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Volumn 145, Issue 1, 1999, Pages 169-176

Partial characterization of a major autolysin from Mycobacterium phlei

Author keywords

Autolysin; Mycobacterium phlei; glycosidase

Indexed keywords

BACTERIAL ENZYME; DIETHYLAMINOETHYL CELLULOSE; GLYCOSIDASE;

EID: 0032945311     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/13500872-145-1-169     Document Type: Article
Times cited : (4)

References (35)
  • 1
    • 0003003336 scopus 로고
    • Metabolism of mycobacteria in tissues
    • Edited by J. Stanford & J. M. Grange. London: Academic Press
    • Barclay, R. & Wheeler, P. R. (1989). Metabolism of mycobacteria in tissues. In The Biology of the Mycobacteria, vol 3, pp. 37-106. Edited by J. Stanford & J. M. Grange. London: Academic Press.
    • (1989) The Biology of the Mycobacteria , vol.3 , pp. 37-106
    • Barclay, R.1    Wheeler, P.R.2
  • 2
    • 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. & Clarke, A. J. (1994). Analysis of the sodium dodecyl sulfate-stable peptidoglycan autolysins of select gram-negative pathogens by using renaturing polyacrylamide gel electrophoresis. J Bacteriol 176, 5225-5232.
    • (1994) J Bacteriol , vol.176 , pp. 5225-5232
    • Bernadsky, G.1    Beveridge, T.J.2    Clarke, A.J.3
  • 3
    • 0026605558 scopus 로고
    • O-acetylated peptidoglycan: Its occurrence, pathobiological significance, and biosynthesis
    • Clarke, A. J. & Dupont, C. (1992). O-acetylated peptidoglycan: its occurrence, pathobiological significance, and biosynthesis. Can J Microbiol 38, 85-91.
    • (1992) Can J Microbiol , vol.38 , pp. 85-91
    • Clarke, A.J.1    Dupont, C.2
  • 4
    • 0024406463 scopus 로고
    • The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin
    • Dolinger, D. L., Daneo-Moore, L. & Shockman, G. D. (1989). The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin. J Bacteriol 171, 4355-4361.
    • (1989) J Bacteriol , vol.171 , pp. 4355-4361
    • Dolinger, D.L.1    Daneo-Moore, L.2    Shockman, G.D.3
  • 5
    • 0018755706 scopus 로고
    • Immunosuppression by mycobacterial arabinomannan
    • Ellner, J. J. & Daniel, T. M. (1979). Immunosuppression by mycobacterial arabinomannan. Clin Exp Immunol 35, 250-257.
    • (1979) Clin Exp Immunol , vol.35 , pp. 250-257
    • Ellner, J.J.1    Daniel, T.M.2
  • 6
    • 0026512822 scopus 로고
    • Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis
    • Foster, S. J. (1992). Analysis of the autolysins of Bacillus subtilis 168 during vegetative growth and differentiation by using renaturing polyacrylamide gel electrophoresis. J Bacteriol 174, 464-470.
    • (1992) J Bacteriol , vol.174 , pp. 464-470
    • Foster, S.J.1
  • 7
    • 0017694128 scopus 로고
    • Enzymes synthesizing and hydrolyzmg murein in Escherichia coli
    • Goodell, E. W. & Schwarte, U. (1977). Enzymes synthesizing and hydrolyzmg murein in Escherichia coli. Eur J Biochem 81, 205-210.
    • (1977) Eur J Biochem , vol.81 , pp. 205-210
    • Goodell, E.W.1    Schwarte, U.2
  • 8
    • 0002725473 scopus 로고
    • Mycobacterial lipids: Chemistry and biologic activities
    • Edited by G. P. Youmans. Philadelphia, PA: W. B. Saunders
    • Goren, M.B. & Brennan, P. J. (1979). Mycobacterial lipids: chemistry and biologic activities. In Tuberculosis, pp. 69-193. Edited by G. P. Youmans. Philadelphia, PA: W. B. Saunders.
    • (1979) Tuberculosis , pp. 69-193
    • Goren, M.B.1    Brennan, P.J.2
