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Volumn 6, Issue 12, 2011, Pages 1415-1427

Providing β-lactams a helping hand: Targeting the AmpC β-lactamase induction pathway

Author keywords

lactam; lactamase; AmpC; AmpG; AmpR; Antibiotic resistance; Cystic fibrosis; FtsZ; NagZ; Pseudomonas aeruginosa

Indexed keywords

AVIBACTAM; AZTREONAM; BACTERIAL PROTEIN; BAL 30376; BETA LACTAM ANTIBIOTIC; BETA LACTAMASE; BETA LACTAMASE AMPC; BETA LACTAMASE INHIBITOR; CARBAPENEM DERIVATIVE; CEFEPIME; CEFOXITIN; CEFTAZIDIME; CEFTOLOZANE; CEPHALOSPORIN DERIVATIVE; CEPHEM; CLAVULANIC ACID; FTSZ PROTEIN; GLYCOSIDASE INHIBITOR; MONOBACTAM; N ACETYL BETA GLUCOSAMINIDASE; N ACETYLGLUCOSAMINE; O (2 ACETAMIDO 2 DEOXY DEXTRO GLUCOPYRANOSYLIDENE)AMINO N PHENYLCARBAMATE; PIPERACILLIN; PROTEIN AMPG; PROTEIN AMPR; PROTEIN NAGZ; SULBACTAM; TAZOBACTAM; UNCLASSIFIED DRUG; URIDINE DIPHOSPHATE N ACETYLMURAMIC ACID;

EID: 82455192469     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/fmb.11.128     Document Type: Article
Times cited : (53)

References (90)
  • 1
    • 14844362964 scopus 로고    scopus 로고
    • Bacterial resistance to beta lactam antibiotics: Compelling opportunism compelling opportunity
    • Fisher JF, Meroueh SO, Mobashery S. Bacterial resistance to beta lactam antibiotics: compelling opportunism, compelling opportunity. Chem. Rev. 105(2), 395-424 (2005).
    • (2005) Chem. Rev. , vol.105 , Issue.2 , pp. 395-424
    • Fisher, J.F.1    Meroueh, S.O.2    Mobashery, S.3
  • 2
    • 70349739265 scopus 로고    scopus 로고
    • The clinical consequences of antimicrobial resistance
    • Rice LB. The clinical consequences of antimicrobial resistance. Curr. Opin. Microbiol. 12(5), 476-481 (2009).
    • (2009) Curr. Opin. Microbiol. , vol.12 , Issue.5 , pp. 476-481
    • Rice, L.B.1
  • 3
    • 77149165713 scopus 로고    scopus 로고
    • Updated functional classification of beta lactamases
    • Bush K, Jacoby GA. Updated functional classification of {beta} lactamases. Antimicrob. Agents Chemother. 54(3), 969-976 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.3 , pp. 969-976
    • Bush, K.1    Jacoby, G.A.2
  • 5
    • 0000908299 scopus 로고
    • AmpC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta lactamases of the penicillinase type
    • Jaurin B, Grundström T. AmpC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta lactamases of the penicillinase type. Proc. Natl Acad. Sci. 78(8), 4897-4901 (1981).
    • (1981) Proc. Natl Acad. Sci. , vol.78 , Issue.8 , pp. 4897-4901
    • Jaurin, B.1    Grundström, T.2
  • 6
    • 59649115459 scopus 로고    scopus 로고
    • AmpC beta lactamases
    • Jacoby GA. AmpC beta lactamases. Clin. Microbiol. Rev. 22(1), 161-182 (2009).
    • (2009) Clin. Microbiol. Rev. , vol.22 , Issue.1 , pp. 161-182
    • Jacoby, G.A.1
  • 7
    • 70449124604 scopus 로고    scopus 로고
    • Antibacterial-resistant Pseudomonas aeruginosa: Clinical impact and complex regulation of chromosomally encoded resistance mechanisms
    • Lister PD, Wolter DJ, Hanson ND. Antibacterial-resistant Pseudomonas aeruginosa: clinical impact and complex regulation of chromosomally encoded resistance mechanisms. Clin. Microbiol. Rev. 22(4), 582-610 (2009).
    • (2009) Clin. Microbiol. Rev. , vol.22 , Issue.4 , pp. 582-610
    • Lister, P.D.1    Wolter, D.J.2    Hanson, N.D.3
  • 8
    • 0036225688 scopus 로고    scopus 로고
    • Lung infections associated with cystic fibrosis
    • Lyczak JB, Cannon CL, Pier GB. Lung infections associated with cystic fibrosis. Clin. Microbiol. Rev. 15(2), 194-222 (2002).
    • (2002) Clin. Microbiol. Rev. , vol.15 , Issue.2 , pp. 194-222
    • Lyczak, J.B.1    Cannon, C.L.2    Pier, G.B.3
  • 9
    • 0142043977 scopus 로고    scopus 로고
    • Pathophysiology and management of pulmonary infections in cystic fibrosis
    • Gibson RL, Burns JL, Ramsey BW. Pathophysiology and management of pulmonary infections in cystic fibrosis. Am. J. Respir. Crit. Care Med. 168(8), 918-951 (2003).
    • (2003) Am. J. Respir. Crit. Care Med. , vol.168 , Issue.8 , pp. 918-951
    • Gibson, R.L.1    Burns, J.L.2    Ramsey, B.W.3
  • 11
    • 77951060664 scopus 로고    scopus 로고
    • Current challenges in antimicrobial chemotherapy: Focus on β lactamase inhibition
    • Bebrone C, Lassaux P, Vercheval L et al. Current challenges in antimicrobial chemotherapy: focus on β lactamase inhibition. Drugs 70(6), 651-679 (2010).
    • (2010) Drugs , vol.70 , Issue.6 , pp. 651-679
    • Bebrone, C.1    Lassaux, P.2    Vercheval, L.3
  • 13
    • 0032920406 scopus 로고    scopus 로고
    • Clavulanate induces expression of the Pseudomonas aeruginosa AmpC cephalosporinase at physiologically relevant concentrations and antagonizes the antibacterial activity of ticarcillin
    • Lister PD, Gardner VM, Sanders CC. Clavulanate induces expression of the Pseudomonas aeruginosa AmpC cephalosporinase at physiologically relevant concentrations and antagonizes the antibacterial activity of ticarcillin. J. Antimicrob. Chemother. 43(4), 882-889 (1999).
