메뉴 건너뛰기




Volumn 181, Issue 19, 1999, Pages 5909-5914

Expression of the Staphylococcus aureus UDP-N-acetylmuramoyl-L-alanyl-D- glutamate:L-lysine ligase in Escherichia coli and effects on peptidoglycan biosynthesis and cell growth

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CARBOXYL GROUP; DEXTRO ALANINE; DIMER; LIGASE; MONOMER; PEPTIDOGLYCAN;

EID: 0032823023     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.19.5909-5914.1999     Document Type: Article
Times cited : (56)

References (33)
  • 1
    • 0030471790 scopus 로고    scopus 로고
    • Kinetic mechanism of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme: Use of a glutathione S-transferase fusion
    • Anderson, M. S., S. S. Eveland, H. R. Onishi, and D. L. Pompliano. 1996. Kinetic mechanism of the Escherichia coli UDP-MurNAc-tripeptide D-alanyl-D-alanine-adding enzyme: use of a glutathione S-transferase fusion. Biochemistry 35:16264-16269.
    • (1996) Biochemistry , vol.35 , pp. 16264-16269
    • Anderson, M.S.1    Eveland, S.S.2    Onishi, H.R.3    Pompliano, D.L.4
  • 3
    • 0030570736 scopus 로고    scopus 로고
    • Effect of analogs of diaminopimelic acid on the meso-diaminopimelate-adding enzyme from Escherichia coli
    • Auger, G., J. van Heijenoort, J. C. Vederas, and D. Blanot. 1996. Effect of analogs of diaminopimelic acid on the meso-diaminopimelate-adding enzyme from Escherichia coli. FEBS Lett. 391:171-174.
    • (1996) FEBS Lett. , vol.391 , pp. 171-174
    • Auger, G.1    Van Heijenoort, J.2    Vederas, J.C.3    Blanot, D.4
  • 4
    • 0014594651 scopus 로고
    • Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure
    • Braun, V., and K. Rehn. 1969. Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure. Eur. J. Biochem. 10:426-438.
    • (1969) Eur. J. Biochem. , vol.10 , pp. 426-438
    • Braun, V.1    Rehn, K.2
  • 5
    • 0026073599 scopus 로고
    • Identification of vancomycin resistance protein VanA as a D-alanine: D-alanine ligase of altered substrate specificity
    • Bugg, T. D. H., S. Dutka-Malen, M. Arthur, P. Courvalin, and C. T. Walsh. 1991. Identification of vancomycin resistance protein VanA as a D-alanine: D-alanine ligase of altered substrate specificity. Biochemistry 30:2017-2021.
    • (1991) Biochemistry , vol.30 , pp. 2017-2021
    • Bugg, T.D.H.1    Dutka-Malen, S.2    Arthur, M.3    Courvalin, P.4    Walsh, C.T.5
  • 6
    • 0026795665 scopus 로고
    • Effect of D-amino acids on structure and synthesis of peptidoglycan in Escherichia coli
    • Caparrós, M., A. G. Pisabarro, and M. A. de Pedro. 1992. Effect of D-amino acids on structure and synthesis of peptidoglycan in Escherichia coli. J. Bacteriol. 174:5549-5559.
    • (1992) J. Bacteriol. , vol.174 , pp. 5549-5559
    • Caparrós, M.1    Pisabarro, A.G.2    De Pedro, M.A.3
  • 7
    • 0016252331 scopus 로고
    • Growth and cell division of Escherichia coli 173-25 in the presence of some analogs of diaminopimelic acid
    • Chaloupka, J., M. Strnadová, J. Caslavská, and K. Vereš. 1974. Growth and cell division of Escherichia coli 173-25 in the presence of some analogs of diaminopimelic acid. Z. Allg. Mikrobiol. 14:283-296.
