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Volumn 581, Issue 25, 2007, Pages 4988-4992

Role of Ser216 in the mechanism of action of membrane-bound lytic transglycosylase B: Further evidence for substrate-assisted catalysis

Author keywords

1,6 anhydromuropeptide; HPAEC; Lytic transglycosylase; Peptidoglycan; Site directed mutagenesis; Substrate assisted catalysis; Zymogram

Indexed keywords

1,6 ANHYDROMURAMOYL; ENZYME; GLYCOSYLTRANSFERASE; HYDROLASE; MEMBRANE ENZYME; N ACETYLGLUCOSAMINE; N ACETYLMURAMIC ACID; SER 216 ENZYME; UNCLASSIFIED DRUG;

EID: 34948837924     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.09.037     Document Type: Article
Times cited : (13)

References (30)
  • 1
    • 0041664049 scopus 로고    scopus 로고
    • Bacterial shape
    • Young K.D. Bacterial shape. Mol. Microbiol. 49 (2003) 571-580
    • (2003) Mol. Microbiol. , vol.49 , pp. 571-580
    • Young, K.D.1
  • 3
    • 50049104157 scopus 로고    scopus 로고
    • Vollmer, W. and Bertsche, U. (2007) Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli. Biochim. Biophys. Acta, doi:10.1016/j.bbamem.2007.06.007. (Epub ahead of print).
  • 4
    • 0016726181 scopus 로고
    • Novel type of murein transglycosylase in Escherichia coli
    • Höltje J.-V., Mirelman D., Sharon N., and Schwarz U. 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
  • 5
    • 0021881891 scopus 로고
    • Recycling of murein by Escherichia coli
    • Goodell E.W. Recycling of murein by Escherichia coli. J. Bacteriol. 163 (1985) 305-310
    • (1985) J. Bacteriol. , vol.163 , pp. 305-310
    • Goodell, E.W.1
  • 6
    • 0026066957 scopus 로고
    • The murein hydrolases of Escherichia coli: properties, functions and impact on the course of infections in vivo
    • Höltje J.-V., and Tuomanen E.I. The murein hydrolases of Escherichia coli: properties, functions and impact on the course of infections in vivo. J. Gen. Microbiol. 137 (1991) 441-454
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 441-454
    • Höltje, J.-V.1    Tuomanen, E.I.2
  • 7
    • 0026605558 scopus 로고
    • O-Acetylated peptidoglycan: its occurrence, pathobiological significance and biosynthesis
    • Clarke A.J., and Dupont C. 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
  • 8
    • 0027499306 scopus 로고
    • Bordetella pertussis tracheal cytotoxin and other muramyl peptides: distinct structure-activity relationships for respiratory epithelial cytopathology
    • Luker K.E., Collier J.L., Kolodziej E.W., Marshall G.R., and Goldman W.E. Bordetella pertussis tracheal cytotoxin and other muramyl peptides: distinct structure-activity relationships for respiratory epithelial cytopathology. Proc. Natl. Acad. Sci. USA 90 (1993) 2365-2369
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2365-2369
    • Luker, K.E.1    Collier, J.L.2    Kolodziej, E.W.3    Marshall, G.R.4    Goldman, W.E.5
  • 9
    • 0021326947 scopus 로고
    • Ability of monomeric peptidoglycan from Neisseria gonorrhoeae to damage human fallopian-tube mucosa
    • Melly M.A., McGee Z.A., and Rosenthal R.S. Ability of monomeric peptidoglycan from Neisseria gonorrhoeae to damage human fallopian-tube mucosa. J. Infect. Dis. 149 (1984) 378-386
    • (1984) J. Infect. Dis. , vol.149 , pp. 378-386
    • Melly, M.A.1    McGee, Z.A.2    Rosenthal, R.S.3
  • 10
    • 0035140936 scopus 로고    scopus 로고
    • Identification of four families of microbial lytic transglycosylases
    • Blackburn N.T., and Clarke A.J. Identification of four families of microbial lytic transglycosylases. J. Mol. Evol. 52 (2001) 78-84
    • (2001) J. Mol. Evol. , vol.52 , pp. 78-84
    • Blackburn, N.T.1    Clarke, A.J.2
