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Volumn 581, Issue 4, 2007, Pages 693-696

The Enterococcus hirae Mur-2 enzyme displays N-acetylglucosaminidase activity

Author keywords

Autolysin; Enterococcus hirae; Mass spectrometry; N acetylglucosaminidase

Indexed keywords

ACETYLGLUCOSAMINIDASE; BACTERIAL ENZYME; CARBOHYDRATE; GLYCOSIDASE;

EID: 33846804223     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.01.033     Document Type: Article
Times cited : (4)

References (19)
  • 1
    • 84873775015 scopus 로고
    • Bagshaped macromolecules - a new outlook on bacterial cell walls
    • Weidel W., and Pelzer H. Bagshaped macromolecules - a new outlook on bacterial cell walls. Adv. Enzymol. Relat. Areas Mol. Biol. 26 (1964) 193-232
    • (1964) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.26 , pp. 193-232
    • Weidel, W.1    Pelzer, H.2
  • 2
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer K.H., and Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol. Rev. 36 (1972) 407-477
    • (1972) Bacteriol. Rev. , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 3
    • 0001904527 scopus 로고    scopus 로고
    • Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers and capsules
    • Sonenshein A.L., Hoch J.A., and Losick R. (Eds), ASM Press, Washington
    • Foster S.J., and Popham D.L. Structure and synthesis of cell wall, spore cortex, teichoic acids, S-layers and capsules. In: Sonenshein A.L., Hoch J.A., and Losick R. (Eds). Bacillus subtilis and its Closest Relatives: from Genes to Cells (2001), ASM Press, Washington 21-41
    • (2001) Bacillus subtilis and its Closest Relatives: from Genes to Cells , pp. 21-41
    • Foster, S.J.1    Popham, D.L.2
  • 4
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis: multiple enzymes with multiple functions
    • Smith T.J., Blackman S.A., and Foster S.J. Autolysins of Bacillus subtilis: multiple enzymes with multiple functions. Microbiology 146 Pt 2 (2000) 249-262
    • (2000) Microbiology , vol.146 , Issue.PART 2 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 5
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280 Pt 2 (1991) 309-316
    • (1991) Biochem. J. , vol.280 , Issue.PART 2 , pp. 309-316
    • Henrissat, B.1
  • 6
    • 17444442315 scopus 로고    scopus 로고
    • The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains
    • Garci{dotless}́a P., Paz Gonzalez M., Garci{dotless}́a E., Garci{dotless}́a J.L., and López R. The molecular characterization of the first autolytic lysozyme of Streptococcus pneumoniae reveals evolutionary mobile domains. Mol. Microbiol. 33 (1999) 128-138
    • (1999) Mol. Microbiol. , vol.33 , pp. 128-138
    • García, P.1    Paz Gonzalez, M.2    García, E.3    García, J.L.4    López, R.5
  • 7
    • 0014199545 scopus 로고
    • The N,O-diacetylmuramidase of Chalaropsis species. I. Purification and crystallization
    • Hash J.H., and Rothlauf M.V. The N,O-diacetylmuramidase of Chalaropsis species. I. Purification and crystallization. J. Biol. Chem. 242 (1967) 5586-5590
    • (1967) J. Biol. Chem. , vol.242 , pp. 5586-5590
    • Hash, J.H.1    Rothlauf, M.V.2
  • 8
    • 0030924599 scopus 로고    scopus 로고
    • Molecular characterization of a germination-specific muramidase from Clostridium perfringens S40 spores and nucleotide sequence of the corresponding gene
    • Chen Y., Miyata S., Makino S., and Moriyama R. Molecular characterization of a germination-specific muramidase from Clostridium perfringens S40 spores and nucleotide sequence of the corresponding gene. J. Bacteriol. 179 (1997) 3181-3187
    • (1997) J. Bacteriol. , vol.179 , pp. 3181-3187