    • (1974) Z. Allg. Mikrobiol. , vol.14 , pp. 283-296
    • Chaloupka, J.1    Strnadová, M.2    Caslavská, J.3    Vereš, K.4
  • 8
    • 0026639828 scopus 로고
    • Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain
    • de Jonge, B. L. M., V.-S. Chang, D. Gage, and A. Tomasz. 1992. Peptidoglycan composition of a highly methicillin-resistant Staphylococcus aureus strain. J. Biol. Chem. 267:11248-11254.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11248-11254
    • De Jonge, B.L.M.1    Chang, V.-S.2    Gage, D.3    Tomasz, A.4
  • 9
    • 0019578458 scopus 로고
    • Reverse-phase high pressure liquid chromatography of uridine diphosphate N-acetylmuramyl peptide precursors of bacterial cell wall peptidoglycan
    • Flouret, B., D. Mengin-Lecreulx, and J. van Heijenoort. 1981. Reverse-phase high pressure liquid chromatography of uridine diphosphate N-acetylmuramyl peptide precursors of bacterial cell wall peptidoglycan. Anal. Biochem. 114:59-63.
    • (1981) Anal. Biochem. , vol.114 , pp. 59-63
    • Flouret, B.1    Mengin-Lecreulx, D.2    Van Heijenoort, J.3
  • 10
    • 0023765918 scopus 로고
    • Separation and quantification of muropeptides with high-performance liquid chromatography
    • Glauner, B. 1988. Separation and quantification of muropeptides with high-performance liquid chromatography. Anal. Biochem. 172:451-464.
    • (1988) Anal. Biochem. , vol.172 , pp. 451-464
    • Glauner, B.1
  • 11
    • 0023677844 scopus 로고
    • The composition of the murein from Escherichia coli
    • Glauner, B., J.-V. Höltje, and U. Schwarz. 1988. The composition of the murein from Escherichia coli. J. Biol. Chem. 263:10088-10095.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10088-10095
    • Glauner, B.1    Höltje, J.-V.2    Schwarz, U.3
  • 12
    • 0016186332 scopus 로고
    • On the specificity of phospho-N-acetylmuramyl-pentapeptide translocase. The peptide subunit of uridine diphosphate-N-acetylmuramyl-pentapeptide
    • Hammes, W. P., and F. C. Neuhaus. 1974. On the specificity of phospho-N-acetylmuramyl-pentapeptide translocase. The peptide subunit of uridine diphosphate-N-acetylmuramyl-pentapeptide. J. Biol. Chem. 249:3140-3150.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3140-3150
    • Hammes, W.P.1    Neuhaus, F.C.2
  • 13
    • 0001625196 scopus 로고
    • Enzymatic synthesis of the peptide in bacterial uridine nucleotides. III. Purification and properties of L-lysine-adding enzyme
    • Ito, E., and J. L. Strominger. 1964. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. III. Purification and properties of L-lysine-adding enzyme. J. Biol. Chem. 239:210-214.
    • (1964) J. Biol. Chem. , vol.239 , pp. 210-214
    • Ito, E.1    Strominger, J.L.2
  • 14
    • 0015919757 scopus 로고
    • Enzymatic synthesis of the peptide in bacterial uridine nucleotides. VII. Comparative biochemistry
    • Ito, E., and J. L. Strominger. 1973. Enzymatic synthesis of the peptide in bacterial uridine nucleotides. VII. Comparative biochemistry. J. Biol. Chem. 248:3131-3136.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3131-3136
    • Ito, E.1    Strominger, J.L.2
  • 15
    • 77956844354 scopus 로고
    • Bacterial peptidoglycan: Overview and evolving concepts
    • J.-M. Ghuysen and R. Hakenbeck (ed.), Elsevier Science B.V., Amsterdam, The Netherlands
    • Labischinski, H., and H. Maidhof. 1994. Bacterial peptidoglycan: overview and evolving concepts, p. 23-38. In J.-M. Ghuysen and R. Hakenbeck (ed.), Bacterial cell wall. New comprehensive biochemistry, vol. 27. Elsevier Science B.V., Amsterdam, The Netherlands.
