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Volumn 46, Issue 18, 2007, Pages 5570-5578

Kinetic mechanism of enterococcal aminoglycoside phosphotransferase 2″-Ib

Author keywords

[No Author keywords available]

Indexed keywords

INHIBITION PATTERNS; SEQUENTIAL MECHANISM; SUBSTRATE BINDING;

EID: 34248147112     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi6024512     Document Type: Article
Times cited : (22)

References (43)
  • 1
    • 22544433208 scopus 로고    scopus 로고
    • Comparison of mortality associated with vancomycin-resistant and vancomycin-susceptible enterococcal bloodstream infections: A meta-analysis
    • DiazGranados, C. A., Zimmer, S. M., Klein, M., and Jernigan, J. A. (2005) Comparison of mortality associated with vancomycin-resistant and vancomycin-susceptible enterococcal bloodstream infections: a meta-analysis, Clin. Infect. Dis. 41, 327-333.
    • (2005) Clin. Infect. Dis , vol.41 , pp. 327-333
    • DiazGranados, C.A.1    Zimmer, S.M.2    Klein, M.3    Jernigan, J.A.4
  • 3
    • 0022451481 scopus 로고
    • Nucleotide sequence analysis of the gene specifying the bifunctional 6′- aminoglyeoside acetyltransferase 2″-aminoglycoside phosphotransferase enzyme in Streptococcus faecalis and identification and cloning of gene regions specifying the two activities
    • Ferretti, J. J., Gilmore, K. S., and Courvalin, P. (1986) Nucleotide sequence analysis of the gene specifying the bifunctional 6′- aminoglyeoside acetyltransferase 2″-aminoglycoside phosphotransferase enzyme in Streptococcus faecalis and identification and cloning of gene regions specifying the two activities, J. Bacteriol. 167, 631-638.
    • (1986) J. Bacteriol , vol.167 , pp. 631-638
    • Ferretti, J.J.1    Gilmore, K.S.2    Courvalin, P.3
  • 4
    • 0020617947 scopus 로고
    • Kinetic studies of aminoglycoside acetyltransferase and phosphotransferase from Staphylococcus aureus RPAL. Relationship between the two activities
    • Mattel, A., Masson, M., Moreau, N., and Le Goffic, F. (1983) Kinetic studies of aminoglycoside acetyltransferase and phosphotransferase from Staphylococcus aureus RPAL. Relationship between the two activities, Eur. J. Biochem. 133, 515-521.
    • (1983) Eur. J. Biochem , vol.133 , pp. 515-521
    • Mattel, A.1    Masson, M.2    Moreau, N.3    Le Goffic, F.4
  • 5
    • 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
    • 0030888830 scopus 로고    scopus 로고
    • Properties of a bifunctional bacterial antibiotic resistance enzyme that catalyzes ATP-dependent 2″-phosphorylation and acetyl-CoA-dependent 6′-acetylation of aminoglycosides
    • Azucena, E., Grapsas, I., and Mobashery, S. (1997) Properties of a bifunctional bacterial antibiotic resistance enzyme that catalyzes ATP-dependent 2″-phosphorylation and acetyl-CoA-dependent 6′-acetylation of aminoglycosides, J. Am. Chem. Soc. 119, 2317-2318.
    • (1997) J. Am. Chem. Soc , vol.119 , pp. 2317-2318
    • Azucena, E.1    Grapsas, I.2    Mobashery, S.3
  • 8
    • 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
  • 9
    • 0031970944 scopus 로고    scopus 로고
    • Tsai, S. F., Zervos, M. J., Clewell, D. B., Donabedian, S. M., Sahm, D. F., and Chow, J. W. (1998) A new high-level gentamicin resistance gene, aph(2″)-Id, in Enterococcus spp, Antimicrob. Agents Chemother. 42, 1229-1232.
    • Tsai, S. F., Zervos, M. J., Clewell, D. B., Donabedian, S. M., Sahm, D. F., and Chow, J. W. (1998) A new high-level gentamicin resistance gene, aph(2″)-Id, in Enterococcus spp, Antimicrob. Agents Chemother. 42, 1229-1232.
  • 12
    • 1542267777 scopus 로고    scopus 로고
    • Fluorinated aminoglycosides and their mechanistic implication for aminoglycoside 3′-phosphotransferases from Gram-negative bacteria
