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Volumn 95, Issue 6, 2013, Pages 1319-1325

Domain dissection and characterization of the aminoglycoside resistance enzyme ANT(3″)-Ii/AAC(6′)-IId from Serratia marcescens

Author keywords

Acetyltransferase; Aminoglycoside antibiotics; Bacterial resistance; Bifunctional enzyme; Nucleotidyltransferase

Indexed keywords

ANT(3'') II AND AAC(6') IID; ENZYME; UNCLASSIFIED DRUG;

EID: 84877790567     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2013.02.011     Document Type: Article
Times cited : (11)

References (28)
  • 1
    • 33644547013 scopus 로고    scopus 로고
    • Molecular understanding of aminoglycoside action and resistance
    • S. Jana, and J.K. Deb Molecular understanding of aminoglycoside action and resistance Appl. Microbiol. Biotechnol. 70 2006 140 150
    • (2006) Appl. Microbiol. Biotechnol. , vol.70 , pp. 140-150
    • Jana, S.1    Deb, J.K.2
  • 4
    • 34548213103 scopus 로고    scopus 로고
    • A Common Mechanism of Cellular Death Induced by Bactericidal Antibiotics
    • DOI 10.1016/j.cell.2007.06.049, PII S0092867407008999
    • M.A. Kohanski, D.J. Dwyer, B. Hayete, C.A. Lawrence, and J.J. Collins A common mechanism of cellular death induced by bactericidal antibiotics Cell 130 2007 797 810 (Pubitemid 47332566)
    • (2007) Cell , vol.130 , Issue.5 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 5
    • 33745853833 scopus 로고    scopus 로고
    • Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3′)-Ii/AAC(6′)-IId from Serratia marcescens
    • DOI 10.1021/bi060723g
    • C. Kim, D. Hesek, J. Zajicek, S.B. Vakulenko, and S. Mobashery Characterization of the bifunctional aminoglycoside-modifying enzyme ANT(3′)-Ii/AAC(6′)-IId from Serratia marcescens Biochemistry 45 2006 8368 8377 (Pubitemid 44036543)
    • (2006) Biochemistry , vol.45 , Issue.27 , pp. 8368-8377
    • Kim, C.1    Hesek, D.2    Zajicek, J.3    Vakulenko, S.B.4    Mobashery, S.5
  • 6
    • 0036241539 scopus 로고    scopus 로고
    • Presence of a group II intron in a multiresistant Serratia marcescens strain that harbors three integrons and a novel gene fusion
    • DOI 10.1128/AAC.46.5.1402-1409.2002
    • D. Centron, and P.H. Roy Presence of a group II intron in a multiresistant Serratia marcescens strain that harbors three integrons and a novel gene fusion Antimicrob. Agents Chemother. 46 2002 1402 1409 (Pubitemid 34415321)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.5 , pp. 1402-1409
    • Centron, D.1    Roy, P.H.2
  • 7
    • 0033080180 scopus 로고    scopus 로고
    • Prodigious substrate specificity of AAC(6')-APH(2''), an aminoglycoside antibiotic resistance determinant in enterococci and staphylococci
    • DOI 10.1016/S1074-5521(99)80006-4
    • D.M. Daigle, D.W. Hughes, and G.D. Wright Prodigious substrate specificity of AAC(6′)-APH(2″), an aminoglycoside antibiotic resistance determinant in enterococci and staphylococci Chem. Biol. 6 1999 99 110 (Pubitemid 29363160)
    • (1999) Chemistry and Biology , vol.6 , Issue.2 , pp. 99-110
    • Daigle, D.M.1    Hughes, D.W.2    Wright, G.D.3
  • 8
    • 0032621936 scopus 로고    scopus 로고
    • Aminoglycoside resistance mediated by the bifunctional enzyme 6′-N-aminoglycoside acetyltransferase-2″-O-aminoglycoside phosphotransferase
