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Volumn 179, Issue 12, 1997, Pages 4061-4065

A putative monofunctional glycosyltransferase is expressed in Ralstonia eutropha

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLTRANSFERASE; PENICILLIN BINDING PROTEIN;

EID: 0031010726     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.12.4061-4065.1997     Document Type: Article
Times cited : (13)

References (28)
  • 2
    • 0021321955 scopus 로고
    • A rapid sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots
    • Blake, M. S., K. H. Johnson, G. Russell-Jones, and E. C. Gotschlich. 1984. A rapid sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blots. Anal. Biochem. 136:175-179.
    • (1984) Anal. Biochem. , vol.136 , pp. 175-179
    • Blake, M.S.1    Johnson, K.H.2    Russell-Jones, G.3    Gotschlich, E.C.4
  • 3
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 5
    • 0030603148 scopus 로고    scopus 로고
    • The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes: Overexpression and determination of the glycan-polymerising activity
    • Di Berardino. M., A. Dijkstra, D. Stüber, W. Keck, and M. Gubler. 1996. The monofunctional glycosyltransferase of Escherichia coli is a member of a new class of peptidoglycan-synthesising enzymes: overexpression and determination of the glycan-polymerising activity. FEBS Lett. 392:184-188.
    • (1996) FEBS Lett. , vol.392 , pp. 184-188
    • Di Berardino, M.1    Dijkstra, A.2    Stüber, D.3    Keck, W.4    Gubler, M.5
  • 8
    • 0001098472 scopus 로고
    • Biochemistry of the penicilloyl-serine transferases
    • J.-M. Ghuysen and R. Hakenbeck (ed.), Elsevier Sciences BV, Amsterdam, The Netherlands
    • Ghuysen, J.-M., and G. Dive. 1994. Biochemistry of the penicilloyl-serine transferases, p. 103-129. In J.-M. Ghuysen and R. Hakenbeck (ed.), Bacterial cell wall. Elsevier Sciences BV, Amsterdam, The Netherlands.
    • (1994) Bacterial Cell Wall , pp. 103-129
    • Ghuysen, J.-M.1    Dive, G.2
  • 9
    • 0019842601 scopus 로고
    • Role of sulA and sulB in filamentation by Lon mutants of Escherichia coli K-12
    • Gottesmann, S., E. Halpern, and P. Trisler. 1981. Role of sulA and sulB in filamentation by Lon mutants of Escherichia coli K-12. J. Bacteriol. 148:265-273.
    • (1981) J. Bacteriol. , vol.148 , pp. 265-273
    • Gottesmann, S.1    Halpern, E.2    Trisler, P.3
  • 10
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • Guan, C., P. D. Li, and M. Inouye. 1987. Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67:21-30.
    • (1987) Gene , vol.67 , pp. 21-30
    • Guan, C.1    Li, P.D.2    Inouye, M.3
  • 11
    • 0022538204 scopus 로고
    • Penicillin-binding proteins of penicillin-susceptible and -resistant pneumococci: Immunological relatedness of altered proteins and changes in peptides carrying the β-lactam binding site
    • Hakenbeck, R., H. Ellerbrok, T. Briese, S. Handwerger, and A. Tomasz. 1986. Penicillin-binding proteins of penicillin-susceptible and -resistant pneumococci: immunological relatedness of altered proteins and changes in peptides carrying the β-lactam binding site. Antimicrob. Agents Chemother. 30:553-558.
    • (1986) Antimicrob. Agents Chemother. , vol.30 , pp. 553-558
    • Hakenbeck, R.1    Ellerbrok, H.2    Briese, T.3    Handwerger, S.4    Tomasz, A.5
  • 12
    • 0027183518 scopus 로고
    • The Alcaligenes eutrophus ldh structural gene encodes a novel type of lactate dehydrogenase
    • Jendrossek, D., H. D. Kratzin, and A. Steinbüchel. 1993. The Alcaligenes eutrophus ldh structural gene encodes a novel type of lactate dehydrogenase. FEMS Microbiol. Lett. 112:229-236.