    • Kim, C., Haddad, J., Vakulenko, S. B., Meroueh, S. O., Wu, Y., Yan, H., and Mobashery, S. (2004) Fluorinated aminoglycosides and their mechanistic implication for aminoglycoside 3′-phosphotransferases from Gram-negative bacteria, Biochemistry 43, 2373-2383.
    • (2004) Biochemistry , vol.43 , pp. 2373-2383
    • Kim, C.1    Haddad, J.2    Vakulenko, S.B.3    Meroueh, S.O.4    Wu, Y.5    Yan, H.6    Mobashery, S.7
  • 14
    • 33644757144 scopus 로고
    • Correlation of proton and N-15 chemical-shifts by multiple quantum NMR
    • Bax, A., Griffey, R. H., and Hawkins, B. L. (1983) Correlation of proton and N-15 chemical-shifts by multiple quantum NMR, J. Magn. Reson. 55, 301-315.
    • (1983) J. Magn. Reson , vol.55 , pp. 301-315
    • Bax, A.1    Griffey, R.H.2    Hawkins, B.L.3
  • 15
    • 49149138654 scopus 로고
    • An improved method for heteronuclear chemical-shift correlation by two-dimensional NMR
    • Bax, A., and Morris, G. A. (1981) An improved method for heteronuclear chemical-shift correlation by two-dimensional NMR, J. Magn. Reson. 42, 501-505.
    • (1981) J. Magn. Reson , vol.42 , pp. 501-505
    • Bax, A.1    Morris, G.A.2
  • 16
    • 0345311216 scopus 로고
    • H-1 and C-13 assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR
    • Bax, A., and Summers, M. F. (1986) H-1 and C-13 assignments from sensitivity-enhanced detection of heteronuclear multiple-bond connectivity by 2D multiple quantum NMR, J. Am. Chem. Soc. 108, 2093-2094.
    • (1986) J. Am. Chem. Soc , vol.108 , pp. 2093-2094
    • Bax, A.1    Summers, M.F.2
  • 17
    • 0024282849 scopus 로고
    • Clean TOCSY for H-1 spin system-identification in macromolecules
    • Griesinger, C., Otting, G., Wuthrich, K., and Ernst, R. R. (1988) Clean TOCSY for H-1 spin system-identification in macromolecules, J. Am. Chem. Soc. 110, 7870-7872.
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 7870-7872
    • Griesinger, C.1    Otting, G.2    Wuthrich, K.3    Ernst, R.R.4
  • 18
    • 0001576285 scopus 로고
    • A 3-dimensional heteronuclear multiple-quantum coherence homonuclear Hartmann-Hahn experiment
    • Wijmenga, S. S., Hallenga, K., and Hilbers, C. W. (1989) A 3-dimensional heteronuclear multiple-quantum coherence homonuclear Hartmann-Hahn experiment, J. Magn. Reson. 84, 634-642.
    • (1989) J. Magn. Reson , vol.84 , pp. 634-642
    • Wijmenga, S.S.1    Hallenga, K.2    Hilbers, C.W.3
  • 20
    • 0003965863 scopus 로고    scopus 로고
    • 85th ed, Section 8, pp, CRC Press, Boca Raton, FL
    • Lide, D. R. (2004) Handbook of chemistry and physics, 85th ed., Section 8, pp 58-84, CRC Press, Boca Raton, FL.
    • (2004) Handbook of chemistry and physics , pp. 58-84
    • Lide, D.R.1
  • 21
    • 33745812244 scopus 로고    scopus 로고
    • Enzyme activity: Reversible inhibition
    • Morrison, J. F. (2001) Enzyme activity: Reversible inhibition, Encycl. Life Sci. 1-8.
    • (2001) Encycl. Life Sci , pp. 1-8
    • Morrison, J.F.1
  • 22
    • 0002244138 scopus 로고
    • Characterization of 4 Lactose Monophosphates by Application of P-31-NMR, C-13-NMR, and H-1-NMR Spectroscopy
    • Breg, J., Romijn, D., Vanhalbeek, H., Vliegenthart, J. F. G., Visser, R. A., and Haasnoot, C. A. G. (1988) Characterization of 4 Lactose Monophosphates by Application of P-31-NMR, C-13-NMR, and H-1-NMR Spectroscopy, Carbohydr. Res. 174, 23-36.
    • (1988) Carbohydr. Res , vol.174 , pp. 23-36
    • Breg, J.1    Romijn, D.2    Vanhalbeek, H.3    Vliegenthart, J.F.G.4    Visser, R.A.5    Haasnoot, C.A.G.6
  • 23
    • 0021436726 scopus 로고
    • Nucleic-Acid Constituents. 36. C-13 NMR in Conformational-Analysis of Nucleic-Acid Fragments. 2. A Reparametrization of the Karplus Equation for Vicinal NMR Coupling-Constants in CCOP and HCOP Fragments
    • Lankhorst, P. P., Haasnoot, C. A. G., Erkelens, C., and Altona, C. (1984) Nucleic-Acid Constituents. 36. C-13 NMR in Conformational-Analysis of Nucleic-Acid Fragments. 2. A Reparametrization of the Karplus Equation for Vicinal NMR Coupling-Constants in CCOP and HCOP Fragments, J. Biomol. Struct. Dyn. 1, 1387-1405.