    • (1999) J. Antimicrob. Chemother. , vol.43 , Issue.4 , pp. 882-889
    • Lister, P.D.1    Gardner, V.M.2    Sanders, C.C.3
  • 14
    • 74249108028 scopus 로고    scopus 로고
    • Three decades of beta lactamase inhibitors
    • Drawz SM, Bonomo RA. Three decades of beta lactamase inhibitors. Clin. Microbiol. Rev. 23(1), 160-201 (2010).
    • (2010) Clin. Microbiol. Rev. , vol.23 , Issue.1 , pp. 160-201
    • Drawz, S.M.1    Bonomo, R.A.2
  • 15
    • 0345102428 scopus 로고    scopus 로고
    • The complexed structure and antimicrobial activity of a non-β lactam inhibitor of AmpC β lactamase
    • Powers RA, Blázquez J, Weston GS, Shoichet BK, Morosini M-I, Baquero F. The complexed structure and antimicrobial activity of a non-β lactam inhibitor of AmpC β lactamase. Protein Sci. 8(11), 2330-2337 (1999).
    • (1999) Protein Sci. , vol.8 , Issue.11 , pp. 2330-2337
    • Powers, R.A.1    Blázquez, J.2    Weston, G.S.3    Shoichet, B.K.4    Morosini, M.-I.5    Baquero, F.6
  • 16
    • 4444347175 scopus 로고    scopus 로고
    • In vitro activity of AVE1330A an innovative broad-spectrum non-β lactam β lactamase inhibitor
    • Bonnefoy A, Dupuis-Hamelin C, Steier VR et al. In vitro activity of AVE1330A, an innovative broad-spectrum non-β lactam β lactamase inhibitor. J. Antimicrob. Chemother. 54(2), 410-417 (2004).
    • (2004) J. Antimicrob. Chemother. , vol.54 , Issue.2 , pp. 410-417
    • Bonnefoy, A.1    Dupuis-Hamelin, C.2    Steier, V.R.3
  • 17
    • 77957867755 scopus 로고    scopus 로고
    • Activity of BAL30376 monobactam BAL19764 + BAL29880 + clavulanate versus Gram-negative bacteria with characterized resistance mechanisms
    • Livermore DM, Mushtaq S, Warner M. Activity of BAL30376 (monobactam BAL19764 + BAL29880 + clavulanate) versus Gram-negative bacteria with characterized resistance mechanisms. J. Antimicrob. Chemother. 65(11), 2382-2395 (2010).
    • (2010) J. Antimicrob. Chemother. , vol.65 , Issue.11 , pp. 2382-2395
    • Livermore, D.M.1    Mushtaq, S.2    Warner, M.3
  • 19
    • 77149179342 scopus 로고    scopus 로고
    • Activity of a new cephalosporin CXA-101 FR264205 against β lactam-resistant Pseudomonas aeruginosa mutants selected in vitro and after antipseudomonal treatment of intensive care unit patients
    • Moya B, Zamorano L, Juan C, Perez JL, Ge Y, Oliver A. Activity of a new cephalosporin, CXA-101 (FR264205), against β lactam-resistant Pseudomonas aeruginosa mutants selected in vitro and after antipseudomonal treatment of intensive care unit patients. Antimicrob. Agents Chemother. 54(3), 1213-1217 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.3 , pp. 1213-1217
    • Moya, B.1    Zamorano, L.2    Juan, C.3    Perez, J.L.4    Ge, Y.5    Oliver, A.6
  • 20
    • 44949258242 scopus 로고    scopus 로고
    • How bacteria consume their own exoskeletons turnover and recycling of cell wall peptidoglycan
    • Park JT, Uehara T. How bacteria consume their own exoskeletons (turnover and recycling of cell wall peptidoglycan). Microbiol. Mol. Biol. Rev. 72(2), 211-227, (2008).
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , Issue.2 , pp. 211-227
    • Park, J.T.1    Uehara, T.2
  • 21
    • 0028883511 scopus 로고
    • Livermore D.M. β lactamases in laboratory and clinical resistance
    • Livermore DM. β lactamases in laboratory and clinical resistance. Clin. Microbiol. Rev. 8(4), 557-584 (1995).
    • (1995) Clin. Microbiol. Rev. , vol.8 , Issue.4 , pp. 557-584
  • 22
    • 67049107914 scopus 로고    scopus 로고
    • Inactivation of the glycoside hydrolase NagZ attenuates antipseudomonal β lactam resistance in Pseudomonas aeruginosa
    • Asgarali A, Stubbs KA, Oliver A, Vocadlo DJ, Mark BL. Inactivation of the glycoside hydrolase NagZ attenuates antipseudomonal β lactam resistance in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 53(6), 2274-2282 (2009).
    • (2009) Antimicrob. Agents Chemother. , vol.53 , Issue.6 , pp. 2274-2282
    • Asgarali, A.1    Stubbs, K.A.2    Oliver, A.3    Vocadlo, D.J.4    Mark, B.L.5
  • 23
    • 77956128431 scopus 로고    scopus 로고
    • NagZ inactivation prevents and reverts β lactam resistance driven by AmpD and PBP 4 mutations in Pseudomonas aeruginosa
    • Zamorano L, Reeve TM, Deng L et al. NagZ inactivation prevents and reverts β lactam resistance, driven by AmpD and PBP 4 mutations, in Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 54(9), 3557-3563 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.9 , pp. 3557-3563
    • Zamorano, L.1    Reeve, T.M.2    Deng, L.3
  • 24
    • 79955534986 scopus 로고    scopus 로고
    • AmpG Inactivation restores susceptibility of pan-beta lactam resistant Pseudomonas aeruginosa clinical strains
    • Zamorano L, Reeve TM, Juan C et al. AmpG Inactivation restores susceptibility of pan-beta lactam resistant Pseudomonas aeruginosa clinical strains. Antimicrob. Agents Chemother. 55(5), 1990-1996 (2011).
    • (2011) Antimicrob. Agents Chemother. , vol.55 , Issue.5 , pp. 1990-1996
    • Zamorano, L.1    Reeve, T.M.2    Juan, C.3
  • 25
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli
    • Holtje J-V. Growth of the stress-bearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol. Mol. Biol. Rev. 62(1), 181-203 (1998).