    • (1994) Bacterial Cell Wall. New Comprehensive Biochemistry , vol.27 , pp. 23-38
    • Labischinski, H.1    Maidhof, H.2
  • 16
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4
    • Laemmli, U. K., and M. Favre. 1973. Maturation of the head of bacteriophage T4. J. Mol. Biol. 80:575-599.
    • (1973) J. Mol. Biol. , vol.80 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 18
    • 0028361885 scopus 로고
    • Replacement of diaminopimelic acid by cystathionine or lanthionine in the peptidoglycan of Escherichia coli
    • Mengin-Lecreulx, D., D. Blanot, and J. van Heijenoort. 1994. Replacement of diaminopimelic acid by cystathionine or lanthionine in the peptidoglycan of Escherichia coli. J. Bacteriol. 176:4321-4327.
    • (1994) J. Bacteriol. , vol.176 , pp. 4321-4327
    • Mengin-Lecreulx, D.1    Blanot, D.2    Van Heijenoort, J.3
  • 19
    • 0020458828 scopus 로고
    • Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli
    • Mengin-Lecreulx, D., B. Flouret, and J. van Heijenoort. 1982. Cytoplasmic steps of peptidoglycan synthesis in Escherichia coli. J. Bacteriol. 151:1109-1117.
    • (1982) J. Bacteriol. , vol.151 , pp. 1109-1117
    • Mengin-Lecreulx, D.1    Flouret, B.2    Van Heijenoort, J.3
  • 20
    • 0020560713 scopus 로고
    • Pool levels of UDP-N-acetylglucosamine and UDP-N-acetylglucosamine-enolpyruvate in Escherichia coli and correlation with peptidoglycan synthesis
    • Mengin-Lecreulx, D., B. Flouret, and J. van Heijenoort. 1983. Pool levels of UDP-N-acetylglucosamine and UDP-N-acetylglucosamine-enolpyruvate in Escherichia coli and correlation with peptidoglycan synthesis. J. Bacteriol. 154:1284-1290.
    • (1983) J. Bacteriol. , vol.154 , pp. 1284-1290
    • Mengin-Lecreulx, D.1    Flouret, B.2    Van Heijenoort, J.3
  • 21
    • 0023949796 scopus 로고
    • Incorporation of LL-diaminopimelic acid into peptidoglycan of Escherichia coli mutants lacking diaminopimelate epimerase encoded by dapF
    • Mengin-Lecreulx, D., C. Michaud, C. Richaud, D. Blanot, and J. van Heijenoort 1988. Incorporation of LL-diaminopimelic acid into peptidoglycan of Escherichia coli mutants lacking diaminopimelate epimerase encoded by dapF. J. Bacteriol. 170:2031-2039.
    • (1988) J. Bacteriol. , vol.170 , pp. 2031-2039
    • Mengin-Lecreulx, D.1    Michaud, C.2    Richaud, C.3    Blanot, D.4    Van Heijenoort, J.5
  • 22
    • 0022257611 scopus 로고
    • Effect of growth conditions on peptidoglycan content and cytoplasmic steps of its biosynthesis in Escherichia coli
    • Mengin-Lecreulx, D., and J. van Heijenoort. 1985. Effect of growth conditions on peptidoglycan content and cytoplasmic steps of its biosynthesis in Escherichia coli. J. Bacteriol. 163:208-212.