  • 10
    • 0021233596 scopus 로고
    • Attachment of pneumococcal autolysin to wall teichoic acids, an essential step in enzymatic wall degradation
    • Guidicelli, S. & Tomasz, A. (1984). Attachment of pneumococcal autolysin to wall teichoic acids, an essential step in enzymatic wall degradation. J Bacteriol 158, 1188-1190.
    • (1984) J Bacteriol , vol.158 , pp. 1188-1190
    • Guidicelli, S.1    Tomasz, A.2
  • 11
    • 0029783598 scopus 로고    scopus 로고
    • Molecular interplay of murein synthases and murein hydrolases in Escherichia coli
    • Höltje, J.-V. (1996). Molecular interplay of murein synthases and murein hydrolases in Escherichia coli. Microb Drug Resist 2, 99-103.
    • (1996) Microb Drug Resist , vol.2 , pp. 99-103
    • Höltje, J.-V.1
  • 12
    • 0037858060 scopus 로고    scopus 로고
    • Growth of the stress-hearing and shape-maintaining murein sacculus of Escherichia coli
    • Höltje, J.-V. (1998). Growth of the stress-hearing and shape-maintaining murein sacculus of Escherichia coli. Microbiol Mol Biol Rev 62, 181-203.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 181-203
    • Höltje, J.-V.1
  • 13
    • 0021346578 scopus 로고
    • Metal binding by the peptidoglycan sacculus of Escherichia coli K-12
    • Hoyle, B.D. & Beveridge, T. J. (1984). Metal binding by the peptidoglycan sacculus of Escherichia coli K-12. Can J Microbiol 30, 204-211.
    • (1984) Can J Microbiol , vol.30 , pp. 204-211
    • Hoyle, B.D.1    Beveridge, T.J.2
  • 14
    • 0024592506 scopus 로고
    • Isolation and characterization of the highly immunological cell wall-associated protein of Mycobacterium leprae
    • Hunter, S. W., McNeil, M., Modlin, R. L., Mehra, V., Bloom, B. R. & Brennan, P. J. (1989). Isolation and characterization of the highly immunological cell wall-associated protein of Mycobacterium leprae. J Immunol 142, 2864-2872.
    • (1989) J Immunol , vol.142 , pp. 2864-2872
    • Hunter, S.W.1    McNeil, M.2    Modlin, R.L.3    Mehra, V.4    Bloom, B.R.5    Brennan, P.J.6
  • 15
    • 0017350437 scopus 로고
    • Characterization of autolysins from Mycobacterium smegmatis
    • Kilburn, J. O. & Best, G. K. (1977). Characterization of autolysins from Mycobacterium smegmatis. J Bacteriol 29, 750-755.
    • (1977) J Bacteriol , vol.29 , pp. 750-755
    • Kilburn, J.O.1    Best, G.K.2
  • 16
    • 0025346080 scopus 로고
    • Additional arguments for the key role of 'smart' autolysins in the enlargement of the wall of gram-negative bacteria
    • Koch, A. L. (1990). Additional arguments for the key role of 'smart' autolysins in the enlargement of the wall of gram-negative bacteria. Res Microbiol 141, 529-541.
    • (1990) Res Microbiol , vol.141 , pp. 529-541
    • Koch, A.L.1
  • 17
    • 0017736277 scopus 로고
    • Carbohydrate determination with 4-hydroxybenzoic acid hydrazide (PAHBAH): Effect of bismuth on the reaction
    • Lever, M. (1972). Carbohydrate determination with 4-hydroxybenzoic acid hydrazide (PAHBAH): effect of bismuth on the reaction. Anal Biochem 81, 21-27.
    • (1972) Anal Biochem , vol.81 , pp. 21-27
    • Lever, M.1
  • 18
    • 0027146367 scopus 로고
    • A species-specific periplasmic flagella protein of Serpulina (Treponema) hyodysenteriae
    • Li, Z. S., Dumas, F., Dubreuil, D. & Jacques, M. (1993). A species-specific periplasmic flagella protein of Serpulina (Treponema) hyodysenteriae. J Bacteriol 175, 8000-8007.
    • (1993) J Bacteriol , vol.175 , pp. 8000-8007
