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Volumn 439, Issue 2, 2013, Pages 73-79

Assay for peptidoglycan O-acetyltransferase: A potential new antibacterial target

Author keywords

Muramic acid; O acetylation; O acetyltransferase; Peptidoglycan; Transacetylase

Indexed keywords

ACETYLATION; BACTERIOLOGY; CATALYSIS; DESORPTION; DRUG PRODUCTS; ENZYMES; MASS SPECTROMETRY; STAPHYLOCOCCUS AUREUS; SUBSTRATES;

EID: 84879229569     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2013.04.022     Document Type: Article
Times cited : (27)

References (24)
  • 1
    • 84871808951 scopus 로고    scopus 로고
    • Control of lytic transglycosylase activity within bacterial cell walls
    • in: C.W. Reid, S.M. Twine, A.N. Reid (Eds.), Caister Academic Press, Norfolk, UK
    • J.M. Pfeffer, P.J. Moynihan, C.A. Clarke, A.J. Clarke, Control of lytic transglycosylase activity within bacterial cell walls, in: C.W. Reid, S.M. Twine, A.N. Reid (Eds.), Bacterial Glycomics, Caister Academic Press, Norfolk, UK, 2012, pp. 55-68.
    • (2012) Bacterial Glycomics , pp. 55-68
    • Pfeffer, J.M.1    Moynihan, P.J.2    Clarke, C.A.3    Clarke, A.J.4
  • 2
    • 39149102149 scopus 로고    scopus 로고
    • Structural variation in the glycan strands of bacterial peptidoglycan
    • DOI 10.1111/j.1574-6976.2007.00088.x
    • W. Vollmer, Structural variation in the glycan strands of bacterial peptidoglycan, FEMS Microbiol. Rev. 32 (2008) 287-306. (Pubitemid 351257811)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.2 , pp. 287-306
    • Vollmer, W.1
  • 3
    • 0026605558 scopus 로고
    • O-Acetylated peptidoglycan: Its occurrence pathobiological significance and biosynthesis
    • A.J. Clarke, C. Dupont, O-Acetylated peptidoglycan: its occurrence, pathobiological significance, and biosynthesis, Can. J. Microbiol. 38 (1992) 85-91.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 85-91
    • Clarke, A.J.1    Dupont, C.2
  • 4
    • 0025972046 scopus 로고
    • Dependence of lysozyme-catalysed solubilization of proteus mirabilis peptidoglycan on the extent of o-Acetylation
    • C. Dupont, A.J. Clarke, Dependence of lysozyme-catalysed solubilization of Proteus mirabilis peptidoglycan on the extent of O-Acetylation, Eur. J. Biochem. 195 (1991) 763-769.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 763-769
    • Dupont, C.1    Clarke, A.J.2
  • 5
    • 0021033685 scopus 로고
    • Strain distribution in extents of lysozyme resistance and O-acetylation of gonococcal peptidoglycan determined by high-performance liquid chromatography
    • S.G. Swim, M.A. Gfell, C.E. Wilde III, R.S. Rosenthal, Strain distribution in extents of lysozyme resistance and O-Acetylation of gonocccal peptidoglycan determined by high-performance liquid chromatography, Infect. Immun. 42 (1983) 446-452. (Pubitemid 14230232)
    • (1983) Infection and Immunity , vol.42 , Issue.2 , pp. 446-452
    • Swim, S.C.1    Gfell, M.A.2    Wilde III, C.E.3    Rosenthal, R.S.4
  • 6
    • 0020632077 scopus 로고
    • Resistance of oacetylated gonococcal peptidoglycan to human peptidoglycan-degrading enzymes
    • R.S. Rosenthal, W.J. Folkening, D.R. Miller, S.C. Swim, Resistance of Oacetylated gonococcal peptidoglycan to human peptidoglycan-degrading enzymes, Infect. Immun. 40 (1983) 826-829.
    • (1983) Infect. Immun. , vol.40 , pp. 826-829
    • Rosenthal, R.S.1    Folkening, W.J.2    Miller, D.R.3    Swim, S.C.4
  • 7
    • 0020028114 scopus 로고
    • Strain-related differences in lysozyme sensitivity and extent of O-acetylation of gonococcal peptidoglycan
    • R.S. Rosenthal, J.K. Blundell, H.R. Perkins, Strain-related differences in lysozyme sensitivity and extent of O-Acetylation of gonococcal peptidoglycan, Infect. Immun. 37 (1982) 826-829. (Pubitemid 12100075)
