Control of complex metal ion equilibria in biochemical reaction systems. Intrinsic and apparent stability constants of metal-adenine nucleotide complexes
    • Adolfsen, R., and Moudrianakis, E. N. (1978) Control of complex metal ion equilibria in biochemical reaction systems. Intrinsic and apparent stability constants of metal-adenine nucleotide complexes, J. Biol. Chem. 253, 4378-4379.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4378-4379
    • Adolfsen, R.1    Moudrianakis, E.N.2
  • 26
    • 0035577336 scopus 로고    scopus 로고
    • Rapid measurement of low levels of sodium, potassium-ATPase activity by ascorbic acid reduction without strong acid
    • Spokas, E. G., and Spur, B. W. (2001) Rapid measurement of low levels of sodium, potassium-ATPase activity by ascorbic acid reduction without strong acid, Anal. Biochem. 299, 112-116.
    • (2001) Anal. Biochem. , vol.299 , pp. 112-116
    • Spokas, E.G.1    Spur, B.W.2
  • 27
    • 4244120872 scopus 로고
    • Microdetermination of Phosphorus
    • Chen, P. S., Toribara, T. Y., and Warner, H. (1956) Microdetermination of Phosphorus, Anal. Chem. 28, 1756-1759.
    • (1956) Anal. Chem. , vol.28 , pp. 1756-1759
    • Chen, P.S.1    Toribara, T.Y.2    Warner, H.3
  • 28
    • 0013612812 scopus 로고
    • (Boyer, P., Ed.), Academic Press, New York
    • Cleland, W. W. (1970) in The Enzymes (Boyer, P., Ed.) pp 1-65, Academic Press, New York.
    • (1970) The Enzymes , pp. 1-65
    • Cleland, W.W.1
  • 30
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J. F., and Lin, L. N. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter, Anal. Biochem. 179, 131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 31
    • 0032189652 scopus 로고    scopus 로고
    • Sequence specificity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interaction
    • Esposito, D., and Craigie, R. (1998) Sequence specificity of viral end DNA binding by HIV-1 integrase reveals critical regions for protein-DNA interaction, EMBO J. 17, 5832-5843.
    • (1998) EMBO J. , vol.17 , pp. 5832-5843
    • Esposito, D.1    Craigie, R.2
  • 33
    • 0001423719 scopus 로고
    • A study of manganous complexes by paramagnetic resonance absorption
    • Cohn, M., and Townsend, J. (1954) A study of manganous complexes by paramagnetic resonance absorption, Nature 173, 1090-1091.
    • (1954) Nature , vol.173 , pp. 1090-1091
    • Cohn, M.1    Townsend, J.2
  • 34
    • 0023651160 scopus 로고
    • ADP, chloride ion, and metal ion binding to bovine brain glutamine synthetase
    • Maurizi, M. R., Pinkofsky, H. B., and Ginsburg, A. (1987) ADP, chloride ion, and metal ion binding to bovine brain glutamine synthetase, Biochemistry 26, 5023-5031.
    • (1987) Biochemistry , vol.26 , pp. 5023-5031
    • Maurizi, M.R.1    Pinkofsky, H.B.2    Ginsburg, A.3
  • 35
    • 0030026560 scopus 로고    scopus 로고
    • Asp537 and Asp812 in bacteriophage T7 RNA polymerase as metal ion-binding sites studied by EPR, flow-dialysis, and transcription
    • Woody, A. Y., Eaton, S. S., Osumi-Davis, P. A., and Woody, R. W. (1996) Asp537 and Asp812 in bacteriophage T7 RNA polymerase as metal ion-binding sites studied by EPR, flow-dialysis, and transcription, Biochemistry 35, 144-152.
    • (1996) Biochemistry , vol.35 , pp. 144-152
    • Woody, A.Y.1    Eaton, S.S.2    Osumi-Davis, P.A.3    Woody, R.W.4
  • 36
    • 0018719364 scopus 로고
    • Stability constants for biologically important metal-ligand complexes
    • O'Sullivan, W. J., and Smithers, G. W. (1979) Stability constants for biologically important metal-ligand complexes, Methods Enzymol. 63, 294-336.