    • E. Culebras, and J.L. Martinez Aminoglycoside resistance mediated by the bifunctional enzyme 6′-N-aminoglycoside acetyltransferase-2″-O- aminoglycoside phosphotransferase Front. Biosci. 4 1999 D1 D8
    • (1999) Front. Biosci. , vol.4
    • Culebras, E.1    Martinez, J.L.2
  • 9
    • 84871541597 scopus 로고    scopus 로고
    • Revisiting the nucleotide and aminoglycoside substrate specificity of the bifunctional aminoglycoside Acetyltransferase(6′)-ie/aminoglycoside Phosphotransferase(2″)-ia enzyme
    • H. Frase, M. Toth, and S.B. Vakulenko Revisiting the nucleotide and aminoglycoside substrate specificity of the bifunctional aminoglycoside Acetyltransferase(6′)-ie/aminoglycoside Phosphotransferase(2″)-ia enzyme J. Biol. Chem. 287 2012 43262 43269
    • (2012) J. Biol. Chem. , vol.287 , pp. 43262-43269
    • Frase, H.1    Toth, M.2    Vakulenko, S.B.3
  • 10
    • 34247577481 scopus 로고    scopus 로고
    • Mechanistic characterization of the bifunctional aminoglycoside-modifying enzyme AAC(3)-Ib/AAC(6′)-Ib′ from Pseudomonas aeruginosa
    • DOI 10.1021/bi700111z
    • C. Kim, A. Villegas-Estrada, D. Hesek, and S. Mobashery Mechanistic characterization of the bifunctional aminoglycoside-modifying enzyme AAC(3)-Ib/AAC(6′)-Ib′ from Pseudomonas aeruginosa Biochemistry 46 2007 5270 5282 (Pubitemid 46683023)
    • (2007) Biochemistry , vol.46 , Issue.17 , pp. 5270-5282
    • Kim, C.1    Villegas-Estrada, A.2    Hesek, D.3    Mobashery, S.4
  • 11
    • 0036167876 scopus 로고    scopus 로고
    • GES-1 and a fused product of aac(3)-Ib/aac(6′)-Ib′ gene cassettes in Pseudomonas aeruginosa
    • DOI 10.1128/AAC.46.3.638-645.2002
    • V. Dubois, L. Poirel, C. Marie, C. Arpin, P. Nordmann, and C. Quentin Molecular characterization of a novel class 1 integron containing bla(GES-1) and a fused product of aac3-Ib/aac6′-Ib′ gene cassettes in Pseudomonas aeruginosa Antimicrob. Agents Chemother. 46 2002 638 645 (Pubitemid 34157645)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.3 , pp. 638-645
    • Dubois, V.1    Poirel, L.2    Marie, C.3    Arpin, C.4    Nordmann, P.5    Quentin, C.6
  • 13
    • 9644302496 scopus 로고    scopus 로고
    • IMP-16, and a fused form of aminoglycoside-resistant gene aac(6′)-30/aac(6′)-Ib′: Report from the SENTRY Antimicrobial Surveillance Program
    • DOI 10.1128/AAC.48.12.4693-4702.2004
    • R.E. Mendes, M.A. Toleman, J. Ribeiro, H.S. Sader, R.N. Jones, and T.R. Walsh Integron carrying a novel metallo-beta-lactamase gene, blaIMP-16, and a fused form of aminoglycoside-resistant gene aac(6′)-30/aac(6′)- Ib′: report from the SENTRY Antimicrobial Surveillance Program Antimicrob. Agents Chemother. 48 2004 4693 4702 (Pubitemid 39577674)
    • (2004) Antimicrobial Agents and Chemotherapy , vol.48 , Issue.12 , pp. 4693-4702
    • Mendes, R.E.1    Toleman, M.A.2    Ribeiro, J.3    Sader, H.S.4    Jones, R.N.5    Walsh, T.R.6
  • 14
    • 79959277696 scopus 로고    scopus 로고
    • Effects of altering aminoglycoside structures on bacterial resistance enzyme activities
    • K.D. Green, W. Chen, and S. Garneau-Tsodikova Effects of altering aminoglycoside structures on bacterial resistance enzyme activities Antimicrob. Agents Chemother. 55 2011 3207 3213