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , Issue.1 , pp. 181-203
    • Holtje, J.-V.1
  • 26
    • 0035204466 scopus 로고    scopus 로고
    • Morphogenesis of Escherichia coli
    • Vollmer W, Holtje JV. Morphogenesis of Escherichia coli. Curr. Opin. Microbiol. 4(6), 625-633 (2001).
    • (2001) Curr. Opin. Microbiol. , vol.4 , Issue.6 , pp. 625-633
    • Vollmer, W.1    Holtje, J.V.2
  • 27
    • 0028825333 scopus 로고
    • From growth to autolysis: The murein hydrolases in Escherichia coli
    • Höltje J-V. From growth to autolysis: the murein hydrolases in Escherichia coli. Arch. Microbiol. 164(4), 243-254 (1995).
    • (1995) Arch. Microbiol. , vol.164 , Issue.4 , pp. 243-254
    • Höltje, J.-V.1
  • 28
    • 0343632366 scopus 로고    scopus 로고
    • Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta lactam resistance in Gram-negative bacteria
    • Jacobs C, Frere JM, Normark S. Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta lactam resistance in Gram-negative bacteria. Cell 88(6), 823-832 (1997).
    • (1997) Cell , vol.88 , Issue.6 , pp. 823-832
    • Jacobs, C.1    Frere, J.M.2    Normark, S.3
  • 29
    • 0028147092 scopus 로고
    • Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta lactamase induction
    • Jacobs C, Huang LJ, Bartowsky E, Normark S, Park JT. Bacterial cell wall recycling provides cytosolic muropeptides as effectors for beta lactamase induction. EMBO J. 13(19), 4684-4694 (1994).
    • (1994) EMBO J. , vol.13 , Issue.19 , pp. 4684-4694
    • Jacobs, C.1    Huang, L.J.2    Bartowsky, E.3    Normark, S.4    Park, J.T.5
  • 31
    • 0036889483 scopus 로고    scopus 로고
    • Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides
    • Cheng Q, Park JT. Substrate specificity of the AmpG permease required for recycling of cell wall anhydro-muropeptides. J. Bacteriol. 184(23), 6434-6436 (2002).
    • (2002) J. Bacteriol. , vol.184 , Issue.23 , pp. 6434-6436
    • Cheng, Q.1    Park, J.T.2
  • 32
    • 0029796071 scopus 로고    scopus 로고
    • Location of N-acetylmuramyl-l-alanyl-D-glutamylmesodiaminopimelic acid presumed signal molecule for beta lactamase induction, in the bacterial cell
    • Dietz H, Pfeifle D, Wiedemann B. Location of N-acetylmuramyl-l-alanyl-D- glutamylmesodiaminopimelic acid, presumed signal molecule for beta lactamase induction, in the bacterial cell. Antimicrob. Agents Chemother. 40(9), 2173-2177 (1996).
    • (1996) Antimicrob. Agents Chemother. , vol.40 , Issue.9 , pp. 2173-2177
    • Dietz, H.1    Pfeifle, D.2    Wiedemann, B.3
  • 33
    • 0033897724 scopus 로고    scopus 로고
    • Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling
    • Cheng Q, Li H, Merdek K, Park JT. Molecular characterization of the beta-N-acetylglucosaminidase of Escherichia coli and its role in cell wall recycling. J. Bacteriol. 182(17), 4836-4840 (2000).
    • (2000) J. Bacteriol. , vol.182 , Issue.17 , pp. 4836-4840
    • Cheng, Q.1    Li, H.2    Merdek, K.3    Park, J.T.4
  • 34
    • 0034671524 scopus 로고    scopus 로고
    • Characterization of a b-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and beta lactamase induction
    • Votsch W, Templin MF. Characterization of a b-N-acetylglucosaminidase of Escherichia coli and elucidation of its role in muropeptide recycling and beta lactamase induction. J. Biol. Chem. 275(50), 39032-39038 (2000).
    • (2000) J. Biol. Chem. , vol.275 , Issue.50 , pp. 39032-39038
    • Votsch, W.1    Templin, M.F.2
  • 35
    • 0030802782 scopus 로고    scopus 로고
    • The signal molecule for beta lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide
    • Dietz H, Pfeifle D, Wiedemann B. The signal molecule for beta lactamase induction in Enterobacter cloacae is the anhydromuramyl-pentapeptide. Antimicrob. Agents Chemother. 41(10), 2113-2120 (1997).
    • (1997) Antimicrob. Agents Chemother. , vol.41 , Issue.10 , pp. 2113-2120
    • Dietz, H.1    Pfeifle, D.2    Wiedemann, B.3
  • 36
    • 0033517146 scopus 로고    scopus 로고
    • A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli
    • Templin MF, Ursinus A, Holtje JV. A defect in cell wall recycling triggers autolysis during the stationary growth phase of Escherichia coli. EMBO J. 18(15), 4108-4117 (1999).
    • (1999) EMBO J. , vol.18 , Issue.15 , pp. 4108-4117
    • Templin, M.F.1    Ursinus, A.2    Holtje, J.V.3
  • 37
    • 0025834140 scopus 로고
    • Purification and mutant analysis of Citrobacter freundii AmpR the regulator for chromosomal AmpC beta lactamase
    • Bartowsky E, Normark S. Purification and mutant analysis of Citrobacter freundii AmpR, the regulator for chromosomal AmpC beta lactamase. Mol. Microbiol. 5(7), 1715-1725 (1991).
    • (1991) Mol. Microbiol. , vol.5 , Issue.7 , pp. 1715-1725
    • Bartowsky, E.1    Normark, S.2
  • 38
    • 0024401346 scopus 로고
    • Binding of the Citrobacter freundii AmpR regulator to a single DNA site provides both autoregulation and activation of the inducible ampC beta lactamase gene
    • Lindquist S, Lindberg F, Normark S. Binding of the Citrobacter freundii AmpR regulator to a single DNA site provides both autoregulation and activation of the inducible ampC beta lactamase gene. J. Bacteriol. 171(7), 3746-3753 (1989).