    • (1979) Methods Enzymol. , vol.63 , pp. 294-336
    • O'Sullivan, W.J.1    Smithers, G.W.2
  • 37
    • 0035979336 scopus 로고    scopus 로고
    • Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase
    • Burk, D. L., Hon, W. C., Leung, A. K, and Berghuis, A. M. (2001) Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase, Biochemistry 40, 8756-8764.
    • (2001) Biochemistry , vol.40 , pp. 8756-8764
    • Burk, D.L.1    Hon, W.C.2    Leung, A.K.3    Berghuis, A.M.4
  • 38
    • 0027163526 scopus 로고
    • Crystal structure of bacteriophage T7 RNA polymerase at 3.3 a resolution
    • Sousa, R., Chung, Y. J., Rose, J. P., and Wang, B. C. (1993) Crystal structure of bacteriophage T7 RNA polymerase at 3.3 A resolution [see comment], Nature 364, 593-599.
    • (1993) Nature , vol.364 , pp. 593-599
    • Sousa, R.1    Chung, Y.J.2    Rose, J.P.3    Wang, B.C.4
  • 39
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69
    • Wang, J., Sattar, A. K., Wang, C. C., Karam, J. D., Konigsberg, W. H., and Steitz, T. A. (1997) Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69, Cell 89, 1087-1099.
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1    Sattar, A.K.2    Wang, C.C.3    Karam, J.D.4    Konigsberg, W.H.5    Steitz, T.A.6
  • 40
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublie, S., Tabor, S., Long, A. M., Richardson, C. C., and Ellenberger, T. (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution [see comment], Nature 391, 251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 41
    • 0031571638 scopus 로고    scopus 로고
    • Structure of the RNA-dependent RNA polymerase of poliovirus
    • Hansen, J. L., Long, A. M., and Schultz, S. C. (1997) Structure of the RNA-dependent RNA polymerase of poliovirus, Structure 5, 1109-1122.
    • (1997) Structure , vol.5 , pp. 1109-1122
    • Hansen, J.L.1    Long, A.M.2    Schultz, S.C.3
  • 42
    • 0027496278 scopus 로고
    • Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-Å resolution
    • Sakon, J., Liao, H. H., Kanikula, A. M., Henning, M. M., Rayment, I., and Holden, H. M. (1993) Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-Å resolution, Biochemistry 32, 11977-11984.
    • (1993) Biochemistry , vol.32 , pp. 11977-11984
    • Sakon, J.1    Liao, H.H.2    Kanikula, A.M.3    Henning, M.M.4    Rayment, I.5    Holden, H.M.6
  • 43
    • 0033080180 scopus 로고    scopus 로고
    • Prodigious substrate specificity of AAC(6′)-APH(2″), an aminoglycoside antibiotic resistance determinant in enterococci and staphylococci
    • Daigle, D. M., Hughes, D. W., and Wright, G. D. (1999) Prodigious substrate specificity of AAC(6′)-APH(2″), an aminoglycoside antibiotic resistance determinant in enterococci and staphylococci, Chem. Biol. 6, 99-110.
    • (1999) Chem. Biol. , vol.6 , pp. 99-110
    • Daigle, D.M.1    Hughes, D.W.2    Wright, G.D.3
  • 44
    • 0032716399 scopus 로고    scopus 로고
    • Kinetic Mechanism of Kanamycin Nucleotidyltransferase from Staphylococcus aureus
    • Chen-Goodspeed, M., Vanhooke, J. L., Holden, H. M., and Raushel, F. M. (1999) Kinetic Mechanism of Kanamycin Nucleotidyltransferase from Staphylococcus aureus, Bioorg. Chem. 27, 395-408.