    • (2011) Antimicrob. Agents Chemother. , vol.55 , pp. 3207-3213
    • Green, K.D.1    Chen, W.2    Garneau-Tsodikova, S.3
  • 15
    • 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
    • DOI 10.1021/ja964278w, PII S0002786396042783
    • E. Azucena, I. Grapsas, and S. Mobashery 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 1997 2317 2318 (Pubitemid 27160011)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.9 , pp. 2317-2318
    • Azucena, E.1    Grapsas, I.2    Mobashery, S.3
  • 17
    • 44349172245 scopus 로고    scopus 로고
    • Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase
    • DOI 10.1111/j.1742-4658.2008.06460.x
    • T. Biswas, and O.V. Tsodikov Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase Febs J. 275 2008 3064 3071 (Pubitemid 351743582)
    • (2008) FEBS Journal , vol.275 , Issue.12 , pp. 3064-3071
    • Biswas, T.1    Tsodikov, O.V.2
  • 18
    • 75649101296 scopus 로고    scopus 로고
    • Exploring the substrate promiscuity of drug-modifying enzymes for the chemoenzymatic generation of N-acylated aminoglycosides
    • K.D. Green, W.J. Chen, J.L. Houghton, M. Fridman, and S. Garneau-Tsodikova Exploring the substrate promiscuity of drug-modifying enzymes for the chemoenzymatic generation of N-acylated aminoglycosides ChemBioChem 11 2010 119 126
    • (2010) ChemBioChem , vol.11 , pp. 119-126
    • Green, K.D.1    Chen, W.J.2    Houghton, J.L.3    Fridman, M.4    Garneau-Tsodikova, S.5
  • 19
    • 59749101384 scopus 로고    scopus 로고
    • A nonradioactive high-throughput assay for screening and characterization of adenylation domains for nonribosomal peptide combinatorial biosynthesis
    • T.J. McQuade, A.D. Shallop, A. Sheoran, J.E. Delproposto, O.V. Tsodikov, and S. Garneau-Tsodikova A nonradioactive high-throughput assay for screening and characterization of adenylation domains for nonribosomal peptide combinatorial biosynthesis Anal. Biochem. 386 2009 244 250
    • (2009) Anal. Biochem. , vol.386 , pp. 244-250
    • McQuade, T.J.1    Shallop, A.D.2    Sheoran, A.3    Delproposto, J.E.4    Tsodikov, O.V.5    Garneau-Tsodikova, S.6
  • 20
    • 78649713996 scopus 로고    scopus 로고
    • Dissecting the cosubstrate structure requirements of the Staphylococcus aureus aminoglycoside resistance enzyme ANT(4 ′)
    • V.R. Porter, K.D. Green, O.E. Zolova, J.L. Houghton, and S. Garneau-Tsodikova Dissecting the cosubstrate structure requirements of the Staphylococcus aureus aminoglycoside resistance enzyme ANT(4 ′) Biochem. Biophys Res. Commun. 403 2010 85 90
    • (2010) Biochem. Biophys Res. Commun. , vol.403 , pp. 85-90
    • Porter, V.R.1    Green, K.D.2    Zolova, O.E.3    Houghton, J.L.4    Garneau-Tsodikova, S.5
  • 21
    • 3342941674 scopus 로고    scopus 로고
    • Domain-domain interactions in the aminoglycoside antibiotic resistance enzyme AAC(6′)-APH(2′)
    • DOI 10.1021/bi049135y
    • D.D. Boehr, D.M. Daigle, and G.D. Wright Domain-domain interactions in the aminoglycoside antibiotic resistance enzyme AAC(6′)-APH(2′) Biochemistry 43 2004 9846 9855 (Pubitemid 38993834)
    • (2004) Biochemistry , vol.43 , Issue.30 , pp. 9846-9855