    • (1989) J. Bacteriol. , vol.171 , Issue.7 , pp. 3746-3753
    • Lindquist, S.1    Lindberg, F.2    Normark, S.3
  • 39
    • 0028168986 scopus 로고
    • The negative regulator of beta lactamase induction AmpD is a N-acetyl-anhydromuramyl-l-alanine amidase
    • Holtje JV, Kopp U, Ursinus A, Wiedemann B. The negative regulator of beta lactamase induction AmpD is a N-acetyl-anhydromuramyl-l-alanine amidase. FEMS Microbiol. Lett. 122(1-2), 159-164 (1994).
    • (1994) FEMS Microbiol. Lett. , vol.122 , Issue.1-2 , pp. 159-164
    • Holtje, J.V.1    Kopp, U.2    Ursinus, A.3    Wiedemann, B.4
  • 40
    • 0028986826 scopus 로고
    • AmpD essential for both beta lactamase regulation and cell wall recycling is a novel cytosolic N-acetylmuramyl-l-alanine amidase
    • Jacobs C, Joris B, Jamin M et al. AmpD, essential for both beta lactamase regulation and cell wall recycling, is a novel cytosolic N-acetylmuramyl-l- alanine amidase. Mol. Microbiol. 15(3), 553-559 (1995).
    • (1995) Mol. Microbiol. , vol.15 , Issue.3 , pp. 553-559
    • Jacobs, C.1    Joris, B.2    Jamin, M.3
  • 41
    • 27544473088 scopus 로고    scopus 로고
    • Contribution of clonal dissemination and selection of mutants during therapy to Pseudomonas aeruginosa antimicrobial resistance in an intensive care unit setting
    • Juan C, Gutiérrez O, Oliver A, Ayestarán JI, Borrell N, Pérez JL. Contribution of clonal dissemination and selection of mutants during therapy to Pseudomonas aeruginosa antimicrobial resistance in an intensive care unit setting. Clin. Microbiol. Infec. 11(11), 887-892 (2005).
    • (2005) Clin. Microbiol. Infec. , vol.11 , Issue.11 , pp. 887-892
    • Juan, C.1    Gutiérrez, O.2    Oliver, A.3    Ayestarán, J.I.4    Borrell, N.5    Pérez, J.L.6
  • 42
    • 0025061590 scopus 로고
    • Rapid emergence of resistance in Pseudomonas aeruginosa in cystic fibrosis patients due to in-vivo selection of stable partially derepressed beta lactamase producing strains
    • Giwercman B, Lambert P, Rosdahl V, Shand G, Hoiby N. Rapid emergence of resistance in Pseudomonas aeruginosa in cystic fibrosis patients due to in-vivo selection of stable partially derepressed beta lactamase producing strains. J. Antimicrob. Chemother. 26(2), 247-259 (1990).
    • (1990) J. Antimicrob. Chemother. , vol.26 , Issue.2 , pp. 247-259
    • Giwercman, B.1    Lambert, P.2    Rosdahl, V.3    Shand, G.4    Hoiby, N.5
  • 43
    • 0034685940 scopus 로고    scopus 로고
    • High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection
    • Oliver A, Canton R, Campo P, Baquero F, Blazquez J. High frequency of hypermutable Pseudomonas aeruginosa in cystic fibrosis lung infection. Science 288(5469), 1251-1254 (2000).
    • (2000) Science , vol.288 , Issue.5469 , pp. 1251-1254
    • Oliver, A.1    Canton, R.2    Campo, P.3    Baquero, F.4    Blazquez, J.5
  • 44
    • 35848954104 scopus 로고    scopus 로고
    • Resistance mechanisms of multiresistant Pseudomonas aeruginosa strains from Germany and correlation with hypermutation
    • Henrichfreise B, Wiegand I, Pfister W, Wiedemann B. Resistance mechanisms of multiresistant Pseudomonas aeruginosa strains from Germany and correlation with hypermutation. Antimicrob. Agents Chemother. 51(11), 4062-4070 (2007).
    • (2007) Antimicrob. Agents Chemother. , vol.51 , Issue.11 , pp. 4062-4070
    • Henrichfreise, B.1    Wiegand, I.2    Pfister, W.3    Wiedemann, B.4
  • 45
    • 34948828022 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa may accumulate drug resistance mechanisms without losing its ability to cause bloodstream infections
    • Hocquet D, Berthelot P, Roussel-Delvallez M et al. Pseudomonas aeruginosa may accumulate drug resistance mechanisms without losing its ability to cause bloodstream infections. Antimicrob. Agents Chemother. 51(10), 3531-3536 (2007).
    • (2007) Antimicrob. Agents Chemother. , vol.51 , Issue.10 , pp. 3531-3536
    • Hocquet, D.1    Berthelot, P.2    Roussel-Delvallez, M.3
  • 46
    • 79955530880 scopus 로고    scopus 로고
    • Overexpression of AmpC and efflux pumps in Pseudomonas aeruginosa isolates from bloodstream infections: Prevalence and impact on resistance in a spanish multicenter study. Antimicrob
    • Cabot G, Ocampo-Sosa AA, Tubau F et al. Overexpression of AmpC and efflux pumps in Pseudomonas aeruginosa isolates from bloodstream infections: prevalence and impact on resistance in a spanish multicenter study. Antimicrob. Agents Chemother. 55(5), 1906-1911 (2011).
    • (2011) Agents Chemother. , vol.55 , Issue.5 , pp. 1906-1911
    • Cabot, G.1    Ocampo-Sosa, A.A.2    Tubau, F.3
  • 47
    • 20444447520 scopus 로고    scopus 로고
    • Gene mutations responsible for overexpression of AmpC beta lactamase in some clinical isolates of Enterobacter cloacae
    • Kaneko K, Okamoto R, Nakano R, Kawakami S, Inoue M. Gene mutations responsible for overexpression of AmpC beta lactamase in some clinical isolates of Enterobacter cloacae. J. Clin. Microbiol. 43(6), 2955-2958 (2005).
    • (2005) J. Clin. Microbiol. , vol.43 , Issue.6 , pp. 2955-2958
    • Kaneko, K.1    Okamoto, R.2    Nakano, R.3    Kawakami, S.4    Inoue, M.5
  • 48
    • 27644573842 scopus 로고    scopus 로고
    • Molecular mechanisms of beta lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains
    • Juan C, Macia MD, Gutierrez O, Vidal C, Perez JL, Oliver A. Molecular mechanisms of beta lactam resistance mediated by AmpC hyperproduction in Pseudomonas aeruginosa clinical strains. Antimicrob. Agents Chemother. 49(11), 4733-4738 (2005).