    • Li, Z.S.1    Dumas, F.2    Dubreuil, D.3    Jacques, M.4
  • 19
    • 0030002937 scopus 로고    scopus 로고
    • A major autolysin of Pseudomonas aeruginosa: Subcellular distribution, potential role in cell growth and division, and secretion in surface membrane vesicles
    • Li, Z. S., Clarke, A. J. & Beveridge, T. J. (1996). A major autolysin of Pseudomonas aeruginosa: subcellular distribution, potential role in cell growth and division, and secretion in surface membrane vesicles. J Bacteriol 178, 2479-2488.
    • (1996) J Bacteriol , vol.178 , pp. 2479-2488
    • Li, Z.S.1    Clarke, A.J.2    Beveridge, T.J.3
  • 20
    • 0023696905 scopus 로고
    • The inhibitory effects of mycobacterial lipoarabinomannan and polysaccharides upon polyclonal and monoclonal human T cell proliferation
    • Moreno, C., Mehlert, A. & Lamb, J. (1988). The inhibitory effects of mycobacterial lipoarabinomannan and polysaccharides upon polyclonal and monoclonal human T cell proliferation. Clin Exp Immunol 74, 206-210.
    • (1988) Clin Exp Immunol , vol.74 , pp. 206-210
    • Moreno, C.1    Mehlert, A.2    Lamb, J.3
  • 21
    • 0026655895 scopus 로고
    • Re-evaluation of envelope profiles and cytoplasmic ultrastructure of mycobacteria processed by conventional embedding and freeze-substitution protocols
    • Paul, T. R. & Beveridge, T. J. (1992). Re-evaluation of envelope profiles and cytoplasmic ultrastructure of mycobacteria processed by conventional embedding and freeze-substitution protocols. J Bacteriol 174, 6508-6517.
    • (1992) J Bacteriol , vol.174 , pp. 6508-6517
    • Paul, T.R.1    Beveridge, T.J.2
  • 22
    • 0028327368 scopus 로고
    • Preservation of surface lipids and determination of ultrastructure of Mycobacterium kansasii by freeze-substitution
    • Paul, T. R. & Beveridge, T. J. (1994). Preservation of surface lipids and determination of ultrastructure of Mycobacterium kansasii by freeze-substitution. Infect Immun 62, 1542-1550.
    • (1994) Infect Immun , vol.62 , pp. 1542-1550
    • Paul, T.R.1    Beveridge, T.J.2
  • 23
    • 0042478238 scopus 로고
    • The structure of the mycobacterial cell wall
    • Edited by G. P. Kubica & L. G. Wayne. New York : Marcel Dekker
    • Petit, J.-F. & Lederer, E. (1984). The structure of the mycobacterial cell wall. In The Mycobacteria, part A, pp. 301-313. Edited by G. P. Kubica & L. G. Wayne. New York : Marcel Dekker.
    • (1984) The Mycobacteria , Issue.PART A , pp. 301-313
    • Petit, J.-F.1    Lederer, E.2
  • 24
    • 0025033435 scopus 로고
    • The carbohydrate-and lipid-containing cell wall of mycobacteria, phenolic glycolipids: Structure and immunological properties
    • Puzo, G. (1990). The carbohydrate-and lipid-containing cell wall of mycobacteria, phenolic glycolipids: structure and immunological properties. Crit Rev Microbiol 17, 1101-1120.
    • (1990) Crit Rev Microbiol , vol.17 , pp. 1101-1120
    • Puzo, G.1
  • 25
    • 0023473794 scopus 로고
    • Rapid isoelectric focusing in vertical polyacrylamide minigel system
    • Robertson, E. F., Dannelly, H. K., Malloy, P. J. & Reeves, H. C. (1987). Rapid isoelectric focusing in vertical polyacrylamide minigel system. Anal Biochem 167, 290-294.
    • (1987) Anal Biochem , vol.167 , pp. 290-294
    • Robertson, E.F.1    Dannelly, H.K.2    Malloy, P.J.3    Reeves, H.C.4
  • 26
    • 0003122522 scopus 로고
    • The bacterial autolysins
    • Edited by H. J. Rogers, H. R. Perkins & J. B. Ward. London: Chapman & Hall
