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Volumn 235, Issue 3, 1996, Pages 601-605

Construction of a multifunctional pneumococcal murein hydrolase by module assembly

Author keywords

Cell wall; Chimeric enzymes; Domain fusions; Molecular evolution

Indexed keywords

CHIMERIC PROTEIN; HYDROLASE; PEPTIDOGLYCAN HYDROLASE; UNCLASSIFIED DRUG;

EID: 0030049811     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00601.x     Document Type: Article
Times cited : (10)

References (32)
  • 1
    • 0025037846 scopus 로고
    • Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages
    • García, P., García, J. L., García, E. & López, R. (1990) Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages, Gene (Amst.) 86, 81-88.
    • (1990) Gene (Amst.) , vol.86 , pp. 81-88
    • García, P.1    García, J.L.2    García, E.3    López, R.4
  • 2
    • 0025288833 scopus 로고
    • Cloning and expression of gene fragments encoding the choline-binding domain of the pneumococcal murein hydrolases
    • Sánchez-Puelles, J. M., Sanz, J. M., García, J. L. & García, E. (1990) Cloning and expression of gene fragments encoding the choline-binding domain of the pneumococcal murein hydrolases, Gene (Amst.) 89, 69-75.
    • (1990) Gene (Amst.) , vol.89 , pp. 69-75
    • Sánchez-Puelles, J.M.1    Sanz, J.M.2    García, J.L.3    García, E.4
  • 3
    • 0026546261 scopus 로고
    • Studies on the structure and function of the N-terminal domain of the pneumococcal murein hydrolases
    • Sanz, J. M., Díaz, E. & García, J. L. (1992) Studies on the structure and function of the N-terminal domain of the pneumococcal murein hydrolases, Mol. Microbiol. 6, 921-931.
    • (1992) Mol. Microbiol. , vol.6 , pp. 921-931
    • Sanz, J.M.1    Díaz, E.2    García, J.L.3
  • 4
    • 0025186362 scopus 로고
    • Chimeric phage-bacterial enzymes, a clue in the molecular evolution of genes
    • Díaz, E., López, R. & García, J. L. (1990) Chimeric phage-bacterial enzymes, a clue in the molecular evolution of genes, Proc. Natl Acad. Sci. USA 87, 8125-8129.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 8125-8129
    • Díaz, E.1    López, R.2    García, J.L.3
  • 5
    • 0027121406 scopus 로고
    • Structural analysis and biological significance of the cell wall lytic enzymes of Streptococcus pneumoniae and its bacteriophages
    • López, R., García, J. L., García, E., Ronda, C. & García, P. (1992) Structural analysis and biological significance of the cell wall lytic enzymes of Streptococcus pneumoniae and its bacteriophages, FEMS Microbiol. Lett. 100, 439-448.
    • (1992) FEMS Microbiol. Lett. , vol.100 , pp. 439-448
    • López, R.1    García, J.L.2    García, E.3    Ronda, C.4    García, P.5
  • 6
    • 0024295204 scopus 로고
    • Structural requirements of choline derivatives for 'conversion' of pneumococcal amidase
    • Sanz, J. M., López, R. & García, J. L. (1988) Structural requirements of choline derivatives for 'conversion' of pneumococcal amidase, FEBS Lett. 232, 308-312.
    • (1988) FEBS Lett. , vol.232 , pp. 308-312
    • Sanz, J.M.1    López, R.2    García, J.L.3
  • 7
    • 0026518485 scopus 로고
    • Immobilization and single-step purification of fusion proteins using DEAE-cellulose
    • Sánchez-Puelles, J. M., Sanz, J. M., García, J. L. & García, E. (1992) Immobilization and single-step purification of fusion proteins using DEAE-cellulose, Eur. J. Biochem. 203, 153-159.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 153-159
    • Sánchez-Puelles, J.M.1    Sanz, J.M.2    García, J.L.3    García, E.4
  • 9
    • 0017155116 scopus 로고
    • Purification of the pneumococcal N-acetylmuramyl-L-alanine amidase to biochemical homogeneity
