메뉴 건너뛰기




Volumn 57, Issue 1, 2013, Pages 452-457

Novel aminoglycoside 2″-phosphotransferase identified in a gram- negative pathogen

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; AMIKACIN; AMINOGLYCOSIDE; AMINOGLYCOSIDE 2'' PHOSPHOTRANSFERASE; DIBEKACIN; GUANOSINE TRIPHOSPHATE; HABEKACIN; ISEPAMICIN; KANAMYCIN; NETILMICIN; PHOSPHOTRANSFERASE; SISOMICIN; TOBRAMYCIN; UNCLASSIFIED DRUG;

EID: 84872048832     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02049-12     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 0032226544 scopus 로고    scopus 로고
    • Aminoglycoside antibiotics. Structures, functions, and resistance
    • Wright GD, Berghuis AM, Mobashery S. 1998. Aminoglycoside antibiotics. Structures, functions, and resistance. Adv. Exp. Med. Biol. 456:27-69.
    • (1998) Adv. Exp. Med. Biol. , vol.456 , pp. 27-69
    • Wright, G.D.1    Berghuis, A.M.2    Mobashery, S.3
  • 2
    • 0036233697 scopus 로고    scopus 로고
    • 30S ribosomal subunit assembly is a target for inhibition by aminoglycosides in Escherichia coli
    • Mehta R, Champney WS. 2002. 30S ribosomal subunit assembly is a target for inhibition by aminoglycosides in Escherichia coli. Antimicrob. Agents Chemother. 46:1546 -1549.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1546-1549
    • Mehta, R.1    Champney, W.S.2
  • 3
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • Moazed D, Noller HF. 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
  • 5
    • 0037770202 scopus 로고    scopus 로고
    • Versatility of aminoglycosides and prospects for their future
    • Vakulenko SB, 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
  • 8
    • 79959609118 scopus 로고    scopus 로고
    • Current use of aminoglycosides: Indications, pharmacokinetics and monitoring for toxicity
    • Avent ML, Rogers BA, Cheng AC, Paterson DL. 2011. Current use of aminoglycosides: indications, pharmacokinetics and monitoring for toxicity. Intern. Med. J. 41:441- 449.
    • (2011) Intern. Med. J. , vol.41 , pp. 441-449
    • Avent, M.L.1    Rogers, B.A.2    Cheng, A.C.3    Paterson, D.L.4
  • 9
    • 0018405342 scopus 로고
    • Mechanism of aminoglycoside antibiotic resistance in anaerobic bacteria: Clostridium perfringens and Bacteroides fragilis
    • Bryan LE, Kowand SK, van den Elzen HM. 1979. Mechanism of aminoglycoside antibiotic resistance in anaerobic bacteria: Clostridium perfringens and Bacteroides fragilis. Antimicrob. Agents Chemother. 15:7-13.
    • (1979) Antimicrob. Agents Chemother. , vol.15 , pp. 7-13
    • Bryan, L.E.1    Kowand, S.K.2    Van Den Elzen, H.M.3
  • 10
    • 0025812422 scopus 로고
    • The Garrod Lecture. The enterococcus: A classic example of the impact of antimicrobial resistance on therapeutic options
    • Moellering RC, Jr. 1991. The Garrod Lecture. The enterococcus: a classic example of the impact of antimicrobial resistance on therapeutic options. J. Antimicrob. Chemother. 28:1-12.
    • (1991) J. Antimicrob. Chemother. , vol.28 , pp. 1-12
    • Moellering Jr., R.C.1
  • 11
    • 0345466364 scopus 로고    scopus 로고
    • Involvement of an active efflux system in the natural resistance of Pseudomonas aeruginosa to aminoglycosides
    • Aires JR, Kohler T, Nikaido H, Plesiat P. 1999. Involvement of an active efflux system in the natural resistance of Pseudomonas aeruginosa to aminoglycosides. Antimicrob. Agents Chemother. 43:2624 -2628.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 2624-2628
    • Aires, J.R.1    Kohler, T.2    Nikaido, H.3    Plesiat, P.4
  • 12
    • 0035178557 scopus 로고    scopus 로고
    • Resistance-nodulation-cell division-type efflux pump involved in aminoglycoside resistance in Acinetobacter baumannii strain BM4454
    • Magnet S, Courvalin P, Lambert T. 2001. Resistance-nodulation-cell division-type efflux pump involved in aminoglycoside resistance in Acinetobacter baumannii strain BM4454. Antimicrob. Agents Chemother. 45: 3375-3380.
    • (2001) Antimicrob. Agents Chemother. , vol.45 , pp. 3375-3380
    • Magnet, S.1    Courvalin, P.2    Lambert, T.3
  • 15
    • 0015424671 scopus 로고
    • Evidence for mutation to streptomycin resistance in clinical strains of Staphylococcus aureus
    • Lacey RW, Chopra I. 1972. Evidence for mutation to streptomycin resistance in clinical strains of Staphylococcus aureus. J. Gen. Microbiol. 73: 175-180.
    • (1972) J. Gen. Microbiol. , vol.73 , pp. 175-180
    • Lacey, R.W.1    Chopra, I.2
  • 16
    • 0016360794 scopus 로고
    • Ribosomal resistance to streptomycin and spectinomycin in Neisseria gonorrhoeae
    • Maness MJ, Foster GC, Sparling PF. 1974. Ribosomal resistance to streptomycin and spectinomycin in Neisseria gonorrhoeae. J. Bacteriol. 120:1293-1299.
    • (1974) J. Bacteriol. , vol.120 , pp. 1293-1299
    • Maness, M.J.1    Foster, G.C.2    Sparling, P.F.3
  • 17
    • 0023091436 scopus 로고
    • Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides
    • Beauclerk AA, Cundliffe E. 1987. Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides. J. Mol. Biol. 193:661- 671.
    • (1987) J. Mol. Biol. , vol.193 , pp. 661-671
    • Beauclerk, A.A.1    Cundliffe, E.2
  • 18
    • 43349087698 scopus 로고    scopus 로고
    • New plasmid-mediated resistances to antimicrobial agents
    • Courvalin P. 2008. New plasmid-mediated resistances to antimicrobial agents. Arch. Microbiol. 189:289 -291.
    • (2008) Arch. Microbiol. , vol.189 , pp. 289-291
    • Courvalin, P.1
  • 19
    • 34250839342 scopus 로고    scopus 로고
    • 16S ribosomal RNA methylation: Emerging resistance mechanism against aminoglycosides
    • Doi Y, Arakawa Y. 2007. 16S ribosomal RNA methylation: emerging resistance mechanism against aminoglycosides. Clin. Infect. Dis. 45: 88-94.
    • (2007) Clin. Infect. Dis. , vol.45 , pp. 88-94
    • Doi, Y.1    Arakawa, Y.2
  • 21
    • 0034458472 scopus 로고    scopus 로고
    • Aminoglycoside resistance in enterococci
    • Chow JW. 2000. Aminoglycoside resistance in enterococci. Clin. Infect. Dis. 31:586 -589.
    • (2000) Clin. Infect. Dis. , vol.31 , pp. 586-589
    • Chow, J.W.1
  • 23
    • 65449151891 scopus 로고    scopus 로고
    • Source of phosphate in the enzymic reaction as a point of distinction among aminoglycoside 2″-phosphotransferases
    • Toth M, Chow JW, Mobashery S, Vakulenko SB. 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
  • 24
    • 77955109419 scopus 로고    scopus 로고
    • Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase- 2″-IVa
    • Toth M, Frase H, Antunes NT, Smith CA, Vakulenko SB. 2010. Crystal structure and kinetic mechanism of aminoglycoside phosphotransferase- 2″-IVa. Protein Sci. 19:1565-1576.
    • (2010) Protein Sci. , vol.19 , pp. 1565-1576
    • Toth, M.1    Frase, H.2    Antunes, N.T.3    Smith, C.A.4    Vakulenko, S.B.5
  • 28
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constants
    • Dixon M. 1953. The determination of enzyme inhibitor constants. Biochem. J. 55:170 -171.
    • (1953) Biochem. J. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 30
    • 84859747165 scopus 로고    scopus 로고
    • Aminoglycoside 2″-phosphotransferase IIIa (APH(2″)-IIIa) prefers GTP over ATP: Structural templates for nucleotide recognition in the bacterial ami-noglycoside- 2″ kinases
    • Smith CA, Toth M, Frase H, Byrnes LJ, Vakulenko SB. 2012. Aminoglycoside 2″-phosphotransferase IIIa (APH(2″)-IIIa) prefers GTP over ATP: structural templates for nucleotide recognition in the bacterial ami-noglycoside- 2″ kinases. J. Biol. Chem. 287:12893-12903.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12893-12903
    • Smith, C.A.1    Toth, M.2    Frase, H.3    Byrnes, L.J.4    Vakulenko, S.B.5
  • 31
    • 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 PG, Walanj R, Lakshmi V, Byrnes LJ, Metcalf P, Baker EN, Vakulenko SB, Smith CA. 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
  • 32
    • 19544364887 scopus 로고    scopus 로고
    • Mosaic structure of a multiple-drug- Resistant, conjugative plasmid from Campylobacter jejuni
    • Nirdnoy W, Mason CJ, Guerry P. 2005. Mosaic structure of a multiple-drug- resistant, conjugative plasmid from Campylobacter jejuni. Antimicrob. Agents Chemother. 49:2454 -2459.
    • (2005) Antimicrob. Agents Chemother. , vol.49 , pp. 2454-2459
    • Nirdnoy, W.1    Mason, C.J.2    Guerry, P.3
  • 33
    • 0032892950 scopus 로고    scopus 로고
    • Semisynthetic aminoglycoside antibiotics: Development and enzymatic modifications
    • Kondo S, 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
  • 34
    • 0020617947 scopus 로고
    • Kinetic studies of aminoglycoside acetyltransferase and phosphotransferase from Staphylococcus aureus RPAL. Relationship between the two activities
    • Martel A, Masson M, Moreau N, 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
    • Martel, A.1    Masson, M.2    Moreau, N.3    Le Goffic, F.4
  • 35
    • 0033080180 scopus 로고    scopus 로고
    • Prodigious substrate specificity of AAC(6′)-APH(2″), an aminoglycoside antibiotic resistance determinant in enterococci and staphylococci
    • Daigle DM, Hughes DW, Wright GD. 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
  • 36
    • 33646365631 scopus 로고    scopus 로고
    • Hydrolysis of ATP by aminoglycoside 3′-phosphotransferases: An unexpected cost to bacteria for harboring an antibiotic resistance enzyme
    • Kim C, Cha JY, Yan H, Vakulenko SB, Mobashery S. 2006. Hydrolysis of ATP by aminoglycoside 3′-phosphotransferases: an unexpected cost to bacteria for harboring an antibiotic resistance enzyme. J. Biol. Chem. 281: 6964-6969.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6964-6969
    • Kim, C.1    Cha, J.Y.2    Yan, H.3    Vakulenko, S.B.4    Mobashery, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.