    • (2005) Antimicrob. Agents Chemother , vol.49 , Issue.11 , pp. 4733-4738
    • Juan, C.1    Macia, M.D.2    Gutierrez, O.3    Vidal, C.4    Perez, J.L.5    Oliver, A.6
  • 49
    • 0023216969 scopus 로고
    • Inactivation of the ampD gene causes semiconstitutive overproduction of the inducible Citrobacter freundii beta lactamase
    • Lindberg F, Lindquist S, Normark S. Inactivation of the ampD gene causes semiconstitutive overproduction of the inducible Citrobacter freundii beta lactamase. J. Bacteriol. 169(5), 1923-1928 (1987).
    • (1987) J. Bacteriol. , vol.169 , Issue.5 , pp. 1923-1928
    • Lindberg, F.1    Lindquist, S.2    Normark, S.3
  • 50
    • 33744814106 scopus 로고    scopus 로고
    • Genetic adaptation by Pseudomonas aeruginosa to the airways of cystic fibrosis patients
    • Smith EE, Buckley DG, Wu Z et al. Genetic adaptation by Pseudomonas aeruginosa to the airways of cystic fibrosis patients. Proc. Natl Acad. Sci. USA 103(22), 8487-8492 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , Issue.22 , pp. 8487-8492
    • Smith, E.E.1    Buckley, D.G.2    Wu, Z.3
  • 51
    • 33646458074 scopus 로고    scopus 로고
    • Stepwise upregulation of the Pseudomonas aeruginosa chromosomal cephalosporinase conferring high-level beta lactam resistance involves three AmpD homologues
    • Juan C, Moya B, Perez JL, Oliver A. Stepwise upregulation of the Pseudomonas aeruginosa chromosomal cephalosporinase conferring high-level beta lactam resistance involves three AmpD homologues. Antimicrob. Agents Chemother. 50(5), 1780-1787 (2006).
    • (2006) Antimicrob Agents Chemother. , vol.50 , Issue.5 , pp. 1780-1787
    • Juan, C.1    Moya, B.2    Perez, J.L.3    Oliver, A.4
  • 52
    • 54049144292 scopus 로고    scopus 로고
    • Benefit of having multiple ampD genes for acquiring β lactam resistance without losing fitness and virulence of Pseudomonas aeruginosa
    • Moya B, Juan C, Alberti S, Perez JL, Oliver A. Benefit of having multiple ampD genes for acquiring β lactam resistance without losing fitness and virulence of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 52(10), 3694-3700 (2008).
    • (2008) Antimicrob. Agents Chemother. , vol.52 , Issue.10 , pp. 3694-3700
    • Moya, B.1    Juan, C.2    Alberti, S.3    Perez, J.L.4    Oliver, A.5
  • 53
    • 55849133386 scopus 로고    scopus 로고
    • Role of ampD homologs in overproduction of AmpC in clinical isolates of Pseudomonas aeruginosa
    • Schmidtke AJ, Hanson ND. Role of ampD homologs in overproduction of AmpC in clinical isolates of Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 52(11), 3922-3927 (2008).
    • (2008) Antimicrob. Agents Chemother. , vol.52 , Issue.11 , pp. 3922-3927
    • Schmidtke, A.J.1    Hanson, N.D.2
  • 54
    • 63449128597 scopus 로고    scopus 로고
    • Beta lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein
    • Moya B, Dotsch A, Juan C et al. Beta lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein. PLoS Pathog. 5(3), e1000353 (2009).
    • (2009) PLoS Pathog. , vol.5 , Issue.3
    • Moya, B.1    Dotsch, A.2    Juan, C.3
  • 55
    • 0033997202 scopus 로고    scopus 로고
    • Ampr gene mutations that greatly increase class C beta lactamase activity in Enterobacter cloacae
    • Kuga A, Okamoto R, Inoue M. ampR gene mutations that greatly increase class C beta lactamase activity in Enterobacter cloacae. Antimicrob. Agents Chemother. 44(3), 561-567 (2000).
    • (2000) Antimicrob. Agents Chemother. , vol.44 , Issue.3 , pp. 561-567
    • Kuga, A.1    Okamoto, R.2    Inoue, M.3
  • 56
    • 0036841078 scopus 로고    scopus 로고
    • Constitutive high expression of chromosomal beta lactamase in Pseudomonas aeruginosa caused by a new insertion sequence IS1669 located in ampD
    • Bagge N, Ciofu O, Hentzer M, Campbell JI, Givskov M, Hoiby N. Constitutive high expression of chromosomal beta lactamase in Pseudomonas aeruginosa caused by a new insertion sequence (IS1669) located in ampD. Antimicrob. Agents Chemother. 46(11), 3406-3411 (2002).
    • (2002) Antimicrob. Agents Chemother. , vol.46 , Issue.11 , pp. 3406-3411
    • Bagge, N.1    Ciofu, O.2    Hentzer, M.3    Campbell, J.I.4    Givskov, M.5    Hoiby, N.6
  • 57
    • 27644463418 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB beta lactamases proteases, quorum sensing and other virulence factors
    • Kong KF, Jayawardena SR, Indulkar SD et al. Pseudomonas aeruginosa AmpR is a global transcriptional factor that regulates expression of AmpC and PoxB beta lactamases, proteases, quorum sensing, and other virulence factors. Antimicrob. Agents Chemother. 49(11), 4567-4575 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.11 , pp. 4567-4575
    • Kong, K.F.1    Jayawardena, S.R.2    Indulkar, S.D.3
  • 58
    • 36749062400 scopus 로고    scopus 로고
    • Molecular epidemiology and mechanisms of carbapenem resistance in Pseudomonas aeruginosa isolates from spanish hospitals
    • Gutierrez O, Juan C, Cercenado E et al. Molecular epidemiology and mechanisms of carbapenem resistance in Pseudomonas aeruginosa isolates from spanish hospitals. Antimicrob. Agents Chemother. 51(12), 4329-4335 (2007).