    • (1993) FEMS Microbiol. Lett. , vol.112 , pp. 229-236
    • Jendrossek, D.1    Kratzin, H.D.2    Steinbüchel, A.3
  • 13
    • 0024215242 scopus 로고
    • A vector to express and purify foreign protein in Escherichia coli by fusion to, and separation from, maltose binding protein
    • Maina, C. V., P. D. Riggs, A. G. I. Grandea, B. E. Slatko, L. S. Moran, J. A. Tagliamonte, L. A. McReynolds, and C. Guan. 1988. A vector to express and purify foreign protein in Escherichia coli by fusion to, and separation from, maltose binding protein. Gene 74:365-373.
    • (1988) Gene , vol.74 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea, A.G.I.3    Slatko, B.E.4    Moran, L.S.5    Tagliamonte, J.A.6    McReynolds, L.A.7    Guan, C.8
  • 15
    • 0026711139 scopus 로고
    • Nucleotide sequences of genes encoding penicillin-binding proteins from Streptococcus pneumoniae and Streptococcus oralis with high homology to Escherichia coli penicillin-binding protein 1A and 1B
    • Martin, C., T. Briese, and R. Hakenbeck. 1992. Nucleotide sequences of genes encoding penicillin-binding proteins from Streptococcus pneumoniae and Streptococcus oralis with high homology to Escherichia coli penicillin-binding protein 1A and 1B. J. Bacteriol. 174:4517-4523.
    • (1992) J. Bacteriol. , vol.174 , pp. 4517-4523
    • Martin, C.1    Briese, T.2    Hakenbeck, R.3
  • 16
    • 0026782144 scopus 로고
    • Relatedness of penicillin-binding protein 1a genes from different clones of penicillin-resistant Streptococcus pneumoniae isolated in South Africa and Spain
    • Martin, C., C. Sibold, and R. Hakenbeck. 1992. Relatedness of penicillin-binding protein 1a genes from different clones of penicillin-resistant Streptococcus pneumoniae isolated in South Africa and Spain. EMBO J. 11:3831-3836.
    • (1992) EMBO J. , vol.11 , pp. 3831-3836
    • Martin, C.1    Sibold, C.2    Hakenbeck, R.3
  • 17
    • 0021690285 scopus 로고
    • Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides
    • Nakagawa, J., S. Taraaki, S. Tomioka, and M. Matsuhashi, 1984. Functional biosynthesis of cell wall peptidoglycan by polymorphic bifunctional polypeptides. J. Biol. Chem. 259:13937-13946.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13937-13946
    • Nakagawa, J.1    Taraaki, S.2    Tomioka, S.3    Matsuhashi, M.4
  • 18
    • 0029988098 scopus 로고    scopus 로고
    • X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme
    • Pares, S., N. Mouz, Y. Pétillot, R. Hakenbeck, and O. Dideberg. 1996. X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin target enzyme. Nature Struct. Biol. 3:284-289.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 284-289
    • Pares, S.1    Mouz, N.2    Pétillot, Y.3    Hakenbeck, R.4    Dideberg, O.5
  • 19
    • 0021341553 scopus 로고
    • Staphyhcoccus aureus and Micrococcus luteus peptidoglycan transglycosylases that are not penicillin-binding proteins
    • Park, W., and M. Matsuhashi. 1984. Staphyhcoccus aureus and Micrococcus luteus peptidoglycan transglycosylases that are not penicillin-binding proteins. J. Bacteriol. 157:538-544.
    • (1984) J. Bacteriol. , vol.157 , pp. 538-544
    • Park, W.1    Matsuhashi, M.2
  • 20
    • 0021970299 scopus 로고
    • Major peptidoglycan transglycosylase activity in Streptococcus pneumoniae that is not a penicillin-binding protein
    • Park, W., H. Seto, R. Hakenbeck, and M. Matsuhashi. 1985. Major peptidoglycan transglycosylase activity in Streptococcus pneumoniae that is not a penicillin-binding protein. FEMS Microbiol. Lett. 27:45-48.
    • (1985) FEMS Microbiol. Lett. , vol.27 , pp. 45-48