    • (1982) Infection and Immunity , vol.37 , Issue.2 , pp. 826-829
    • Rosenthal, R.S.1    Blundell, J.K.2    Perkins, H.R.3
  • 8
    • 0019127047 scopus 로고
    • The peptidoglycan of Neisseria gonorrhoeae: O-acetyl groups and lysozyme sensitivity
    • DOI 10.1016/0378-1097(80)90028-2
    • J.K. Blundell, G.J. Smith, H.R. Perkins, The peptidoglycan of Neisseria gonorrhoeae: O-Acetyl groups and lysozyme sensitivity, FEMS Microbiol. Lett. 9 (1980) 259-261. (Pubitemid 11178176)
    • (1980) FEMS Microbiology Letters , vol.9 , Issue.4 , pp. 259-261
    • Blundell, J.K.1    Smith, G.J.2    Perkins, H.R.3
  • 9
    • 79953157865 scopus 로고    scopus 로고
    • O-Acetylation of peptidoglycan is required for proper cell separation and s-layer anchoring in bacillus anthracis
    • M.-H. Laaberki, J. Pfeffer, A.J. Clarke, J. Dworkin, O-Acetylation of peptidoglycan is required for proper cell separation and S-layer anchoring in Bacillus anthracis, J. Biol. Chem. 286 (2011) 5278-5288.
    • (2011) J. Biol. Chem. , vol.286 , pp. 5278-5288
    • Laaberki, M.-H.1    Pfeffer, J.2    Clarke, A.J.3    Dworkin, J.4
  • 10
    • 31344451043 scopus 로고    scopus 로고
    • Peptidoglycan O acetylation and autolysin profile of Enterococcus faecalis in the viable but nonculturable state
    • DOI 10.1128/JB.188.3.902-908.2006
    • J.M. Pfeffer, H. Strating, J.T. Weadge, A.J. Clarke, Peptidoglcyan O-Acetylation and autolysin profile of Enterococcus faecalis in the viable but non-culturable state, J. Bacteriol. 188 (2006) 902-908. (Pubitemid 43146405)
    • (2006) Journal of Bacteriology , vol.188 , Issue.3 , pp. 902-908
    • Pfeffer, J.M.1    Strating, H.2    Weadge, J.T.3    Clarke, A.J.4
  • 11
    • 80255137078 scopus 로고    scopus 로고
    • O-Acetylated peptidoglycan: Controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems
    • P.J. Moynihan, A.J. Clarke, O-Acetylated peptidoglycan: controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems, Int. J. Biochem. Cell Biol. 43 (2011) 1655-1659.
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1655-1659
    • Moynihan, P.J.1    Clarke, A.J.2
  • 13
    • 0344393521 scopus 로고    scopus 로고
    • Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria
    • DOI 10.1007/s00018-003-3056-1
    • G. Koraimann, Lytic transglycosylases in macromolecular transport systems of gram-negative bacteria, Cell. Mol. Life Sci. 60 (2003) 2371-2388. (Pubitemid 37487258)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.11 , pp. 2371-2388
    • Koraimann, G.1
  • 14
    • 0016726181 scopus 로고
    • Novel type of murein transglycosylase in escherichia coli
    • J.-V. Höltje, D. Mirelman, N. Sharon, U. Schwarz, Novel type of murein transglycosylase in Escherichia coli, J. Bacteriol. 124 (1975) 1067-1076.
    • (1975) J. Bacteriol. , vol.124 , pp. 1067-1076
    • Höltje, J.-V.1    Mirelman, D.2    Sharon, N.3    Schwarz, U.4
  • 15
    • 77951243041 scopus 로고    scopus 로고
    • O-Acetylation of peptidoglycan in gram-negative bacteria: Identification and characterization of peptidoglycan oacetyltransferase in neisseria gonorrhoeae
    • P.J. Moynihan, A.J. Clarke, O-Acetylation of peptidoglycan in gram-negative bacteria: identification and characterization of peptidoglycan Oacetyltransferase in Neisseria gonorrhoeae, J. Biol. Chem. 285 (2010) 13264-13273.
    • (2010) J. Biol. Chem. , vol.285 , pp. 13264-13273
    • Moynihan, P.J.1    Clarke, A.J.2
  • 16
    • 84874201976 scopus 로고    scopus 로고
    • De-o-Acetylation of peptidoglycan regulates glycan chain extension and affects in vivo survival of neisseria meningitides
    • F.J. Veyrier, A.H. Williams, S. Mesnage, C. Schmitt, M.-K. Taha1, I.G. Boneca, De-O-Acetylation of peptidoglycan regulates glycan chain extension and affects in vivo survival of Neisseria meningitides, Mol. Microbiol. 87 (2013) 1100-1112.