    • (2007) Antimicrob. Agents Chemother. , vol.51 , Issue.12 , pp. 4329-4335
    • Gutierrez, O.1    Juan, C.2    Cercenado, E.3
  • 59
    • 0026730399 scopus 로고
    • Interplay of impermeability and chromosomal beta lactamase activity in imipenem-resistant Pseudomonas aeruginosa
    • Livermore DM. Interplay of impermeability and chromosomal beta lactamase activity in imipenem-resistant Pseudomonas aeruginosa. Antimicrob. Agents Chemother. 36(9), 2046-2048 (1992).
    • (1992) Antimicrob. Agents Chemother. , vol.36 , Issue.9 , pp. 2046-2048
    • Livermore, D.M.1
  • 60
    • 33646453620 scopus 로고    scopus 로고
    • Interplay of efflux system ampC and oprD expression in carbapenem resistance of Pseudomonas aeruginosa clinical isolates
    • Quale J, Bratu S, Gupta J, Landman D. Interplay of efflux system, ampC, and oprD expression in carbapenem resistance of Pseudomonas aeruginosa clinical isolates. Antimicrob. Agents Chemother. 50(5), 1633-1641 (2006).
    • (2006) Antimicrob. Agents Chemother. , vol.50 , Issue.5 , pp. 1633-1641
    • Quale, J.1    Bratu, S.2    Gupta, J.3    Landman, D.4
  • 61
    • 0025015612 scopus 로고
    • Synthesis of 2-acetamido-2-deoxy-d-gluconhydroximolactone-derived and chitobionhydroximolactone-derived N-phenylcarbamates, potential inhibitors of beta-N-acetylglucosaminidase
    • Beer D, Maloisel JL, Rast DM, Vasella A. Synthesis of 2-acetamido-2-deoxy-d-gluconhydroximolactone-derived and chitobionhydroximolactone-derived N-phenylcarbamates, potential inhibitors of beta-N-acetylglucosaminidase. Helv. Chim. Acta 73(7), 1918-1922 (1990).
    • (1990) Helv. Chim. Acta , vol.73 , Issue.7 , pp. 1918-1922
    • Beer, D.1    Maloisel, J.L.2    Rast, D.M.3    Vasella, A.4
  • 62
    • 34547125795 scopus 로고    scopus 로고
    • Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta lactam resistance
    • Stubbs KA, Balcewich M, Mark BL, Vocadlo DJ. Small molecule inhibitors of a glycoside hydrolase attenuate inducible AmpC-mediated beta lactam resistance. J. Biol. Chem. 282(29), 21382-21391 (2007).
    • (2007) J. Biol. Chem. , vol.282 , Issue.29 , pp. 21382-21391
    • Stubbs, K.A.1    Balcewich, M.2    Mark, B.L.3    Vocadlo, D.J.4
  • 63
    • 0034635169 scopus 로고    scopus 로고
    • Mechanism of action and identification of Asp242 as the catalytic nucleophile of Vibrio furnisii N-acetyl-beta-d-glucosaminidase using 2-acetamido-2-deoxy-5-fluoro-alpha-l-idopyranosyl fluoride
    • Vocadlo DJ, Mayer C, He S, Withers SG. Mechanism of action and identification of Asp242 as the catalytic nucleophile of Vibrio furnisii N-acetyl-beta-d-glucosaminidase using 2-acetamido-2-deoxy-5-fluoro-alpha-l- idopyranosyl fluoride. Biochemistry 39(1), 117-126 (2000).
    • (2000) Biochemistry , vol.39 , Issue.1 , pp. 117-126
    • Vocadlo, D.J.1    Mayer, C.2    He, S.3    Withers, S.G.4
  • 64
    • 38349018251 scopus 로고    scopus 로고
    • Synthesis and use of mechanism-based protein-profiling probes for retaining beta-d-glucosaminidases facilitate identification of Pseudomonas aeruginosa NagZ
    • Stubbs KA, Scaffidi A, Debowski AW, Mark BL, Stick RV, Vocadlo DJ. Synthesis and use of mechanism-based protein-profiling probes for retaining beta-d-glucosaminidases facilitate identification of Pseudomonas aeruginosa NagZ. J. Am. Chem. Soc. 130(1), 327-335 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , Issue.1 , pp. 327-335
    • Stubbs, K.A.1    Scaffidi, A.2    Debowski, A.W.3    Mark, B.L.4    Stick, R.V.5    Vocadlo, D.J.6
  • 65
    • 53849121583 scopus 로고    scopus 로고
    • Mechanistic insights into glycosidase chemistry
    • Vocadlo DJ, Davies GJ. Mechanistic insights into glycosidase chemistry. Curr. Opin. Chem. Biol. 12(5), 539-555 (2008).
    • (2008) Curr. Opin. Chem. Biol. , vol.12 , Issue.5 , pp. 539-555
    • Vocadlo, D.J.1    Davies, G.J.2
  • 66
    • 25444533563 scopus 로고    scopus 로고
    • Detailed Comparative analysis of the catalytic mechanisms of beta-N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases
    • Vocadlo DJ, Withers SG. Detailed Comparative analysis of the catalytic mechanisms of beta-N-acetylglucosaminidases from families 3 and 20 of glycoside hydrolases. Biochemistry 44(38), 12809-12818 (2005).
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12809-12818
    • Vocadlo, D.J.1    Withers, S.G.2
  • 67
    • 0029940470 scopus 로고    scopus 로고
    • Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease
    • Tews I, Perrakis A, Oppenheim A, Dauter Z, Wilson KS, Vorgias CE. Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease. Nat. Struct. Biol. 3(7), 638-648 (1996).
    • (1996) Nat. Struct. Biol. , vol.3 , Issue.7 , pp. 638-648
    • Tews, I.1    Perrakis, A.2    Oppenheim, A.3    Dauter, Z.4    Wilson, K.S.5    Vorgias, C.E.6
  • 68
    • 0035971079 scopus 로고    scopus 로고
    • Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase
    • Mark BL, Vocadlo DJ, Knapp S, Triggs-Raine BL, Withers SG, James MN. Crystallographic evidence for substrate-assisted catalysis in a bacterial beta-hexosaminidase. J. Biol. Chem. 276(13), 10330-10337 (2001).