    • (1984) J. Biomol. Struct. Dyn , vol.1 , pp. 1387-1405
    • Lankhorst, P.P.1    Haasnoot, C.A.G.2    Erkelens, C.3    Altona, C.4
  • 24
    • 0027530890 scopus 로고
    • Structures of enzymatically-modified products of arbekacin by methicillin-resistant Staphylococcus aureus
    • Kondo, S., Tamura, A., Gomi, S., Ikeda, Y., Takeuchi, T., and Mitsuhashi, S. (1993) Structures of enzymatically-modified products of arbekacin by methicillin-resistant Staphylococcus aureus, J. Antibiot. 46, 310-315.
    • (1993) J. Antibiot , vol.46 , pp. 310-315
    • Kondo, S.1    Tamura, A.2    Gomi, S.3    Ikeda, Y.4    Takeuchi, T.5    Mitsuhashi, S.6
  • 25
    • 0028003930 scopus 로고
    • Active-site labeling of an aminoglycoside antibiotic phosphotransferase (APH(3′)-IIIa)
    • Mckay, G. A., Robinson, R. A., Lane, W. S., and Wright, G. D. (1994) Active-site labeling of an aminoglycoside antibiotic phosphotransferase (APH(3′)-IIIa), Biochemistry 33, 14115-14120.
    • (1994) Biochemistry , vol.33 , pp. 14115-14120
    • Mckay, G.A.1    Robinson, R.A.2    Lane, W.S.3    Wright, G.D.4
  • 26
    • 0030250627 scopus 로고    scopus 로고
    • Mechanism of aminoglycoside 3′-phosphotransferase type IIIa: His188 is not a phosphate-accepting residue
    • Thompson, P. R., Hughes, D. W., and Wright, G. D. (1996) Mechanism of aminoglycoside 3′-phosphotransferase type IIIa: His188 is not a phosphate-accepting residue, Chem. Biol. 3, 747-755.
    • (1996) Chem. Biol , vol.3 , pp. 747-755
    • Thompson, P.R.1    Hughes, D.W.2    Wright, G.D.3
  • 27
    • 0020440235 scopus 로고
    • Regression-Analysis, Experimental Error, and Statistical Criteria in the Design and Analysis of Experiments for Discrimination between Rival Kinetic-Models
    • Mannervik, B. (1982) Regression-Analysis, Experimental Error, and Statistical Criteria in the Design and Analysis of Experiments for Discrimination between Rival Kinetic-Models, Methods Enzymol. 87, 370-390.
    • (1982) Methods Enzymol , vol.87 , pp. 370-390
    • Mannervik, B.1
  • 28
    • 21144432894 scopus 로고    scopus 로고
    • Kinetic mechanism of streptomycin adenylyltransferase from a recombinant Escherichia coli
    • Jana, S., and Deb, J. K. (2005) Kinetic mechanism of streptomycin adenylyltransferase from a recombinant Escherichia coli, Biotechnol. Lett. 27, 519-524.
    • (2005) Biotechnol. Lett , vol.27 , pp. 519-524
    • Jana, S.1    Deb, J.K.2
  • 29
    • 33745853833 scopus 로고    scopus 로고
    • Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3″)-Ii/AAC(6′)-IId from Serratia marcescens
    • Kim, C., Hesek, D., Zajicek, J., Vakulenko, S. B., and Mobashery, S. (2006) Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3″)-Ii/AAC(6′)-IId from Serratia marcescens, Biochemistry 45, 8368-8377.
    • (2006) Biochemistry , vol.45 , pp. 8368-8377
    • Kim, C.1    Hesek, D.2    Zajicek, J.3    Vakulenko, S.B.4    Mobashery, S.5
  • 30
    • 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
  • 31
    • 0038728733 scopus 로고    scopus 로고
    • Kinetic mechanism of the GCN5-related chromosomal aminoglycoside acetyltransferase AAC(6′)-Ii from Enterococcus faecium: Evidence of dimer subunit cooperativity
    • Draker, K. A., Northrop, D. B., and Wright, G. D. (2003) Kinetic mechanism of the GCN5-related chromosomal aminoglycoside acetyltransferase AAC(6′)-Ii from Enterococcus faecium: evidence of dimer subunit cooperativity, Biochemistry 42, 6565-6574.
    • (2003) Biochemistry , vol.42 , pp. 6565-6574
    • Draker, K.A.1    Northrop, D.B.2    Wright, G.D.3
  • 32
    • 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
  • 33
    • 0028805074 scopus 로고
    • Purification, characterization, and investigation of the mechanism of aminoglycoside 3′-phosphotransferase type Ia
