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Volumn 6, Issue 2, 1999, Pages 99-110

Prodigious substrate specificity of AAC(6')-APH(2''), an aminoglycoside antibiotic resistance determinant in enterococci and staphylococci

Author keywords

Aminoglycoside; Antibiotic resistance; Regiospecificity

Indexed keywords

BACILLUS SUBTILIS; ENTEROCOCCUS; POSIBACTERIA; STAPHYLOCOCCI; STAPHYLOCOCCUS;

EID: 0033080180     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)80006-4     Document Type: Article
Times cited : (99)

References (35)
  • 2
    • 0002881670 scopus 로고
    • Aminoglycoside-aminocyclitol antibiotics and their modifying enzymes
    • (Lorian, V. ed.), Williams & Wilkins, Baltimore
    • Davies, J.E. (1991). Aminoglycoside-aminocyclitol antibiotics and their modifying enzymes. In Antibiotics in Laboratory Medicine 3rd Ed, (Lorian, V. ed.), pp. 691-713, Williams & Wilkins, Baltimore.
    • (1991) Antibiotics in Laboratory Medicine 3rd Ed , pp. 691-713
    • Davies, J.E.1
  • 3
    • 0026760182 scopus 로고
    • The crisis in antibiotic resistance
    • Neu, H.C. (1992). The crisis in antibiotic resistance. Science 257, 1064-1073.
    • (1992) Science , vol.257 , pp. 1064-1073
    • Neu, H.C.1
  • 4
    • 23444440823 scopus 로고
    • Inactivation of antibiotics and the dissemination of resistance genes
    • Davies, J. (1994). Inactivation of antibiotics and the dissemination of resistance genes. Science 264, 375-382.
    • (1994) Science , vol.264 , pp. 375-382
    • Davies, J.1
  • 5
    • 0030792311 scopus 로고    scopus 로고
    • Bacterial resistance to aminoglycoside antibiotics
    • Davies, J. & Wright, G.D. (1997). Bacterial resistance to aminoglycoside antibiotics. Trends Microbiol. 5, 234-240.
    • (1997) Trends Microbiol. , vol.5 , pp. 234-240
    • Davies, J.1    Wright, G.D.2
  • 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. & 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
    • 0031021201 scopus 로고    scopus 로고
    • The most frequent aminoglycoside resistance mechanism-changes with time and geographic area: A reflection of aminoglycoside usage patterns?
    • Miller, G.H., et al. & Aminoglycoside Resistance Study Groups (1997). The most frequent aminoglycoside resistance mechanism-changes with time and geographic area: A reflection of aminoglycoside usage patterns? Clin. Infect. Dis. 24(suppl I), S46-S62.
    • (1997) Clin. Infect. Dis. , vol.24 , Issue.SUPPL. I
    • Miller, G.H.1
  • 8
    • 0015613283 scopus 로고
    • Penicillin-tobramycin synergism against enterococci: A comparison with penicillin and gentamicin
    • Moellering Jr., R.C., Wennersten, C.B. & Weinstein, A.J. (1973). Penicillin-tobramycin synergism against enterococci: A comparison with penicillin and gentamicin. Antimicrob. Agents Chemother. 3, 526-529.
    • (1973) Antimicrob. Agents Chemother. , vol.3 , pp. 526-529
    • Moellering R.C., Jr.1    Wennersten, C.B.2    Weinstein, A.J.3
  • 9
    • 0026671296 scopus 로고
    • Resistance of enterococci to aminoglycosides and glycopeptides
    • Leclerq, R., et al., & Courvalin, P. (1992). Resistance of enterococci to aminoglycosides and glycopeptides. Clin. Infect. Dis. 15, 495-501.
    • (1992) Clin. Infect. Dis. , vol.15 , pp. 495-501
    • Leclerq, R.1    Courvalin, P.2
  • 10
    • 0025299023 scopus 로고
    • High-level gentamicin resistance in Enterococcus: Microbiology, genetic basis, and epidemiology