    • Park, W.1    Seto, H.2    Hakenbeck, R.3    Matsuhashi, M.4
  • 22
    • 34250969714 scopus 로고
    • Ein submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen
    • Schlegel, H. G., H. Kaltwasser, and G. Gottschalk. 1961. Ein submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen. Arch. Mikrobiol. 38:119-128.
    • (1961) Arch. Mikrobiol. , vol.38 , pp. 119-128
    • Schlegel, H.G.1    Kaltwasser, H.2    Gottschalk, G.3
  • 23
    • 0030058939 scopus 로고    scopus 로고
    • Monofunctional biosynthetic peptidoglycan transglycosylases
    • Spratt, B. G., J. Zhou, M. Taylor, and M. J. Merrick. 1996. Monofunctional biosynthetic peptidoglycan transglycosylases. Mol. Microbiol. 19:639-640.
    • (1996) Mol. Microbiol. , vol.19 , pp. 639-640
    • Spratt, B.G.1    Zhou, J.2    Taylor, M.3    Merrick, M.J.4
  • 24
    • 0018855285 scopus 로고
    • In vitro peptidoglycan polymerization catalysed by penicillin-binding protein 1b of Escherichia coli K 12
    • Suzuki, H., Y. van Heijenoort, T. Tamura, J. Mizoguchi, Y. Hirota, and J. van Heijenoort. 1980. In vitro peptidoglycan polymerization catalysed by penicillin-binding protein 1b of Escherichia coli K 12. FEBS Lett. 110:245-249.
    • (1980) FEBS Lett. , vol.110 , pp. 245-249
    • Suzuki, H.1    Van Heijenoort, Y.2    Tamura, T.3    Mizoguchi, J.4    Hirota, Y.5    Van Heijenoort, J.6
  • 25
    • 0017851898 scopus 로고
    • Polymerization by transglycosylation in the biosynthesis of the peptidoglycan of Escherichia coli K 12 and its inhibition by antibiotics
    • van Heijenoort, Y., M. Derrien, and J. van Heijenoort. 1979. Polymerization by transglycosylation in the biosynthesis of the peptidoglycan of Escherichia coli K 12 and its inhibition by antibiotics. FEBS Lett. 89:141-144.
    • (1979) FEBS Lett. , vol.89 , pp. 141-144
    • Van Heijenoort, Y.1    Derrien, M.2    Van Heijenoort, J.3
  • 26
    • 0018902610 scopus 로고
    • Biosynthesis of the peptidoglycan at Escherichia coli K 12. Properties of the in vitro polymerization by transglycosylation
    • van Heijenoort, Y., and J. van Heijenoort. 1980. Biosynthesis of the peptidoglycan at Escherichia coli K 12. Properties of the in vitro polymerization by transglycosylation. FEBS Lett. 110:241-244.
    • (1980) FEBS Lett. , vol.110 , pp. 241-244
    • Van Heijenoort, Y.1    Van Heijenoort, J.2
  • 27
    • 0029888520 scopus 로고    scopus 로고
    • Localization of a putative second membrane association site in penicillin-binding protein 1B of Escherichia coli
    • Wand, C. C., D. E. Schultz, and R. A. Nicholas. 1996. Localization of a putative second membrane association site in penicillin-binding protein 1B of Escherichia coli. Biochem. J. 316:149-156.
    • (1996) Biochem. J. , vol.316 , pp. 149-156
    • Wand, C.C.1    Schultz, D.E.2    Nicholas, R.A.3
  • 28
    • 0028850433 scopus 로고
    • Transfer of two Burkholderia and one Alcaligenes species to Ralslonia gen. nov.: Proposal of Ralstonia pickettii (Ralston, Palleroni and Doudoroff 1973) comb. nov., Ralstonia solanacearum (Smith 1986) comb. nov. and Ralstonia eutropha (Davis 1969) comb. nov
    • Yabuuchi, E., Y. Kosako, I. Yano, H. Hotta, and Y. Nishiuchi. 1995. Transfer of two Burkholderia and one Alcaligenes species to Ralslonia gen. nov.: proposal of Ralstonia pickettii (Ralston, Palleroni and Doudoroff 1973) comb. nov., Ralstonia solanacearum (Smith 1986) comb. nov. and Ralstonia eutropha (Davis 1969) comb. nov. Microbiol. Immunol. 39:897-904.
    • (1995) Microbiol. Immunol. , vol.39 , pp. 897-904
    • Yabuuchi, E.1    Kosako, Y.2    Yano, I.3    Hotta, H.4    Nishiuchi, Y.5


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