    • (1999) Bioorg. Chem. , vol.27 , pp. 395-408
    • Chen-Goodspeed, M.1    Vanhooke, J.L.2    Holden, H.M.3    Raushel, F.M.4
  • 45
    • 0032892950 scopus 로고    scopus 로고
    • Semisynthetic aminoglycoside antibiotics: Development and enzymatic modifications
    • Kondo, S., and Hotta, K. (1999) Semisynthetic aminoglycoside antibiotics: Development and enzymatic modifications, J. Infect. Chemother. 5, 1-9.
    • (1999) J. Infect. Chemother. , vol.5 , pp. 1-9
    • Kondo, S.1    Hotta, K.2
  • 46
    • 0037015158 scopus 로고    scopus 로고
    • Cloning, overexpression, and purification of aminoglycoside antibiotic 3-acetyltransferase-IIIb: Conformational studies with bound substrates
    • Owston, M. A., and Serpersu, E. H. (2002) Cloning, overexpression, and purification of aminoglycoside antibiotic 3-acetyltransferase-IIIb: conformational studies with bound substrates, Biochemistry 41, 10764-10770.
    • (2002) Biochemistry , vol.41 , pp. 10764-10770
    • Owston, M.A.1    Serpersu, E.H.2
  • 47
    • 0032539959 scopus 로고    scopus 로고
    • Solution studies of isepamicin and conformational comparisons between isepamicin and butirosin a when bound to an aminoglycoside 6′-N- acetyltransferase determined by NMR spectroscopy
    • DiGiammarino, E. L., Draker, K. A., Wright, G. D., and Serpersu, E. H. (1998) Solution studies of isepamicin and conformational comparisons between isepamicin and butirosin A when bound to an aminoglycoside 6′-N- acetyltransferase determined by NMR spectroscopy, Biochemistry 37, 3638-3644.
    • (1998) Biochemistry , vol.37 , pp. 3638-3644
    • Digiammarino, E.L.1    Draker, K.A.2    Wright, G.D.3    Serpersu, E.H.4
  • 48
    • 0034577239 scopus 로고    scopus 로고
    • Aminoglycoside antibiotics bound to aminoglycoside-detoxifying enzymes and RNA adopt similar conformations
    • Cox, J. R., Ekman, D. R., DiGiammarino, E. L., Akal-Strader, A., and Serpersu, E. H. (2000) Aminoglycoside antibiotics bound to aminoglycoside- detoxifying enzymes and RNA adopt similar conformations, Cell Biochem. Biophys. 33, 297-308.
    • (2000) Cell Biochem. Biophys. , vol.33 , pp. 297-308
    • Cox, J.R.1    Ekman, D.R.2    Digiammarino, E.L.3    Akal-Strader, A.4    Serpersu, E.H.5
  • 50
    • 0015676874 scopus 로고
    • Structure-activity relationships among the aminoglycoside antibiotics: Role of hydroxyl and amino groups
    • Benveniste, R., and Davies, J. (1973) Structure-activity relationships among the aminoglycoside antibiotics: role of hydroxyl and amino groups, Antimicrob. Agents Chemother. 4, 402-409.
    • (1973) Antimicrob. Agents Chemother. , vol.4 , pp. 402-409
    • Benveniste, R.1    Davies, J.2
  • 51
    • 0028879950 scopus 로고
    • Loss of Individual Electrostatic Interactions between Aminoglycoside Antibiotics and Resistance Enzymes as an Effective Means to Overcoming Bacterial Drug Resistance
    • Roestamadji, J., Graspas, I., and Mobashery, S. (1995) Loss of Individual Electrostatic Interactions between Aminoglycoside Antibiotics and Resistance Enzymes as an Effective Means to Overcoming Bacterial Drug Resistance, j. Am. Chem. Soc. 117, 11060-11069.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11060-11069
    • Roestamadji, J.1    Graspas, I.2    Mobashery, S.3
  • 54
    • 0026019625 scopus 로고
    • Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
    • Beese, L. S., and Steitz, T. A. (1991) Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism, EMBO J. 10, 25-33.