    • (2001) J. Biol. Chem. , vol.276 , Issue.13 , pp. 10330-10337
    • Mark, B.L.1    Vocadlo, D.J.2    Knapp, S.3    Triggs-Raine, B.L.4    Withers, S.G.5    James, M.N.6
  • 69
    • 33744798282 scopus 로고    scopus 로고
    • Crystallographic structure of human beta-hexosaminidase A Interpretation of Tay-Sachs mutations and loss of G M2 ganglioside hydrolysis
    • Lemieux MJ, Mark BL, Cherney MM, Withers SG, Mahuran DJ, James MN. Crystallographic structure of human beta-hexosaminidase A. Interpretation of Tay-Sachs mutations and loss of G(M2) ganglioside hydrolysis. J. Mol. Biol. 359(4), 913-929 (2006).
    • (2006) J. Mol. Biol. , vol.359 , Issue.4 , pp. 913-929
    • Lemieux, M.J.1    Mark, B.L.2    Cherney, M.M.3    Withers, S.G.4    Mahuran, D.J.5    James, M.N.6
  • 70
    • 33745049963 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity
    • Dennis RJ, Taylor EJ, Macauley MS et al. Structure and mechanism of a bacterial beta-glucosaminidase having O-GlcNAcase activity. Nat. Struct. Mol. Biol. 13(4), 365-371 (2006).
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , Issue.4 , pp. 365-371
    • Dennis, R.J.1    Taylor, E.J.2    Macauley, M.S.3
  • 71
    • 67650070343 scopus 로고    scopus 로고
    • Insight into a strategy for attenuating AmpC-mediated beta lactam resistance:Structural basis for selective inhibition of the glycoside hydrolase NagZ
    • Balcewich MD, Stubbs KA, He Y et al. Insight into a strategy for attenuating AmpC-mediated beta lactam resistance: structural basis for selective inhibition of the glycoside hydrolase NagZ. Protein Sci. 18(7), 1541-1551 (2009).
    • (2009) Protein Sci. , vol.18 , Issue.7 , pp. 1541-1551
    • Balcewich, M.D.1    Stubbs, K.A.2    He, Y.3
  • 72
    • 0027312630 scopus 로고
    • AmpG a signal transducer in chromosomal beta lactamase induction
    • Lindquist S, Weston-Hafer K, Schmidt H et al. AmpG, a signal transducer in chromosomal beta lactamase induction. Mol. Microbiol. 9(4), 703-715 (1993).
    • (1993) Mol. Microbiol. , vol.9 , Issue.4 , pp. 703-715
    • Lindquist, S.1    Weston-Hafer, K.2    Schmidt, H.3
  • 73
    • 0029004837 scopus 로고
    • The signal transducer encoded by ampG is essential for induction of chromosomal AmpC beta lactamase in Escherichia coli by beta lactam antibiotics and unspecific inducers
    • Pt 5
    • Schmidt H, Korfmann G, Barth H, Martin H. The signal transducer encoded by ampG is essential for induction of chromosomal AmpC beta lactamase in Escherichia coli by beta lactam antibiotics and 'unspecific' inducers. Microbiology 141(Pt 5), 1085-1092 (1995).
    • (1995) Microbiology , vol.141 , pp. 1085-1092
    • Schmidt, H.1    Korfmann, G.2    Barth, H.3    Martin, H.4
  • 74
    • 78049256337 scopus 로고    scopus 로고
    • Ampg gene of Pseudomonas aeruginosa and its role in beta lactamase expression
    • Zhang Y, Bao Q, Gagnon L et al. ampG gene of Pseudomonas aeruginosa and its role in beta lactamase expression. Antimicrob. Agents Chemother. 54(11), 4772-4779 (2010).
    • (2010) Antimicrob. Agents Chemother. , vol.54 , Issue.11 , pp. 4772-4779
    • Zhang, Y.1    Bao, Q.2    Gagnon, L.3
  • 75
    • 78650628952 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa beta lactamase induction requires two permeases AmpG and AmpP
    • Kong K-F, Aguila A, Schneper L, Mathee K. Pseudomonas aeruginosa beta lactamase induction requires two permeases, AmpG and AmpP. BMC Microbiol. 10(1), 328 (2010).
    • (2010) BMC Microbiol. , vol.10 , Issue.1 , pp. 328
    • Kong, K.-F.1    Aguila, A.2    Schneper, L.3    Mathee, K.4
  • 76
    • 39649099979 scopus 로고    scopus 로고
    • Lytic transglycosylases: Bacterial space-making autolysins
    • Scheurwater E, Reid CW, Clarke AJ. Lytic transglycosylases: bacterial space-making autolysins. Int. J. Biochem. Cell Biol. 40(4), 586-591 (2008).
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , Issue.4 , pp. 586-591
    • Scheurwater, E.1    Reid, C.W.2    Clarke, A.J.3
  • 77
    • 16244380780 scopus 로고    scopus 로고
    • Susceptibility to antibiotics and beta lactamase induction in murein hydrolase mutants of Escherichia coli
    • Korsak D, Liebscher S, Vollmer W. Susceptibility to antibiotics and beta lactamase induction in murein hydrolase mutants of Escherichia coli. Antimicrob. Agents Chemother. 49(4), 1404-1409 (2005).
    • (2005) Antimicrob. Agents Chemother. , vol.49 , Issue.4 , pp. 1404-1409
    • Korsak, D.1    Liebscher, S.2    Vollmer, W.3
  • 78
    • 77954624016 scopus 로고    scopus 로고
    • Crystal structure of the ampr effector binding domain provides insight into the molecular regulation of inducible AmpC β lactamase
    • Balcewich MD, Reeve TM, Orlikow EA, Donald LJ, Vocadlo DJ, Mark BL. Crystal structure of the ampr effector binding domain provides insight into the molecular regulation of inducible AmpC β lactamase. J. Mol. Biol. 400(5), 998-1010 (2010).
    • (2010) J. Mol. Biol. , vol.400 , Issue.5 , pp. 998-1010
    • Balcewich, M.D.1    Reeve, T.M.2    Orlikow, E.A.3    Donald, L.J.4    Vocadlo, D.J.5    Mark, B.L.6
  • 79
    • 78650078263 scopus 로고    scopus 로고
    • FtsZ in bacterial cytokinesis: Cytoskeleton and force generator all in one
    • Erickson HP, Anderson DE, Osawa M. FtsZ in bacterial cytokinesis: cytoskeleton and force generator all in one. Microbiol. Mol. Biol. Rev. 74(4), 504-528 (2010).