    • Patterson, J.E. & Zervos, M.J. (1990). High-level gentamicin resistance in Enterococcus: Microbiology, genetic basis, and epidemiology. Rev. Infect. Diseases 12, 644-652.
    • (1990) Rev. Infect. Diseases , vol.12 , pp. 644-652
    • Patterson, J.E.1    Zervos, M.J.2
  • 11
    • 0025756145 scopus 로고
    • Characterization of the gentamicin resistance transposon Tn5281 from Enterococcus faecalis and comparison to staphylococcal transposons Tn4001 and Tn4031
    • Hodel-Christian, S.L. & Murray, B.E. (1991). Characterization of the gentamicin resistance transposon Tn5281 from Enterococcus faecalis and comparison to staphylococcal transposons Tn4001 and Tn4031. Antimicrob. Agents Chemother. 35, 1147-1152.
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 1147-1152
    • Hodel-Christian, S.L.1    Murray, B.E.2
  • 12
    • 0026728776 scopus 로고
    • Identical genes confer high-level resistance to gentamicin upon Enterococcus faecalis, Enterococccus faecium, and Streptococcus agalactiae
    • Kaufhold, A., Podbielski, A., Horaud, T. & Ferrieri, P. (1992). Identical genes confer high-level resistance to gentamicin upon Enterococcus faecalis, Enterococccus faecium, and Streptococcus agalactiae. Antimicrob. Agents Chemother. 36, 1215-1218.
    • (1992) Antimicrob. Agents Chemother. , vol.36 , pp. 1215-1218
    • Kaufhold, A.1    Podbielski, A.2    Horaud, T.3    Ferrieri, P.4
  • 13
    • 0027465810 scopus 로고
    • Molecular characterization of highly gentamicin-resistant Enterococcus faecalis isolates lacking high-level streptomycin reistance
    • Thal, L.A., et al., & Zervos, M.J. (1993). Molecular characterization of highly gentamicin-resistant Enterococcus faecalis isolates lacking high-level streptomycin reistance. Antimicrob. Agents Chemother. 37, 134-137.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 134-137
    • Thal, L.A.1    Zervos, M.J.2
  • 14
    • 0021368889 scopus 로고
    • Tn4001: A gentamicin and kanamycin resistance transposon in Staphylococccus aureus
    • Lyon, B.R., May, J.W. & Skurray, R.A. (1984). Tn4001: A gentamicin and kanamycin resistance transposon in Staphylococccus aureus. Mol. Gen. Genet. 193, 554-556.
    • (1984) Mol. Gen. Genet. , vol.193 , pp. 554-556
    • Lyon, B.R.1    May, J.W.2    Skurray, R.A.3
  • 15
    • 0024407008 scopus 로고
    • Mobility of gentamicin resistance genes from staphylococci isolated in the United States: Identification of Tn4031, a gentamicin resistance transposon from Staphylococcus epidermidis
    • Thomas Jr., W.D. & Archer, G.L. (1989). Mobility of gentamicin resistance genes from staphylococci isolated in the United States: Identification of Tn4031, a gentamicin resistance transposon from Staphylococcus epidermidis. Antimicrob. Agents Chemother. 33, 1335-1341.
    • (1989) Antimicrob. Agents Chemother. , vol.33 , pp. 1335-1341
    • Thomas W.D., Jr.1    Archer, G.L.2
  • 16
    • 0022451481 scopus 로고
    • Nucleotide sequence analysis of the gene specifying the bifunctional 6′-aminoglycoside 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. & Courvalin, P. (1986). Nucleotide sequence analysis of the gene specifying the bifunctional 6′-aminoglycoside 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
  • 17
    • 0023552975 scopus 로고
    • The aacA-aphD gentamicin and kanamycin resistance determinant of Tn4001 from Staphylococcus aureus: Expression and nucleotide sequence analysis
