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Volumn 54, Issue 4, 2010, Pages 1590-1595

Mutant APH(2″)-IIa enzymes with increased activity against amikacin and isepamicin

Author keywords

[No Author keywords available]

Indexed keywords

AMIKACIN; AMINOGLYCOSIDE 2'' PHOSPHOTRANSFERASE IIA; DIBEKACIN; GENTAMICIN; ISEPAMICIN; KANAMYCIN; MUTANT PROTEIN; NETILMICIN; PHOSPHOTRANSFERASE; SISOMICIN; TOBRAMYCIN; UNCLASSIFIED DRUG;

EID: 77950108480     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.01444-09     Document Type: Article
Times cited : (13)

References (22)
  • 1
    • 55249117030 scopus 로고    scopus 로고
    • Emergence and management of drug-resistant enterococcal infections. Expert Rev. Anti Infect
    • Arias, C. A., and B. E. Murray. 2008. Emergence and management of drug-resistant enterococcal infections. Expert Rev. Anti Infect. Ther. 6:637-655.
    • (2008) Ther , vol.6 , pp. 637-655
    • Arias, C.A.1    Murray, B.E.2
  • 3
    • 38749142232 scopus 로고    scopus 로고
    • Characterization of nucleotide pools as a function of physiological state in Escherichia coli
    • Buckstein, M. H., J. He, and H. Rubin. 2008. Characterization of nucleotide pools as a function of physiological state in Escherichia coli. J. Bacteriol. 190:718-726.
    • (2008) J. Bacteriol , vol.190 , pp. 718-726
    • Buckstein, M.H.1    He, J.2    Rubin, H.3
  • 4
    • 0034458472 scopus 로고    scopus 로고
    • Aminoglycoside resistance in enterococci
    • Chow, J. W. 2000. Aminoglycoside resistance in enterococci. Clin. Infect. Dis. 31:586-589.
    • (2000) Clin. Infect. Dis , vol.31 , pp. 586-589
    • Chow, J.W.1
  • 5
    • 0034806930 scopus 로고    scopus 로고
    • Aminoglycoside resistance genes aph(2″)-Ib and aac(6′)-Im detected together in strains of both Escherichia coli and Enterococcus faecium
    • Chow, J. W., V. Kak, I. You, S. J. Kao, J. Petrin, D. B. Clewell, S. A. Lerner, G. H. Miller, and K. J. Shaw. 2001. Aminoglycoside resistance genes aph(2″)-Ib and aac(6′)-Im detected together in strains of both Escherichia coli and Enterococcus faecium. Antimicrob. Agents Chemother. 45:2691-2694.
    • (2001) Antimicrob. Agents Chemother , vol.45 , pp. 2691-2694
    • Chow, J.W.1    Kak, V.2    You, I.3    Kao, S.J.4    Petrin, J.5    Clewell, D.B.6    Lerner, S.A.7    Miller, G.H.8    Shaw, K.J.9
  • 7
    • 0003344510 scopus 로고    scopus 로고
    • Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically; approved standard
    • Clinical and Laboratory Standards Institute, 7th ed, Clinical and Laboratory Standards Institute, Wayne, PA
    • Clinical and Laboratory Standards Institute. 2006. Methods for dilution antimicrobial susceptibility tests for bacteria that grow aerobically; approved standard, 7th ed. Clinical and Laboratory Standards Institute document M7-A7. Clinical and Laboratory Standards Institute, Wayne, PA.
    • (2006) Clinical and Laboratory Standards Institute document
  • 9
    • 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., K. S. Gilmore, and P. Courvalin. 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
  • 12
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • Moazed, D., and H. F. Noller. 1987. Interaction of antibiotics with functional sites in 16S ribosomal RNA. Nature 327:389-394.
    • (1987) Nature , vol.327 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 13
    • 0036323327 scopus 로고    scopus 로고
    • Novel high-level constitutive expression system, pHCE vector, for a convenient and cost-effective soluble production of human tumor necrosis factor-alpha
    • Poo, H., J. J. Song, S. P. Hong, Y. H. Choi, S. W. Yun, J. H. Kim, S. C. Lee, S. G. Lee, and M. H. Sung. 2002. Novel high-level constitutive expression system, pHCE vector, for a convenient and cost-effective soluble production of human tumor necrosis factor-alpha. Biotechnol. Lett. 24:1185-1189.