    • (2013) Mol. Microbiol. , vol.87 , pp. 1100-1112
    • Veyrier, F.J.1    Williams, A.H.2    Mesnage, S.3    Schmitt, C.4    Tahal, M.-K.5    Boneca, I.G.6
  • 17
    • 84872168801 scopus 로고    scopus 로고
    • Helicobacter pylori peptidoglycan modifications confer lysozyme resistance and contribute to survival in the host
    • G. Wang, L. Lo, L.S. Forsberg, R.J. Maier, Helicobacter pylori peptidoglycan modifications confer lysozyme resistance and contribute to survival in the host, mBio 3 (2012) e00409-e00412.
    • (2012) MBio , vol.3
    • Wang, G.1    Lo, L.2    Forsberg, L.S.3    Maier, R.J.4
  • 18
    • 24344487095 scopus 로고    scopus 로고
    • Identification of a new family of enzymes with potential o-Acetylpeptidoglycan esterase activity in both gram-positive and gram-negative bacteria
    • J.T. Weadge, J.M. Pfeffer, A.J. Clarke, Identification of a new family of enzymes with potential O-Acetylpeptidoglycan esterase activity in both gram-positive and gram-negative bacteria, BMC Microbiol. 5 (2005) 49.
    • (2005) BMC Microbiol. , vol.5 , pp. 49
    • Weadge, J.T.1    Pfeffer, J.M.2    Clarke, A.J.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage t4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 31044439427 scopus 로고    scopus 로고
    • Identification and characterization of O-acetylpeptidoglycan esterase: A novel enzyme discovered in Neisseria gonorrhoeae
    • DOI 10.1021/bi051679s
    • J.T. Weadge, A.J. Clarke, Identification and characterization of Oacetylpeptidoglycan esterase: a novel enzyme discovered in Neisseria gonorrhoeae, Biochemistry 45 (2006) 839-851. (Pubitemid 43122248)
    • (2006) Biochemistry , vol.45 , Issue.3 , pp. 839-851
    • Weadge, J.T.1    Clarke, A.J.2
  • 21
    • 50549087221 scopus 로고    scopus 로고
    • Transacetylations of carbohydrates in organic solvent catalysed by o-Acetylpeptidoglycan esterase from neisseria gonorrhoeae
    • J.T. Weadge, A.J. Clarke, Transacetylations of carbohydrates in organic solvent catalysed by O-Acetylpeptidoglycan esterase from Neisseria gonorrhoeae, Biocatal. Biotransform. 26 (2008) 68-75.
    • (2008) Biocatal. Biotransform. , vol.26 , pp. 68-75
    • Weadge, J.T.1    Clarke, A.J.2
  • 22
    • 0001720836 scopus 로고    scopus 로고
    • Pathways for the o-Acetylation of bacterial cell wall polysaccharides
    • R.J. Doyle (Ed.), Plenum, New York
    • A.J. Clarke, H. Strating, N.T. Blackburn, Pathways for the O-Acetylation of bacterial cell wall polysaccharides, in: R.J. Doyle (Ed.), Glycomicrobiology, Plenum, New York, 2000, pp. 187-223.
    • (2000) Glycomicrobiology , pp. 187-223
    • Clarke, A.J.1    Strating, H.2    Blackburn, N.T.3
  • 23
    • 0016716146 scopus 로고
    • Purification of several bacteriolytic enzymes by affinity chromatography on lysozyme-lysate of micrococcus lysodeikticus cell wall coupled with sepharose
    • T. Yoshimoto, S. Hayashida, M. Tobiishi, K. Kado, D. Tsuru, Purification of several bacteriolytic enzymes by affinity chromatography on lysozyme-lysate of Micrococcus lysodeikticus cell wall coupled with Sepharose, J. Biochem. 78 (1975) 253-259.
    • (1975) J. Biochem. , vol.78 , pp. 253-259
    • Yoshimoto, T.1    Hayashida, S.2    Tobiishi, M.3    Kado, K.4    Tsuru, D.5
  • 24
    • 84858326029 scopus 로고    scopus 로고
    • Identification of first-known inhibitors of oacetylpeptidoglycan esterase: A potential new antibacterial target
    • J.M. Pfeffer, A.J. Clarke, Identification of first-known inhibitors of Oacetylpeptidoglycan esterase: a potential new antibacterial target, ChemBioChem 13 (2012) 722-731.
    • (2012) ChemBioChem , vol.13 , pp. 722-731
    • Pfeffer, J.M.1    Clarke, A.J.2


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