    • (2010) Microbiol. Mol. Biol. Rev. , vol.74 , Issue.4 , pp. 504-528
    • Erickson, H.P.1    Anderson, D.E.2    Osawa, M.3
  • 80
    • 77957963129 scopus 로고    scopus 로고
    • Bacterial shape: Two-dimensional questions and possibilities
    • Young KD. Bacterial shape: two-dimensional questions and possibilities. Annu. Rev. Microbiol. 64(1), 223-240 (2010).
    • (2010) Annu. Rev. Microbiol. , vol.64 , Issue.1 , pp. 223-240
    • Young, K.D.1
  • 82
    • 68549092791 scopus 로고    scopus 로고
    • Targeting FtsZ for antibacterial therapy: A promising avenue
    • Kapoor S, Panda D. Targeting FtsZ for antibacterial therapy: a promising avenue. Expert Opin. Ther. Targets 13(9), 1037-1051 (2009).
    • (2009) Expert Opin. Ther. Targets , vol.13 , Issue.9 , pp. 1037-1051
    • Kapoor, S.1    Panda, D.2
  • 83
    • 52249120794 scopus 로고    scopus 로고
    • An inhibitor of FtsZ with potent and selective anti-staphylococcal activity
    • Haydon DJ, Stokes NR, Ure R et al. An inhibitor of FtsZ with potent and selective anti-staphylococcal activity. Science 321(5896), 1673-1675 (2008).
    • (2008) Science , vol.321 , Issue.5896 , pp. 1673-1675
    • Haydon, D.J.1    Stokes, N.R.2    Ure, R.3
  • 84
    • 0025953798 scopus 로고
    • Induction of a class I beta lactamase from Citrobacter freundii in Escherichia coli requires active ftsZ but not ftsA or ftsQ products
    • Ottolenghi AC, Ayala JA. Induction of a class I beta lactamase from Citrobacter freundii in Escherichia coli requires active ftsZ but not ftsA or ftsQ products. Antimicrob. Agents Chemother. 35(11), 2359-2365 (1991).
    • (1991) Antimicrob. Agents Chemother. , vol.35 , Issue.11 , pp. 2359-2365
    • Ottolenghi, A.C.1    Ayala, J.A.2
  • 85
    • 0036062233 scopus 로고    scopus 로고
    • Role of the murein precursor UDP-N-acetylmuramyl-l-Ala-gamma-d-Glu-meso- diaminopimelic acid-d-Ala-d-Ala in repression of beta lactamase induction in cell division mutants
    • Uehara T, Park JT. Role of the murein precursor UDP-N-acetylmuramyl-l- Ala-gamma-d-Glu-meso-diaminopimelic acid-d-Ala-d-Ala in repression of beta lactamase induction in cell division mutants. J. Bacteriol. 184(15), 4233-4239 (2002).
    • (2002) J. Bacteriol. , vol.184 , Issue.15 , pp. 4233-4239
    • Uehara, T.1    Park, J.T.2
  • 86
    • 29244432515 scopus 로고    scopus 로고
    • Sanguinarine blocks cytokinesis in bacteria by inhibiting FtsZ assembly and bundling
    • Beuria TK, Santra MK, Panda D. Sanguinarine blocks cytokinesis in bacteria by inhibiting FtsZ assembly and bundling. Biochemistry 44(50), 16584-16593 (2005).
    • (2005) Biochemistry , vol.44 , Issue.50 , pp. 16584-16593
    • Beuria, T.K.1    Santra, M.K.2    Panda, D.3
  • 87
    • 0038647815 scopus 로고    scopus 로고
    • Genetic linkage of the penicillinase gene amp and blrAB encoding the regulator of β lactamase expression in Aeromonas spp
    • Niumsup P, Simm AM, Nurmahomed K, Walsh TR, Bennett PM, Avison MB. Genetic linkage of the penicillinase gene, amp, and blrAB, encoding the regulator of β lactamase expression in Aeromonas spp. J. Antimicrob. Chemother. 51(6), 1351-1358 (2003).
    • (2003) J. Antimicrob. Chemother. , vol.51 , Issue.6 , pp. 1351-1358
    • Niumsup, P.1    Simm, A.M.2    Nurmahomed, K.3    Walsh, T.R.4    Bennett, P.M.5    Avison, M.B.6
  • 88
    • 18944367563 scopus 로고    scopus 로고
    • Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate
    • Uehara T, Suefuji K, Valbuena N, Meehan B, Donegan M, Park JT. Recycling of the anhydro-N-acetylmuramic acid derived from cell wall murein involves a two-step conversion to N-acetylglucosamine-phosphate. J. Bacteriol. 187(11), 3643-3649 (2005).
    • (2005) J. Bacteriol. , vol.187 , Issue.11 , pp. 3643-3649
    • Uehara, T.1    Suefuji, K.2    Valbuena, N.3    Meehan, B.4    Donegan, M.5    Park, J.T.6
  • 89
    • 24044450244 scopus 로고    scopus 로고
    • Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli etherase
    • Jaeger T, Arsic M, Mayer C. Scission of the lactyl ether bond of N-acetylmuramic acid by Escherichia coli "etherase". J. Biol. Chem. 280(34), 30100-30106 (2005).
    • (2005) J. Biol. Chem. , vol.280 , Issue.34 , pp. 30100-30106
    • Jaeger, T.1    Arsic, M.2    Mayer, C.3
  • 90
    • 79953316848 scopus 로고    scopus 로고
    • Molecular basis of 1 6-anhydro bond cleavage and phosphoryl transfer by Pseudomonas aeruginosa 1 6-anhydro-N-acetylmuramic acid kinase
    • Bacik J-P, Whitworth GE, Stubbs KA et al. Molecular basis of 1,6-anhydro bond cleavage and phosphoryl transfer by Pseudomonas aeruginosa 1,6-anhydro-N-acetylmuramic acid kinase. J. Biol. Chem. 286(14), 12283-12291 (2011).
    • (2011) J. Biol. Chem. , vol.286 , Issue.14 , pp. 12283-12291
    • Bacik, J.-P.1    Whitworth, G.E.2    Stubbs, K.A.3


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