  • 11
    • 0037154093 scopus 로고    scopus 로고
    • Characterization of soluble and membrane-bound family 3 lytic transglycosylases from Pseudomonas aeruginosa
    • Blackburn N.T., and Clarke A.J. Characterization of soluble and membrane-bound family 3 lytic transglycosylases from Pseudomonas aeruginosa. Biochemistry 41 (2002) 1001-1013
    • (2002) Biochemistry , vol.41 , pp. 1001-1013
    • Blackburn, N.T.1    Clarke, A.J.2
  • 12
    • 4444306016 scopus 로고    scopus 로고
    • Substrate binding affinity of Pseudomonas aeruginosa membrane-bound lytic transglycosylase B by hydrogen-deuterium exchange MALDI-MS
    • Reid C.W., Brewer D., and Clarke A.J. Substrate binding affinity of Pseudomonas aeruginosa membrane-bound lytic transglycosylase B by hydrogen-deuterium exchange MALDI-MS. Biochemistry 43 (2004) 11275-11282
    • (2004) Biochemistry , vol.43 , pp. 11275-11282
    • Reid, C.W.1    Brewer, D.2    Clarke, A.J.3
  • 13
    • 0029947945 scopus 로고    scopus 로고
    • NAG-thiazoline, an N-acetyl-betahexosaminidase inhibitor that implicates acetamido participation
    • Knapp S., Vocadlo D.J., Gao Z., Kirk B., Lou J., and Withers S.G. NAG-thiazoline, an N-acetyl-betahexosaminidase inhibitor that implicates acetamido participation. J. Am. Chem. Soc. 118 (1996) 6804-6805
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6804-6805
    • Knapp, S.1    Vocadlo, D.J.2    Gao, Z.3    Kirk, B.4    Lou, J.5    Withers, S.G.6
  • 14
    • 2342542869 scopus 로고    scopus 로고
    • The effect of NAG-thiazoline on morphology and surface hydrophobicity of Escherichia coli.
    • Reid C.W., Blackburn N.T., and Clarke A.J. The effect of NAG-thiazoline on morphology and surface hydrophobicity of Escherichia coli. FEMS Microbiol. Lett. 234 (2004) 343-348
    • (2004) FEMS Microbiol. Lett. , vol.234 , pp. 343-348
    • Reid, C.W.1    Blackburn, N.T.2    Clarke, A.J.3
  • 16
    • 33144476665 scopus 로고    scopus 로고
    • Role of arginine residues in the active site of the membrane bound lytic transglycosylase B from Pseudomonas aeruginosa
    • Reid C.W., Blackburn N.T., and Clarke A.J. Role of arginine residues in the active site of the membrane bound lytic transglycosylase B from Pseudomonas aeruginosa. Biochemistry 45 (2006) 2129-2138
    • (2006) Biochemistry , vol.45 , pp. 2129-2138
    • Reid, C.W.1    Blackburn, N.T.2    Clarke, A.J.3
  • 17
    • 0027293346 scopus 로고
    • Compositional analysis of peptidoglycan by high-performance anion-exchange chromatography
    • Clarke A.J. Compositional analysis of peptidoglycan by high-performance anion-exchange chromatography. Anal. Biochem. 212 (1993) 344-350
    • (1993) Anal. Biochem. , vol.212 , pp. 344-350
    • Clarke, A.J.1
  • 18
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner B. Separation and quantification of muropeptides with high-performance liquid chromatography. Anal. Biochem. 172 (1988) 451-464
    • (1988) Anal. Biochem. , vol.172 , pp. 451-464
    • Glauner, B.1
  • 19
    • 0034633271 scopus 로고    scopus 로고
    • Assay for lytic transglycosylases: a family of peptidoglycan lyases
    • Blackburn N.T., and Clarke A.J. Assay for lytic transglycosylases: a family of peptidoglycan lyases. Anal. Biochem. 284 (2000) 388-393
    • (2000) Anal. Biochem. , vol.284 , pp. 388-393
    • Blackburn, N.T.1    Clarke, A.J.2
  • 20
    • 0028093382 scopus 로고
    • Analysis of the sodium dodecyl sulfate-stable peptidoglycan autolysins of select gram-negative pathogens by using renaturing polyacrylamide gel electrophoresis