    • (2002) Biotechnol. Lett , vol.24 , pp. 1185-1189
    • Poo, H.1    Song, J.J.2    Hong, S.P.3    Choi, Y.H.4    Yun, S.W.5    Kim, J.H.6    Lee, S.C.7    Lee, S.G.8    Sung, M.H.9
  • 14
    • 84964134387 scopus 로고
    • Streptomycin, a substance exhibiting antibiotic activity against gram positive and gram-negative bacteria
    • Schatz, A., E. Bugie, and S. A. Waksman. 1944. Streptomycin, a substance exhibiting antibiotic activity against gram positive and gram-negative bacteria. Proc. Soc. Exp. Biol. Med. 55:66-69.
    • (1944) Proc. Soc. Exp. Biol. Med , vol.55 , pp. 66-69
    • Schatz, A.1    Bugie, E.2    Waksman, S.A.3
  • 15
    • 0027478123 scopus 로고
    • Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes
    • Shaw, K. J., P. N. Rather, R. S. Hare, and G. H. Miller. 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
  • 16
    • 65449151891 scopus 로고    scopus 로고
    • Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2″-phosphotransferases
    • Toth, M., J. W. Chow, S. Mobashery, and S. B. Vakulenko. 2009. Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2″-phosphotransferases. J. Biol. Chem. 284:6690- 6696.
    • (2009) J. Biol. Chem , vol.284 , pp. 6690-6696
    • Toth, M.1    Chow, J.W.2    Mobashery, S.3    Vakulenko, S.B.4
  • 18
    • 0031970944 scopus 로고    scopus 로고
    • Tsai, S. F., M. J. Zervos, D. B. Clewell, S. M. Donabedian, D. F. Sahm, and J. W. Chow. 1998. A new high-level gentamicin resistance gene, aph(2″)-Id, in Enterococcus spp. Antimicrob. Agents Chemother. 42:1229-1232.
    • Tsai, S. F., M. J. Zervos, D. B. Clewell, S. M. Donabedian, D. F. Sahm, and J. W. Chow. 1998. A new high-level gentamicin resistance gene, aph(2″)-Id, in Enterococcus spp. Antimicrob. Agents Chemother. 42:1229-1232.
  • 19
    • 0037770202 scopus 로고    scopus 로고
    • Versatility of aminoglycosides and prospects for their future
    • Vakulenko, S. B., and S. Mobashery. 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
  • 20
    • 0025799785 scopus 로고
    • Interaction of antibiotics with A-site-specific and P-site-specific bases in 16S ribosomal-RNA
    • Woodcock, J., D. Moazed, M. Cannon, J. Davies, and H. F. Noller. 1991. Interaction of antibiotics with A-site-specific and P-site-specific bases in 16S ribosomal-RNA. EMBO J. 10:3099-3103.
    • (1991) EMBO J , vol.10 , pp. 3099-3103
    • Woodcock, J.1    Moazed, D.2    Cannon, M.3    Davies, J.4    Noller, H.F.5
  • 21
    • 0032226544 scopus 로고    scopus 로고
    • Aminoglycoside antibiotics. Structures, functions, and resistance. Adv. Exp. Med. Biol
    • Wright, G. D., A. M. Berghuis, and S. Mobashery. 1998. Aminoglycoside antibiotics. Structures, functions, and resistance. Adv. Exp. Med. Biol. 456: 27-69.
    • (1998) , vol.456 , pp. 27-69
    • Wright, G.D.1    Berghuis, A.M.2    Mobashery, S.3
  • 22
    • 67649413348 scopus 로고    scopus 로고
    • The crystal structures of substrate and nucleotide complexes of Enterococcus faecium aminoglycoside-2″-phosphotransferase-IIa [APH(2″)-IIa] provide insights into substrate selectivity in the APH(2″) subfamily
    • Young, P. G., R. Walanj, V. Lakshmi, L. J. Byrnes, P. Metcalf, E. N. Baker, S. B. Vakulenko, and C. A. Smith. 2009. The crystal structures of substrate and nucleotide complexes of Enterococcus faecium aminoglycoside-2″-phosphotransferase-IIa [APH(2″)-IIa] provide insights into substrate selectivity in the APH(2″) subfamily. J. Bacteriol. 191:4133-4143.
    • (2009) J. Bacteriol , vol.191 , pp. 4133-4143
    • Young, P.G.1    Walanj, R.2    Lakshmi, V.3    Byrnes, L.J.4    Metcalf, P.5    Baker, E.N.6    Vakulenko, S.B.7    Smith, C.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.