    • Rouch, D.A., Byrne, M.E., Kong, Y.C. & Skurray, R.A. (1987). The aacA-aphD gentamicin and kanamycin resistance determinant of Tn4001 from Staphylococcus aureus: Expression and nucleotide sequence analysis. J. Gen. Microbiol. 133, 3039-3052.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 3039-3052
    • Rouch, D.A.1    Byrne, M.E.2    Kong, Y.C.3    Skurray, R.A.4
  • 18
    • 0021271509 scopus 로고
    • Purification and characterization of aminoglycoside-modifying enzymes from Staphylococcus aureus and Staphylococcus epidermidis
    • Ubukata, K., Yamashita, N., Gotoh, A. & Konno, M. (1984). Purification and characterization of aminoglycoside-modifying enzymes from Staphylococcus aureus and Staphylococcus epidermidis. Antimicrob. Agents Chemother. 25, 754-759.
    • (1984) Antimicrob. Agents Chemother. , vol.25 , pp. 754-759
    • Ubukata, K.1    Yamashita, N.2    Gotoh, A.3    Konno, M.4
  • 19
    • 0020617947 scopus 로고
    • Kinetic studies of aminoglycoside acetyltransferase and phosphotransferase from Staphylococcus aureus RPAL
    • Martel, A., Masson, M., Moreau, N. & Goffic, F.L. (1983). Kinetic studies of aminoglycoside acetyltransferase and phosphotransferase from Staphylococcus aureus RPAL. Eur. J. Biochem. 133, 515-521.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 515-521
    • Martel, A.1    Masson, M.2    Moreau, N.3    Goffic, F.L.4
  • 20
    • 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. & 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
  • 21
    • 0026495787 scopus 로고
    • A series of shuttle vectors for Bacillus subtilis and Escherichia coli
    • Brückner, R. (1992). A series of shuttle vectors for Bacillus subtilis and Escherichia coli. Gene 122, 187-192.
    • (1992) Gene , vol.122 , pp. 187-192
    • Brückner, R.1
  • 22
    • 0030956595 scopus 로고    scopus 로고
    • Overexpression and characterization of the chromosomal aminoglycoside 6′-N-acetyltransferase from Enterococcus faecium
    • Wright, G.D. & Ladak, P. (1997). Overexpression and characterization of the chromosomal aminoglycoside 6′-N-acetyltransferase from Enterococcus faecium. Antimicrob. Agents Chemother. 41, 956-960.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 956-960
    • Wright, G.D.1    Ladak, P.2
  • 23
    • 0028358078 scopus 로고
    • Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: Overexpression, purification, and substrate specificity
    • McKay, G.A., Thompson, P.R. & 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
    • 0028805074 scopus 로고
    • Purification, characterization, and investigation of the mechanism of aminoglycoside 3′-phosphotransferase type la
    • Siregar, J.J., Miroshnikov, K. & Mobashery, S. (1995) Purification, characterization, and investigation of the mechanism of aminoglycoside 3′-phosphotransferase type la. Biochemistry 34, 12681-12688.
    • (1995) Biochemistry , vol.34 , pp. 12681-12688
    • Siregar, J.J.1    Miroshnikov, K.2    Mobashery, S.3
  • 25
    • 0030013605 scopus 로고    scopus 로고
    • Regiospecificity of aminoglycoside phosphotransferase from Enterococci and Staphylococci (APH(3′)-IIIa)
    • Thompson, P.R., Hughes, D.W. & Wright, G.D. (1996). Regiospecificity of aminoglycoside phosphotransferase from Enterococci and Staphylococci (APH(3′)-IIIa). Biochemistry 35, 8686-8695.
    • (1996) Biochemistry , vol.35 , pp. 8686-8695
    • Thompson, P.R.1    Hughes, D.W.2    Wright, G.D.3
