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Volumn 288, Issue 4, 2013, Pages 2605-2613

Mechanism of action of neisseria gonorrhoeae o-acetylpeptidoglycan esterase, an SGNH serine esterase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BINDING STUDIES; CARBOHYDRATE ESTERASE; CATALYTIC RESIDUE; CATALYTIC TRIAD; CELL WALLS; CLASSIFICATION SYSTEM; CONSERVED RESIDUES; KINETIC CHARACTERIZATION; KINETIC STUDY; MECHANISM OF ACTION; NEISSERIA GONORRHOEAE; O-ACETYL GROUP; OXYANION HOLE; PEPTIDOGLYCANS; REACTION MECHANISM; SEQUENCE SIMILARITY; STRUCTURE AND FUNCTION RELATIONSHIP; SUBSTRATE BINDING; THREE-DIMENSIONAL STRUCTURE;

EID: 84873845734     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.436352     Document Type: Article
Times cited : (33)

References (32)
  • 1
    • 39149102149 scopus 로고    scopus 로고
    • Structural variation in the glycan strands of bacterial peptidoglycan
    • Vollmer, W. (2008) Structural variation in the glycan strands of bacterial peptidoglycan. FEMS Microbiol. Rev. 32, 287-306
    • (2008) FEMS Microbiol. Rev. , vol.32 , pp. 287-306
    • Vollmer, W.1
  • 2
  • 3
    • 80255137078 scopus 로고    scopus 로고
    • O-Acetylated peptidoglycan: Controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems
    • Moynihan, P. J., and Clarke, A. J. (2011)O-Acetylated peptidoglycan: Controlling the activity of bacterial autolysins and lytic enzymes of innate immune systems. Int. J. Biochem. Cell Biol. 43, 1655-1659
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 1655-1659
    • Moynihan, P.J.1    Clarke, A.J.2
  • 4
    • 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
    • Weadge, J. T., Pfeffer, J. M., and Clarke, A. J. (2005) Identification of a new family of enzymes with potential O-acetylpeptidoglycan esterase activity in both Gram-positive and Gram-negative bacteria. BMC Microbiol. 5, 49
    • (2005) BMC Microbiol , vol.5 , pp. 49
    • Weadge, J.T.1    Pfeffer, J.M.2    Clarke, A.J.3
  • 5
    • 31044439427 scopus 로고    scopus 로고
    • Identification and characterization ofO-acetylpeptidoglycan esterase: A novel enzyme discovered in Neisseria gonorrhoeae
    • Weadge, J. T., and Clarke, A. J. (2006) Identification and characterization ofO-acetylpeptidoglycan esterase: a novel enzyme discovered in Neisseria gonorrhoeae. Biochemistry 45, 839-851
    • (2006) Biochemistry , vol.45 , pp. 839-851
    • Weadge, J.T.1    Clarke, A.J.2
  • 6
    • 84858326029 scopus 로고    scopus 로고
    • Identification of first-known inhibitors of O-acetylpeptidoglycan esterase: A potential new antibacterial target
    • Pfeffer, J. M., and Clarke, A. J. (2012) Identification of first-known inhibitors of O-acetylpeptidoglycan esterase: A potential new antibacterial target. ChemBioChem. 13, 722-731
    • (2012) ChemBioChem. , vol.13 , pp. 722-731
    • Pfeffer, J.M.1    Clarke, A.J.2
  • 7
    • 34247542105 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, a serine esterase with a Ser-His-Asp catalytic triad
    • Weadge, J. T., and Clarke, A. J. (2007) Neisseria gonorrhoeae O-acetylpeptidoglycan esterase, a serine esterase with a Ser-His-Asp catalytic triad. Biochemistry 46, 4932-4941
    • (2007) Biochemistry , vol.46 , pp. 4932-4941
    • Weadge, J.T.1    Clarke, A.J.2
  • 10
    • 0033954914 scopus 로고    scopus 로고
    • Stable shuttle vectors for Neisseria gonorrhoeae, Haemophilus spp, and other bacteria based on a single origin of replication
    • Pagotto, F. J., Salimnia, H., Totten, P. A., and Dillon, J. R. (2000) Stable shuttle vectors for Neisseria gonorrhoeae, Haemophilus spp., and other bacteria based on a single origin of replication. Gene 244, 13-19
    • (2000) Gene , vol.244 , pp. 13-19
    • Pagotto, F.J.1    Salimnia, H.2    Totten, P.A.3    Dillon, J.R.4
  • 11
    • 0025972046 scopus 로고
    • Dependence of lysozyme-catalysed solubilization of Proteus mirabilis peptidoglycan on the extent ofO-acetylation
    • Dupont, C., and Clarke, A. J. (1991) Dependence of lysozyme-catalysed solubilization of Proteus mirabilis peptidoglycan on the extent ofO-acetylation. Eur. J. Biochem. 195, 763-769
    • (1991) Eur. J. Biochem. , vol.195 , pp. 763-769
    • Dupont, C.1    Clarke, A.J.2
  • 12
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama, N., and Woody, R. W. (1993) A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209, 32-44
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 13
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama, N., Venyaminov, S. Y., and Woody, R. W. (1999) Estimation of the number of α-helical and β-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8, 370-380
    • (1999) Protein Sci. , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 14
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 15
    • 0034672122 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Inclusion of denatured proteins with native proteins in the analysis
    • Sreerama, N., Venyaminov, S. Y., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: inclusion of denatured proteins with native proteins in the analysis. Anal. Biochem. 287, 243-251