    • Boehr, D.D.1    Daigle, D.M.2    Wright, G.D.3
  • 22
    • 84858690259 scopus 로고    scopus 로고
    • Small-angle X-ray scattering analysis of the bifunctional antibiotic resistance enzyme aminoglycoside (6′) acetyltransferase-ie/aminoglycoside (2′) phosphotransferase-ia reveals a rigid solution structure
    • S.J. Caldwell, and A.M. Berghuis Small-angle X-ray scattering analysis of the bifunctional antibiotic resistance enzyme aminoglycoside (6′) acetyltransferase-ie/aminoglycoside (2′) phosphotransferase-ia reveals a rigid solution structure Antimicrob. Agents Chemother. 56 2012 1899 1906
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 1899-1906
    • Caldwell, S.J.1    Berghuis, A.M.2
  • 23
    • 84868028203 scopus 로고    scopus 로고
    • Cosubstrate Tolerance of the aminoglycoside resistance enzyme Eis from Mycobacterium tuberculosis
    • W. Chen, K.D. Green, and S. Garneau-Tsodikova Cosubstrate Tolerance of the aminoglycoside resistance enzyme Eis from Mycobacterium tuberculosis Antimicrob. Agents Chemother. 56 2012 5831 5838
    • (2012) Antimicrob. Agents Chemother. , vol.56 , pp. 5831-5838
    • Chen, W.1    Green, K.D.2    Garneau-Tsodikova, S.3
  • 24
    • 0028865333 scopus 로고
    • Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase
    • L.C. Pedersen, M.M. Benning, and H.M. Holden Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase Biochemistry 34 1995 13305 13311
    • (1995) Biochemistry , vol.34 , pp. 13305-13311
    • Pedersen, L.C.1    Benning, M.M.2    Holden, H.M.3
  • 26
    • 0025603174 scopus 로고
    • Appearance of amikacin and tobramycin resistance due to 4′-aminoglycoside nucleotidyltransferase [ANT(4′)-II] in gram-negative pathogens
    • G.A. Jacoby, M.J. Blaser, P. Santanam, H. Hachler, F.H. Kayser, R.S. Hare, and G.H. Miller Appearance of amikacin and tobramycin resistance due to 4′-aminoglycoside nucleotidyltransferase [ANT(4′)-II] in gram-negative pathogens Antimicrob. Agents Chemother. 34 1990 2381 2386
    • (1990) Antimicrob. Agents Chemother. , vol.34 , pp. 2381-2386
    • Jacoby, G.A.1    Blaser, M.J.2    Santanam, P.3    Hachler, H.4    Kayser, F.H.5    Hare, R.S.6    Miller, G.H.7
  • 27
    • 48749103032 scopus 로고    scopus 로고
    • Enzyme structural plasticity and the emergence of broad-spectrum antibiotic resistance
    • F. Maurice, I. Broutin, I. Podglajen, P. Benas, E. Collatz, and F. Dardel Enzyme structural plasticity and the emergence of broad-spectrum antibiotic resistance EMBO Rep. 9 2008 344 349
    • (2008) EMBO Rep. , vol.9 , pp. 344-349
    • Maurice, F.1    Broutin, I.2    Podglajen, I.3    Benas, P.4    Collatz, E.5    Dardel, F.6
  • 28
    • 1942490112 scopus 로고    scopus 로고
    • A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones
    • DOI 10.1016/j.chembiol.2004.03.017, PII S1074552104000924
    • M.W. Vetting, S. Magnet, E. Nieves, S.L. Roderick, and J.S. Blanchard A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones Chem. Biol. 11 2004 565 573 (Pubitemid 38511761)
    • (2004) Chemistry and Biology , vol.11 , Issue.4 , pp. 565-573
    • Vetting, M.W.1    Magnet, S.2    Nieves, E.3    Roderick, S.L.4    Blanchard, J.S.5


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