  • 26
    • 0001263889 scopus 로고
    • Cross relaxation without TOCSY: Transferase rotating frame overhauser effect spectroscopy
    • Hwang, T.-L. & Shaka, A.J. (1992). Cross relaxation without TOCSY: Transferase rotating frame overhauser effect spectroscopy. J. Am. Chem. Soc. 114, 3157-3159.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3157-3159
    • Hwang, T.-L.1    Shaka, A.J.2
  • 27
    • 46149138072 scopus 로고
    • Transformation of homonuclear two-dimensional NMR techniques using gaussian pulses
    • Kessler, H., Oschkinat, H., Griesinger, C. & Bermel, W. (1986). Transformation of homonuclear two-dimensional NMR techniques using gaussian pulses. J. Magn. Reson. 70, 106-133.
    • (1986) J. Magn. Reson. , vol.70 , pp. 106-133
    • Kessler, H.1    Oschkinat, H.2    Griesinger, C.3    Bermel, W.4
  • 28
    • 84989085820 scopus 로고
    • Multi-dimensional NMR experiments using selective pulses
    • Kessler, H., Mronga, S. & Gremmecker, G. (1991). Multi-dimensional NMR experiments using selective pulses. Magn. Reson. Chem. 29, 527-557.
    • (1991) Magn. Reson. Chem. , vol.29 , pp. 527-557
    • Kessler, H.1    Gremmecker, G.2
  • 29
    • 0029825658 scopus 로고    scopus 로고
    • Structure of the a site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic
    • Fourmy, D., Recht, M.I., Blanchard, S.C. & Puglisi, J.D. (1996). Structure of the a site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic. Science 274, 1376-1371.
    • (1996) Science , vol.274 , pp. 1376-11371
    • Fourmy, D.1    Recht, M.I.2    Blanchard, S.C.3    Puglisi, J.D.4
  • 30
    • 0025774861 scopus 로고
    • Existence of two D-alanine-D-alanine ligases in Escherichia coli: Cloning and sequencing of the ddlA gene and purification and characterization of the DdlA and DdlB enzymes
    • Zawadzke, L.E., Bugg, T.D.H. & Walsh, C.T. (1991). Existence of two D-alanine-D-alanine ligases in Escherichia coli: Cloning and sequencing of the ddlA gene and purification and characterization of the DdlA and DdlB enzymes. Biochemistry 30, 1673-1682.
    • (1991) Biochemistry , vol.30 , pp. 1673-1682
    • Zawadzke, L.E.1    Bugg, T.D.H.2    Walsh, C.T.3
  • 31
    • 0001000071 scopus 로고
    • Optimum conditions for electric pulse-mediated gene transfer to Bacillus subtilis cells
    • Kusaoke, H., Hayashi, Y., Kadowaki, Y. & Kimoto, H. (1989). Optimum conditions for electric pulse-mediated gene transfer to Bacillus subtilis cells. Agric. Biol. Chem. 53, 2441-2446.
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2441-2446
    • Kusaoke, H.1    Hayashi, Y.2    Kadowaki, Y.3    Kimoto, H.4
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the protein-dye binding. Anal. Biochem. 34, 248-254.
    • (1976) Anal. Biochem. , vol.34 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0016410941 scopus 로고
    • Aminoglycoside-modifying enzymes
    • Haas, M.J. & Dowding, J.E. (1975). Aminoglycoside-modifying enzymes. Methods Enzymol. 43, 611-628.
    • (1975) Methods Enzymol. , vol.43 , pp. 611-628
    • Haas, M.J.1    Dowding, J.E.2
  • 35
    • 0018133513 scopus 로고
    • Kinetic mechanisms of gentamicin acetyltransferase I
    • Williams, J.W. & Northrop, D. (1978). Kinetic mechanisms of gentamicin acetyltransferase I. J. Biol. Chem. 253, 5902-5907.
    • (1978) J. Biol. Chem. , vol.253 , pp. 5902-5907
    • Williams, J.W.1    Northrop, D.2


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