    • Siregar, J. J., Miroshnikov, K., and Mobashery, S. (1995) Purification, characterization, and investigation of the mechanism of aminoglycoside 3′-phosphotransferase type Ia, Biochemistry 34, 12681-12688.
    • (1995) Biochemistry , vol.34 , pp. 12681-12688
    • Siregar, J.J.1    Miroshnikov, K.2    Mobashery, S.3
  • 34
    • 0035957254 scopus 로고    scopus 로고
    • Kinetic and mutagenic characterization of the chromosomally encoded Salmonella enterica AAC(6′)-Iy aminoglycoside N-acetyltransferase
    • Magnet, S., Lambert, T., Courvalin, P., and Blanchard, J. S. (2001) Kinetic and mutagenic characterization of the chromosomally encoded Salmonella enterica AAC(6′)-Iy aminoglycoside N-acetyltransferase, Biochemistry 40, 3700-3709.
    • (2001) Biochemistry , vol.40 , pp. 3700-3709
    • Magnet, S.1    Lambert, T.2    Courvalin, P.3    Blanchard, J.S.4
  • 35
    • 0018727624 scopus 로고
    • Use of competitive inhibitors to study substrate binding order
    • Fromm, H. J. (1979) Use of competitive inhibitors to study substrate binding order, Methods Enzymol. 63, 467-486.
    • (1979) Methods Enzymol , vol.63 , pp. 467-486
    • Fromm, H.J.1
  • 36
    • 0018727622 scopus 로고
    • Product inhibition and abortive complex formation
    • Rudolph, F. B. (1979) Product inhibition and abortive complex formation, Methods Enzymol. 63, 411-436.
    • (1979) Methods Enzymol , vol.63 , pp. 411-436
    • Rudolph, F.B.1
  • 37
    • 0024295023 scopus 로고
    • Triosephosphate Isomerase Catalysis Is Diffusion Controlled - Appendix - Analysis of Triose Phosphate Equilibria in Aqueous-Solution by P-31 NMR
    • Blacklow, S. C., Raines, R. T., Lim, W. A., Zamore, P. D., and Knowles, J. R. (1988) Triosephosphate Isomerase Catalysis Is Diffusion Controlled - Appendix - Analysis of Triose Phosphate Equilibria in Aqueous-Solution by P-31 NMR, Biochemistry 27, 1158-1167.
    • (1988) Biochemistry , vol.27 , pp. 1158-1167
    • Blacklow, S.C.1    Raines, R.T.2    Lim, W.A.3    Zamore, P.D.4    Knowles, J.R.5
  • 38
    • 0021403736 scopus 로고
    • Diffusion-Limited Component of Reactions Catalyzed by Bacillus-Cereus Beta-Lactamase-I
    • Hardy, L. W., and Kirsch, J. F. (1984) Diffusion-Limited Component of Reactions Catalyzed by Bacillus-Cereus Beta-Lactamase-I, Biochemistry 23, 1275-1282.
    • (1984) Biochemistry , vol.23 , pp. 1275-1282
    • Hardy, L.W.1    Kirsch, J.F.2
  • 39
    • 0020484823 scopus 로고
    • Investigation of Diffusion-Limited Rates of Chymotrypsin Reactions by Viscosity Variation
    • Brouwer, A. C., and Kirsch, J. F. (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
  • 41
    • 0028927517 scopus 로고
    • High-level resistance to aminoglycosides - Comparison of community and nosocomial fecal isolates of enterococci
    • Coque, T. M., Arduino, R. C., and Murray, B. E. (1995) High-level resistance to aminoglycosides - Comparison of community and nosocomial fecal isolates of enterococci, Clin. Infect. Dis. 20, 1048-1051.
    • (1995) Clin. Infect. Dis , vol.20 , pp. 1048-1051
    • Coque, T.M.1    Arduino, R.C.2    Murray, B.E.3
  • 42
    • 0037770202 scopus 로고    scopus 로고
    • Versatility of aminoglycosides and prospects for their future
    • Vakulenko, S. B., and Mobashery, S. (2003) Versatility of aminoglycosides and prospects for their future, Clin. Microbiol. Rev. 16, 430-450.
    • (2003) Clin. Microbiol. Rev , vol.16 , pp. 430-450
    • Vakulenko, S.B.1    Mobashery, S.2
  • 43
    • 0029941909 scopus 로고    scopus 로고
    • Catalytic mechanism of enterococcal kanamycin kinase (APH(3′)-IIIa): Viscosity, thio, and solvent isotope effects support a Theorell-Chance mechanism
    • McKay, G. A., and Wright, G. D. (1996) Catalytic mechanism of enterococcal 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


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