    • Höltje, J.-V. & Tomasz, A. (1976) Purification of the pneumococcal N-acetylmuramyl-L-alanine amidase to biochemical homogeneity, J. Biol. Chem. 251, 4199-4207.
    • (1976) J. Biol. Chem. , vol.251 , pp. 4199-4207
    • Höltje, J.-V.1    Tomasz, A.2
  • 10
    • 0025768057 scopus 로고
    • Multienzyme systems obtained by gene fusion
    • Bülow, L. & Mosbach, K. (1991) Multienzyme systems obtained by gene fusion, Tibtech 9, 226-231.
    • (1991) Tibtech , vol.9 , pp. 226-231
    • Bülow, L.1    Mosbach, K.2
  • 11
    • 0026594952 scopus 로고
    • Characterization of a recombinant bifunctional enzyme, galactose dehydrogenase/bacterial luciferase, displaying an improved bioluminiscence in a three-enzyme system
    • Lindbladh, C., Persson, M., Bülow, L. & Mosbach, K. (1992) Characterization of a recombinant bifunctional enzyme, galactose dehydrogenase/bacterial luciferase, displaying an improved bioluminiscence in a three-enzyme system, Eur. J. Biochem. 204, 241-247.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 241-247
    • Lindbladh, C.1    Persson, M.2    Bülow, L.3    Mosbach, K.4
  • 12
    • 0028181024 scopus 로고
    • An internal cellulose-binding domain mediates adsorption of an engineered bifunctional xylanase/cellulase
    • Tomme, P., Gilkes, N. R., Miller, R. C. Jr, Warren, A. J. & Kilburn, D. G. (1994) An internal cellulose-binding domain mediates adsorption of an engineered bifunctional xylanase/cellulase, Protein Eng. 7, 117-123.
    • (1994) Protein Eng. , vol.7 , pp. 117-123
    • Tomme, P.1    Gilkes, N.R.2    Miller Jr., R.C.3    Warren, A.J.4    Kilburn, D.G.5
  • 14
    • 0023049966 scopus 로고
    • Searching for autolysin functions. Characterization of a pneumococcal mutant deleted in the lyta gene
    • Sánchez-Puelles, J. M., Ronda, C., García, J. L., García, P., López, R. & García, E. (1986) Searching for autolysin functions. Characterization of a pneumococcal mutant deleted in the lytA gene, Eur. J. Biochem. 158, 289-293.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 289-293
    • Sánchez-Puelles, J.M.1    Ronda, C.2    García, J.L.3    García, P.4    López, R.5    García, E.6
  • 15
    • 0014751314 scopus 로고
    • Cellular metabolism in genetic transformation of pneumococci: Requirement for protein synthesis during induction of competence
    • Tomasz, A. (1970) Cellular metabolism in genetic transformation of pneumococci: requirement for protein synthesis during induction of competence, J. Bacteriol. 101, 860-871.
    • (1970) J. Bacteriol. , vol.101 , pp. 860-871
    • Tomasz, A.1
  • 16
    • 0025017669 scopus 로고
    • Structural studies of the lysozyme coded by the pneumococcal phage Cp-1. Conformational changes induced by choline
    • Sanz, J. M. & García, J. L. (1990) Structural studies of the lysozyme coded by the pneumococcal phage Cp-1. Conformational changes induced by choline, Eur. J. Biochem. 187, 409-416.
    • (1990) Eur. J. Biochem. , vol.187 , pp. 409-416
    • Sanz, J.M.1    García, J.L.2
  • 17
    • 0026697655 scopus 로고
    • Role of Asp-9 and Glu-36 in the active site of the pneumococcal CPL1 lysozyme: An evolutionary perspective of lysozyme mechanism
    • Sanz, J. M., García, P. & García, J. L. (1992) Role of Asp-9 and Glu-36 in the active site of the pneumococcal CPL1 lysozyme: an evolutionary perspective of lysozyme mechanism, Biochemistry 31, 8495-8499.
    • (1992) Biochemistry , vol.31 , pp. 8495-8499
    • Sanz, J.M.1    García, P.2    García, J.L.3
  • 18
    • 0025042601 scopus 로고
    • Sequence of the Streptococcus pneumoniae bacteriophage HB-3 amidase reveals high homology with the major host autolysin