    • (1985) J. Bacteriol. , vol.163 , pp. 208-212
    • Mengin-Lecreulx, D.1    Van Heijenoort, J.2
  • 23
    • 0023643132 scopus 로고
    • Partial purification and specificity studies of the D-glutamate-adding and D-alanyl-D-alanine-adding enzymes from Escherichia coli
    • Michaud, C., D. Blanot, B. Flouret, and J. van Heijenoort. 1987. Partial purification and specificity studies of the D-glutamate-adding and D-alanyl-D-alanine-adding enzymes from Escherichia coli. Eur. J. Biochem. 166:631-637.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 631-637
    • Michaud, C.1    Blanot, D.2    Flouret, B.3    Van Heijenoort, J.4
  • 24
    • 0025688726 scopus 로고
    • Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramoyl-L-alanyl-D-glutamate: Meso-2,6-diaminopimelate ligase from Escherichia coli
    • Michaud, C., D. Mengin-Lecreulx, J. van Heijenoort, and D. Blanot. 1990. Over-production, purification and properties of the uridine-diphosphate-N-acetylmuramoyl-L-alanyl-D-glutamate: meso-2,6-diaminopimelate ligase from Escherichia coli. Eur. J. Biochem. 194:853-861.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 853-861
    • Michaud, C.1    Mengin-Lecreulx, D.2    Van Heijenoort, J.3    Blanot, D.4
  • 25
  • 26
    • 0014429555 scopus 로고
    • Purification and properties of uridine diphosphate N-acetylmuramyl-L-alanyl-D-glutamate: Meso-2,6-diaminopimelate ligase
    • Mizuno, Y., and E. Ito. 1968. Purification and properties of uridine diphosphate N-acetylmuramyl-L-alanyl-D-glutamate: meso-2,6-diaminopimelate ligase. J. Biol. Chem. 243:2665-2672.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2665-2672
    • Mizuno, Y.1    Ito, E.2
  • 27
    • 0001855145 scopus 로고
    • Diaminopimelate and lysine
    • K. M. Herrmann and R. L. Somerville (ed.), Addison-Wesley Publishing Co., Reading, Mass.
    • Patte, J.-C. 1983. Diaminopimelate and lysine, p. 213-228. In K. M. Herrmann and R. L. Somerville (ed.), Amino acids: biosynthesis and genetic regulation. Addison-Wesley Publishing Co., Reading, Mass.
    • (1983) Amino Acids: Biosynthesis and Genetic Regulation , pp. 213-228
    • Patte, J.-C.1
  • 28
    • 0027772882 scopus 로고
    • Directed evolution of biosynthetic pathways. Recruitment of cysteine thioethers for construeting the cell wall of Escherichia coli
    • Richaud, C., D. Mengin-Lecreulx, S. Pochet, E. J. Johnson, G. N. Cohen, and P. Marlière. 1993. Directed evolution of biosynthetic pathways. Recruitment of cysteine thioethers for construeting the cell wall of Escherichia coli. J. Biol. Chem. 268:26827-26835.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26827-26835
    • Richaud, C.1    Mengin-Lecreulx, D.2    Pochet, S.3    Johnson, E.J.4    Cohen, G.N.5    Marlière, P.6
  • 30
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell-walls and their taxonomic implications
    • Schleifer, K. H., and O. Kandler. 1972. Peptidoglycan types of bacterial cell-walls and their taxonomic implications. Bacteriol. Rev. 36:407-477.
    • (1972) Bacteriol. Rev. , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 31
    • 0017229189 scopus 로고
    • Purification and properties of a protein factor stimulating peptidoglycan synthesis in toluene-and LiCl-treated Bacillus megaterium cells
    • Taku, A., and D. P. Fan. 1976. Purification and properties of a protein factor stimulating peptidoglycan synthesis in toluene-and LiCl-treated Bacillus megaterium cells. J. Biol. Chem. 251:1889-1895.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1889-1895
    • Taku, A.1    Fan, D.P.2
  • 32
    • 0000996675 scopus 로고    scopus 로고
    • Murein synthesis
    • F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • van Heijenoort, J. 1996. Murein synthesis, p. 1025-1034. In F. C. Neidhardt, R. Curtis III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella, 2nd ed. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia coli and Salmonella, 2nd Ed. , pp. 1025-1034
    • Van Heijenoort, J.1
  • 33
    • 0011807302 scopus 로고
    • Contribution à l'étude des isomères de l'acide α,α′-diaminopimélique
    • van Heijenoort, J., and E. Bricas. 1968. Contribution à l'étude des isomères de l'acide α,α′-diaminopimélique. Bull. Soc. Chim. Fr. 7:2828-2831.
    • (1968) Bull. Soc. Chim. Fr. , vol.7 , pp. 2828-2831
    • Van Heijenoort, J.A.1    Bricas, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.