    • Rogers, H. J., Perkins, H. R. & Ward, J. B. (1980). The bacterial autolysins. In Microbial Cell Walls and Membranes, pp. 437-460. Edited by H. J. Rogers, H. R. Perkins & J. B. Ward. London: Chapman & Hall.
    • (1980) Microbial Cell Walls and Membranes , pp. 437-460
    • Rogers, H.J.1    Perkins, H.R.2    Ward, J.B.3
  • 27
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer, K. H. & Kandier, O. (1972). Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev 36, 407-471.
    • (1972) Bacteriol Rev , vol.36 , pp. 407-471
    • Schleifer, K.H.1    Kandier, O.2
  • 28
    • 0014674516 scopus 로고
    • Autolytic enzymes and cell division of Escherichia coli
    • Schwarte, U., Asmus, A. & Frank, H. (1969). Autolytic enzymes and cell division of Escherichia coli. J Mol Biol 41, 419-429.
    • (1969) J Mol Biol , vol.41 , pp. 419-429
    • Schwarte, U.1    Asmus, A.2    Frank, H.3
  • 29
    • 77956866741 scopus 로고
    • Microbial peptidoglycan (murein) hydrolases
    • Edited by J.-M. Ghuysen & R. Hakenbeck. Amsterdam: Elsevier
    • Shockman, G. D. & Höltje, J.-V. (1994). Microbial peptidoglycan (murein) hydrolases. In Bacterial Cell Wall, pp. 131-166. Edited by J.-M. Ghuysen & R. Hakenbeck. Amsterdam: Elsevier.
    • (1994) Bacterial Cell Wall , pp. 131-166
    • Shockman, G.D.1    Höltje, J.-V.2
  • 31
    • 0002249336 scopus 로고
    • Building and breaking of bonds in the cell wall of bacteria - The role for aurolysin
    • Edited by C. Nombela. Amsterdam: Elsevier
    • Tomasz, A. (1984). Building and breaking of bonds in the cell wall of bacteria - the role for aurolysin. In Microbial Cell Wall Synthesis and Autolysis, pp. 3-12. Edited by C. Nombela. Amsterdam: Elsevier.
    • (1984) Microbial Cell Wall Synthesis and Autolysis , pp. 3-12
    • Tomasz, A.1
  • 32
    • 0028075008 scopus 로고
    • Initial characterization of two extracellular autolysins from Pseudomonas aeruginosa PAO1
    • Watt, S. R. & Clarke, A. J. (1994). Initial characterization of two extracellular autolysins from Pseudomonas aeruginosa PAO1. J Bacteriol 176, 19-24.
    • (1994) J Bacteriol , vol.176 , pp. 19-24
    • Watt, S.R.1    Clarke, A.J.2
  • 33
    • 0031453760 scopus 로고    scopus 로고
    • Isolation, purification and characterization of the major autolysin from Pseudomonas aeruginosa
    • Watt, S. R. & Clarke, A. J. (1997). Isolation, purification and characterization of the major autolysin from Pseudomonas aeruginosa. Can J Microbiol 43, 1054-1062.
    • (1997) Can J Microbiol , vol.43 , pp. 1054-1062
    • Watt, S.R.1    Clarke, A.J.2
  • 34
    • 0016209670 scopus 로고
    • Occurrence of D-alanyl-D-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in mycobacteria
    • Wietzerbin, J., Das, B. C., Petit, J. F., Lederer, E., Leyh-Bouille, M. & Ghuysen, J.-M. (1974). Occurrence of D-alanyl-D-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in mycobacteria. Biochemistry 13, 3471-3476.
    • (1974) Biochemistry , vol.13 , pp. 3471-3476
    • Wietzerbin, J.1    Das, B.C.2    Petit, J.F.3    Lederer, E.4    Leyh-Bouille, M.5    Ghuysen, J.-M.6
  • 35
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm, M., Shevchenko, A., Houthaeve, T., Breit S., Schweigerer, L., Fotsis, T. & Mann, M. (1996). Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379, 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7


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