    • Bernadsky G., Beveridge T.J., and Clarke A.J. Analysis of the sodium dodecyl sulfate-stable peptidoglycan autolysins of select gram-negative pathogens by using renaturing polyacrylamide gel electrophoresis. J. Bacteriol. 176 (1994) 5225-5232
    • (1994) J. Bacteriol. , vol.176 , pp. 5225-5232
    • Bernadsky, G.1    Beveridge, T.J.2    Clarke, A.J.3
  • 21
    • 0028132119 scopus 로고
    • Role of autolysins in the EDTA-induced lysis of Pseudomonas aeruginosa
    • Watt S.R., and Clarke A.J. Role of autolysins in the EDTA-induced lysis of Pseudomonas aeruginosa. FEMS Microbiol. Lett. 124 (1994) 113-119
    • (1994) FEMS Microbiol. Lett. , vol.124 , pp. 113-119
    • Watt, S.R.1    Clarke, A.J.2
  • 22
    • 0031453760 scopus 로고    scopus 로고
    • Isolation, purification, and characterization of the major autolysin from Pseudomonas aeruginosa
    • Watt S.R., and Clarke A.J. Isolation, purification, and characterization of the major autolysin from Pseudomonas aeruginosa. Can. J. Microbiol. 43 (1997) 1054-1062
    • (1997) Can. J. Microbiol. , vol.43 , pp. 1054-1062
    • Watt, S.R.1    Clarke, A.J.2
  • 23
    • 4944223117 scopus 로고    scopus 로고
    • Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli.
    • Ursinus A., van den Ent F., Brechtel S., de Pedro M., Höltje J.-V., Lowe J., and Vollmer W. Murein (peptidoglycan) binding property of the essential cell division protein FtsN from Escherichia coli. J. Bacteriol. 186 (2004) 6728-6737
    • (2004) J. Bacteriol. , vol.186 , pp. 6728-6737
    • Ursinus, A.1    van den Ent, F.2    Brechtel, S.3    de Pedro, M.4    Höltje, J.-V.5    Lowe, J.6    Vollmer, W.7
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of bacteriophages T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of bacteriophages T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0032584768 scopus 로고    scopus 로고
    • Substrate assistance in the mechanism of family 18 chitinases: theoretical studies of potential intermediates and inhibitors
    • Brameld K.A., Shrader W.D., Imperiali B., and Goddard III W.A. Substrate assistance in the mechanism of family 18 chitinases: theoretical studies of potential intermediates and inhibitors. J. Mol. Biol. 280 (1998) 913-923
    • (1998) J. Mol. Biol. , vol.280 , pp. 913-923
    • Brameld, K.A.1    Shrader, W.D.2    Imperiali, B.3    Goddard III, W.A.4
  • 28
    • 0037131312 scopus 로고    scopus 로고
    • Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state
    • Williams S.J., Mark B.L., Vocadlo D.J., James M.N., and Withers S.G. Aspartate 313 in the Streptomyces plicatus hexosaminidase plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. J. Biol. Chem. 277 (2002) 40055-40065
    • (2002) J. Biol. Chem. , vol.277 , pp. 40055-40065
    • Williams, S.J.1    Mark, B.L.2    Vocadlo, D.J.3    James, M.N.4    Withers, S.G.5
  • 29
    • 0034728363 scopus 로고    scopus 로고
    • Cyrstallographic studies of the interaction of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan
    • van Asselt E.J., Kalk K.H., and Dijkstra B.W. Cyrstallographic studies of the interaction of Escherichia coli lytic transglycosylase Slt35 with peptidoglycan. Biochemistry 39 (2000) 1924-1934
    • (2000) Biochemistry , vol.39 , pp. 1924-1934
    • van Asselt, E.J.1    Kalk, K.H.2    Dijkstra, B.W.3
  • 30
    • 0027240681 scopus 로고
    • Characterization of three different lytic transglycosylases from Escherichia coli
    • Romeis T., Vollmer W., and Höltje J.-V. Characterization of three different lytic transglycosylases from Escherichia coli. FEMS Microbiol. Lett. 111 (1993) 141-146
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 141-146
    • Romeis, T.1    Vollmer, W.2    Höltje, J.-V.3


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