    • Chen, Y.1    Miyata, S.2    Makino, S.3    Moriyama, R.4
  • 9
    • 33845460121 scopus 로고    scopus 로고
    • Functional analysis of AtlA, the major N-acetylglucosaminidase of Enterococcus faecalis
    • Eckert C., Lecerf M., Dubost L., Arthur M., and Mesnage S. Functional analysis of AtlA, the major N-acetylglucosaminidase of Enterococcus faecalis. J. Bacteriol. 188 (2006) 8513-8519
    • (2006) J. Bacteriol. , vol.188 , pp. 8513-8519
    • Eckert, C.1    Lecerf, M.2    Dubost, L.3    Arthur, M.4    Mesnage, S.5
  • 10
    • 20444471564 scopus 로고    scopus 로고
    • AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning
    • Steen A., Buist G., Horsburgh G.J., Venema G., Kuipers O.P., Foster S.J., and Kok J. AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning. Febs J. 272 (2005) 2854-2868
    • (2005) Febs J. , vol.272 , pp. 2854-2868
    • Steen, A.1    Buist, G.2    Horsburgh, G.J.3    Venema, G.4    Kuipers, O.P.5    Foster, S.J.6    Kok, J.7
  • 11
    • 0037457806 scopus 로고    scopus 로고
    • LytG of Bacillus subtilis is a novel peptidoglycan hydrolase: the major active glucosaminidase
    • Horsburgh G.J., Atrih A., Williamson M.P., and Foster S.J. LytG of Bacillus subtilis is a novel peptidoglycan hydrolase: the major active glucosaminidase. Biochemistry 42 (2003) 257-264
    • (2003) Biochemistry , vol.42 , pp. 257-264
    • Horsburgh, G.J.1    Atrih, A.2    Williamson, M.P.3    Foster, S.J.4
  • 13
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman A., and Bycroft M. The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J. Mol. Biol. 299 (2000) 1113-1119
    • (2000) J. Mol. Biol. , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 14
    • 0024406463 scopus 로고
    • The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin
    • Dolinger D.L., Daneo-Moore L., and Shockman G.D. The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin. J. Bacteriol. 171 (1989) 4355-4361
    • (1989) J. Bacteriol. , vol.171 , pp. 4355-4361
    • Dolinger, D.L.1    Daneo-Moore, L.2    Shockman, G.D.3
  • 15
    • 0028798788 scopus 로고
    • Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL
    • Amrein K.E., Takacs B., Stieger M., Molnos J., Flint N.A., and Burn P. Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL. Proc. Natl. Acad. Sci. USA 92 (1995) 1048-1052
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1048-1052
    • Amrein, K.E.1    Takacs, B.2    Stieger, M.3    Molnos, J.4    Flint, N.A.5    Burn, P.6
  • 18
    • 0020507038 scopus 로고
    • Evidence for the presence of a second peptidoglycan hydrolase in Streptococcus faecium
    • Kawamura T., and Shockman G.D. Evidence for the presence of a second peptidoglycan hydrolase in Streptococcus faecium. FEMS Microbiol. Lett. 19 (1983) 65-69
    • (1983) FEMS Microbiol. Lett. , vol.19 , pp. 65-69
    • Kawamura, T.1    Shockman, G.D.2
  • 19
    • 0014268381 scopus 로고
    • Structure of the cell walls of Micrococcus lysodeikticus. 3. Isolation of a new peptide dimer, N-alpha-[l-alanyl-gamma-(alpha-d-glutamylglycine)]-l-lysyl-d-alanyl-N-alpha-[l-alanyl-gamma-(alpha-d-glutamylglycine)]-l-lysyl-d-alanine
    • Ghuysen J.M., Bricas E., Lache M., and Leyh-Bouille M. Structure of the cell walls of Micrococcus lysodeikticus. 3. Isolation of a new peptide dimer, N-alpha-[l-alanyl-gamma-(alpha-d-glutamylglycine)]-l-lysyl-d-alanyl-N-alpha-[l-alanyl-gamma-(alpha-d-glutamylglycine)]-l-lysyl-d-alanine. Biochemistry 7 (1968) 1450-1460
    • (1968) Biochemistry , vol.7 , pp. 1450-1460
    • Ghuysen, J.M.1    Bricas, E.2    Lache, M.3    Leyh-Bouille, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.