    • Romero, A., López, R. & García, P. (1990) Sequence of the Streptococcus pneumoniae bacteriophage HB-3 amidase reveals high homology with the major host autolysin, J. Bacteriol. 172, 5064-5070.
    • (1990) J. Bacteriol. , vol.172 , pp. 5064-5070
    • Romero, A.1    López, R.2    García, P.3
  • 19
    • 0014961281 scopus 로고
    • Choline-containing teichoic acid as a structural component of pneumococcal cell wall and its role in sensitivity of lysis by an autolytic enzyme
    • Mosser, J. L. & Tomasz, A. (1970) Choline-containing teichoic acid as a structural component of pneumococcal cell wall and its role in sensitivity of lysis by an autolytic enzyme, J. Biol. Chem. 245, 287-298.
    • (1970) J. Biol. Chem. , vol.245 , pp. 287-298
    • Mosser, J.L.1    Tomasz, A.2
  • 20
    • 0014253402 scopus 로고
    • A modification of the Park and Johnson reducing sugar determination suitable for the assay of insoluble materials: Its application to bacterial cell walls
    • Thompson, J. S. & Shockman, G. D. (1968) A modification of the Park and Johnson reducing sugar determination suitable for the assay of insoluble materials: its application to bacterial cell walls, Anal. Biochem. 22, 260-268.
    • (1968) Anal. Biochem. , vol.22 , pp. 260-268
    • Thompson, J.S.1    Shockman, G.D.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1969) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1969) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0026289515 scopus 로고
    • Initiation of translation at AUC, AUA and AUU codons in Escherichia coli
    • Romero, A. & García, P. (1991) Initiation of translation at AUC, AUA and AUU codons in Escherichia coli, FEMS Microbiol. Lett. 84, 325-330.
    • (1991) FEMS Microbiol. Lett. , vol.84 , pp. 325-330
    • Romero, A.1    García, P.2
  • 27
    • 0027564279 scopus 로고
    • The evolutionary history of the first three enzymes in pyrimidine biosynthesis
    • Davidson, J. N., Chen, K. C., Jamison, R. S., Musmanno, L. A. & Kern, C. B. (1993) The evolutionary history of the first three enzymes in pyrimidine biosynthesis, Bioessays 15, 157-164.
    • (1993) Bioessays , vol.15 , pp. 157-164
    • Davidson, J.N.1    Chen, K.C.2    Jamison, R.S.3    Musmanno, L.A.4    Kern, C.B.5
  • 28
    • 0028814170 scopus 로고
    • Substrate specificity and detailed characterization of a bifunctional amylase-pullulanase enzyme from Bacillus circulans F-2 having two different active sites on one polypeptide
    • Kim, C.-H. & Kim, Y. S. (1995) Substrate specificity and detailed characterization of a bifunctional amylase-pullulanase enzyme from Bacillus circulans F-2 having two different active sites on one polypeptide, Eur. J. Biochem. 227, 687-693.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 687-693
    • Kim, C.-H.1    Kim, Y.S.2
  • 31
    • 0018263844 scopus 로고
    • Why genes in pieces?
    • Gilbert, W. (1978) Why genes in pieces? Nature 271, 501.
    • (1978) Nature , vol.271 , pp. 501
    • Gilbert, W.1
  • 32
    • 0028908856 scopus 로고
    • A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-β-N-acetylglucosaminidase domain: Cloning, sequence analysis, and characterization
    • Oshida, T., Sugai, M., Komatsuzawa, H., Hong, Y.-M., Suginaka, H. & Tomasz, A. (1995) A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-β-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization, Proc. Natl Acad. Sci. USA 92, 285-289.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 285-289
    • Oshida, T.1    Sugai, M.2    Komatsuzawa, H.3    Hong, Y.-M.4    Suginaka, H.5    Tomasz, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.