    • (2000) Anal. Biochem. , vol.287 , pp. 243-251
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 16
    • 43749112959 scopus 로고    scopus 로고
    • The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase
    • Scheurwater, E. M., and Clarke, A. J. (2008) The C-terminal domain of Escherichia coli YfhD functions as a lytic transglycosylase. J. Biol. Chem. 283, 8363-8373
    • (2008) J. Biol. Chem. , vol.283 , pp. 8363-8373
    • Scheurwater, E.M.1    Clarke, A.J.2
  • 17
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 18
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier, J., Gibrat, J. F., and Robson, B. (1996) GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol. 266, 540-553
    • (1996) Methods Enzymol. , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 20
    • 0033578684 scopus 로고    scopus 로고
    • Protein secondary structure prediction based on position- specific scoring matrices
    • Jones, D. T. (1999) Protein secondary structure prediction based on position- specific scoring matrices. J. Mol. Biol. 292, 195-202
    • (1999) J. Mol. Biol. , vol.292 , pp. 195-202
    • Jones, D.T.1
  • 21
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K., and Jones, D. T. (2000) The PSIPRED protein structure prediction server. Bioinformatics 16, 404-405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0027279951 scopus 로고
    • Extent of peptidoglycan O acetylation in the tribe Proteeae
    • Clarke, A. J. (1993) Extent of peptidoglycan O acetylation in the tribe Proteeae. J. Bacteriol. 175, 4550-4553
    • (1993) J. Bacteriol. , vol.175 , pp. 4550-4553
    • Clarke, A.J.1
  • 25
    • 0027293346 scopus 로고
    • Compositional analysis of peptidoglycan by high performance anion-exchange chromatography
    • Clarke A. J. (1993) Compositional analysis of peptidoglycan by high performance anion-exchange chromatography. Anal. Biochem. 212, 344-350
    • (1993) Anal. Biochem. , vol.212 , pp. 344-350
    • Clarke, A.J.1
  • 26
    • 43049170350 scopus 로고    scopus 로고
    • Crystal structure of a cellulosomal family 3 carbohydrate esterase from Clostridium thermocellum provides insights into the mechanism of substrate recognition
    • Correia, M. A., Prates, J. A., Brás, J., Fontes, C. M., Newman, J. A., Lewis, R. J., Gilbert, H. J., and Flint, J. E. (2008) Crystal structure of a cellulosomal family 3 carbohydrate esterase from Clostridium thermocellum provides insights into the mechanism of substrate recognition. J. Mol. Biol. 379, 64-72
    • (2008) J. Mol. Biol. , vol.379 , pp. 64-72
    • Correia, M.A.1    Prates, J.A.2    Brás, J.3    Fontes, C.M.4    Newman, J.A.5    Lewis, R.J.6    Gilbert, H.J.7    Flint, J.E.8
  • 28
    • 0034655985 scopus 로고    scopus 로고
    • Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases
    • Mølgaard, A., Kauppinen, S., and Larsen, S. (2000) Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases. Structure 8, 373-383
    • (2000) Structure , vol.8 , pp. 373-383
    • Mølgaard, A.1    Kauppinen, S.2    Larsen, S.3
  • 29
    • 0038723702 scopus 로고    scopus 로고
    • Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: Consensus sequence blocks constitute the catalytic center of SGNH-hy- drolases through a conserved hydrogen bond network
    • Lo, Y. C., Lin, S. C., Shaw, J. F., and Liaw, Y. C. (2003) Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hy- drolases through a conserved hydrogen bond network. J. Mol. Biol. 330, 539 -551
    • (2003) J. Mol. Biol. , vol.330 , pp. 539-551
    • Lo, Y.C.1    Lin, S.C.2    Shaw, J.F.3    Liaw, Y.C.4
  • 30
    • 0029960232 scopus 로고    scopus 로고
    • Site-directed mutagenesis of a novel serine arylesterase from Vibrio mimicus identifies residues essential for catalysis
    • Chang, R. C., Chen, J. C., and Shaw, J. F. (1996) Site-directed mutagenesis of a novel serine arylesterase from Vibrio mimicus identifies residues essential for catalysis. Biochem. Biophys. Res. Commun. 221, 477-483
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 477-483
    • Chang, R.C.1    Chen, J.C.2    Shaw, J.F.3
  • 31
    • 27344441825 scopus 로고    scopus 로고
    • Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor
    • Blair, D. E., Schüttelkopf, A. W., MacRae, J. I., and van Aalten, D. M. (2005) Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Proc. Natl. Acad. Sci. U.S.A. 102, 15429-15434
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15429-15434
    • Blair, D.E.1    Schüttelkopf, A.W.2    MacRae, J.I.3    Van Aalten, D.M.4
  • 32
    • 0042330067 scopus 로고    scopus 로고
    • Subsite structure of the endo-type chitin deacetylase from a deuteromycete, Colletotrichum lindemuthianum: An investigation using steady-state kinetic analysis and MS
    • Hekmat, O., Tokuyasu, K., and Withers, S. G. (2003) Subsite structure of the endo-type chitin deacetylase from a deuteromycete, Colletotrichum lindemuthianum: an investigation using steady-state kinetic analysis and MS. Biochem. J. 374, 369-380
    • (2003) Biochem. J. , vol.374 , pp. 369-380
    • Hekmat, O.1    Tokuyasu, K.2    Withers, S.G.3


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