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 55
    • 0026351220 scopus 로고
    • Role of divalent cations in the 3′,5′-exonuclease reaction of DNA polymerase I
    • Han, H., Rifkind, J. M., and Mildvan, A. S. (1991) Role of divalent cations in the 3′,5′-exonuclease reaction of DNA polymerase I, Biochemistry 30, 11104-11108.
    • (1991) Biochemistry , vol.30 , pp. 11104-11108
    • Han, H.1    Rifkind, J.M.2    Mildvan, A.S.3
  • 56
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz, T. A. (1999) DNA polymerases: structural diversity and common mechanisms, J. Biol. Chem. 274, 17395-17398.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 57
    • 8744252619 scopus 로고    scopus 로고
    • Thermodynamics of aminoglycoside binding to aminoglycoside-3′- phosphotransferase IIIa studied by isothermal titration calorimetry
    • Ozen, C., and Serpersu, E. H. (2004) Thermodynamics of aminoglycoside binding to aminoglycoside-3′-phosphotransferase IIIa studied by isothermal titration calorimetry, Biochemistry 43, 14667-14675.
    • (2004) Biochemistry , vol.43 , pp. 14667-14675
    • Ozen, C.1    Serpersu, E.H.2
  • 58
    • 0024290407 scopus 로고
    • Determination of the rate-limiting segment of aminoglycoside nucleotidyltransferase 2″-1Iby pH and viscosity-dependent kinetics [erratum: (1989) Biochemistry 28 (4), 1930]
    • Gates, C. A., and Northrop, D. B. (1988) Determination of the rate-limiting segment of aminoglycoside nucleotidyltransferase 2″-1Iby pH and viscosity-dependent kinetics [erratum: (1989) Biochemistry 28 (4), 1930], Biochemistry 27, 3834-3842.
    • (1988) Biochemistry , vol.27 , pp. 3834-3842
    • Gates, C.A.1    Northrop, D.B.2
  • 59
    • 0003830516 scopus 로고
    • Misread protein creates membrane channels: An essential step in the bactericidal action of aminoglycosides
    • Davis, B. D., Chen, L. L., and Tai, P. C. (1986) Misread protein creates membrane channels: an essential step in the bactericidal action of aminoglycosides, Proc. Natl. Acad. Sci. U.S.A. 83, 6164-6168.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 6164-6168
    • Davis, B.D.1    Chen, L.L.2    Tai, P.C.3
  • 60
    • 0023615466 scopus 로고
    • Mechanism of bactericidal action of aminoglycosides [erratum: (1988) Microbiol. Rev. 52 (1), 153]
    • Davis, B. D. (1987) Mechanism of bactericidal action of aminoglycosides [erratum: (1988) Microbiol. Rev. 52 (1), 153], Microbiol. Rev. 51, 341-350.
    • (1987) Microbiol. Rev. , vol.51 , pp. 341-350
    • Davis, B.D.1
  • 61
    • 0021136644 scopus 로고
    • Correlation of antibiotic resistance with Vmax/Km ratio of enzymatic modification of aminoglycosides by kanamycin acetyltransferase
    • Radika, K., and Northrop, D. B. (1984) Correlation of antibiotic resistance with Vmax/Km ratio of enzymatic modification of aminoglycosides by kanamycin acetyltransferase, Antimicrob. Agents Chemother. 25, 479-482.
    • (1984) Antimicrob. Agents Chemother. , vol.25 , pp. 479-482
    • Radika, K.1    Northrop, D.B.2
  • 62
    • 0028882693 scopus 로고
    • Kinetic mechanism of aminoglycoside phosphotransferase type IIIa. Evidence for a Theorell-Chance mechanism
    • McKay, G. A., and Wright, G. D. (1995) Kinetic mechanism of aminoglycoside phosphotransferase type IIIa. Evidence for a Theorell-Chance mechanism, J. Biol. Chem. 270, 24686-24692.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24686-24692
    • McKay, G.A.1    Wright, G.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.