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Volumn 159, Issue 1, 1998, Pages 47-58

Bacillus licheniformis MC14 alkaline phosphatase I gene with an extended COOH-terminus

Author keywords

Alkaline phosphatase gene; Bacillus lichenformis; Glucose dehydrogenase gene; Sequence comparison

Indexed keywords

ALKALINE PHOSPHATASE; GLUCOSE DEHYDROGENASE;

EID: 0032008248     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(97)00542-9     Document Type: Article
Times cited : (8)

References (34)
  • 1
    • 0022446237 scopus 로고
    • Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli
    • Chang, C.N., Kuang, W.-J. and Chen, E.Y. (1986) Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli. Gene 44, 121.
    • (1986) Gene , vol.44 , pp. 121
    • Chang, C.N.1    Kuang, W.-J.2    Chen, E.Y.3
  • 2
    • 0022335244 scopus 로고
    • Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA
    • Kam, W., Clauser, E., Kim, Y.W., Kan, Y.W. and Rutter, W.J. (1985) Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proc. Natl. Acad. Sci. USA 82, 8715.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8715
    • Kam, W.1    Clauser, E.2    Kim, Y.W.3    Kan, Y.W.4    Rutter, W.J.5
  • 5
    • 0023515035 scopus 로고
    • Structural characteristics of the PH08 gene encoding repressible alkaline phosphatase in Saccharomyces cerevisiae
    • Kaneko, Y., Hayashi, N., Toh-E, A., Banno, I. and Ohima, Y. (1987) Structural characteristics of the PH08 gene encoding repressible alkaline phosphatase in Saccharomyces cerevisiae. Gene 58, 137.
    • (1987) Gene , vol.58 , pp. 137
    • Kaneko, Y.1    Hayashi, N.2    Toh-E, A.3    Banno, I.4    Ohima, Y.5
  • 6
    • 0025977645 scopus 로고
    • Bacillus subtilis alkaline phosphatases III and IV: Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure
    • Hulett, F.M., Kim, E.E., Bookstein, C., Kapp, N.V., Edwards, C.W. and Wyckoff, H.W. (1991) Bacillus subtilis alkaline phosphatases III and IV: Cloning, sequencing, and comparisons of deduced amino acid sequence with Escherichia coli alkaline phosphatase three-dimensional structure. J. Biol. Chem. 266, 1077.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1077
    • Hulett, F.M.1    Kim, E.E.2    Bookstein, C.3    Kapp, N.V.4    Edwards, C.W.5    Wyckoff, H.W.6
  • 7
    • 0025181742 scopus 로고
    • Structure of alkaline phosphatases
    • Kim, E.E. and Wyckoff, H.W. (1989) Structure of alkaline phosphatases. Clin. Chim. Acta 186, 175.
    • (1989) Clin. Chim. Acta , vol.186 , pp. 175
    • Kim, E.E.1    Wyckoff, H.W.2
  • 8
    • 0019459921 scopus 로고
    • Effect of cobalt on synthesis and activation of Bacillus licheniformis phosphatase
    • Spencer, D.B., Chen, C.-P. and Hulett, F.M. (1981) Effect of cobalt on synthesis and activation of Bacillus licheniformis phosphatase. J. Bacteriol. 145, 926.
    • (1981) J. Bacteriol. , vol.145 , pp. 926
    • Spencer, D.B.1    Chen, C.-P.2    Hulett, F.M.3
  • 9
    • 0024447838 scopus 로고
    • Membrane protein sorting: biosynthesis, transport, and processing of yeast vacuolar alkaline phosphatase
    • Klionsky, D.J. and Erm, S.D. (1989) Membrane protein sorting: biosynthesis, transport, and processing of yeast vacuolar alkaline phosphatase. EMBO J. 8, 2241.
    • (1989) EMBO J. , vol.8 , pp. 2241
    • Klionsky, D.J.1    Erm, S.D.2
  • 10
    • 0023732992 scopus 로고
    • Sequence and characterization of the human intestinal alkaline phosphatase
    • Henthorn, P.S., Raducha, M., Kadesch, T., Weiss, M. and Harris, H. (1988) Sequence and characterization of the human intestinal alkaline phosphatase. J. Biol. Chem. 263, 12011.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12011
    • Henthorn, P.S.1    Raducha, M.2    Kadesch, T.3    Weiss, M.4    Harris, H.5
  • 11
    • 0023713647 scopus 로고
    • Chemical characterization of the membrane-anchoring domain of human placental alkaline phosphatase
    • Ogata, S., Hayashi, Y., Takami, N. and Ikehara, Y. (1988) Chemical characterization of the membrane-anchoring domain of human placental alkaline phosphatase. J. Biol. Chem. 263, 10489.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10489
    • Ogata, S.1    Hayashi, Y.2    Takami, N.3    Ikehara, Y.4
  • 12
    • 0344782532 scopus 로고
    • The secreted alkaline phosphatase of Bacillus licheniformis MC14: identification of a possible precursor
    • Academic Press, New York
    • Hulett, F.M. (1986) The secreted alkaline phosphatase of Bacillus licheniformis MC14: identification of a possible precursor. In: Bacillus Molecular Genetics and Biotechnology Applications, pp. 109-127, Academic Press, New York.
    • (1986) In: Bacillus Molecular Genetics and Biotechnology Applications , pp. 109-127
    • Hulett, F.M.1
  • 13
    • 0025136856 scopus 로고
    • Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis
    • Hulett, F.M., Bookstein, C. and Jensen, K. (1990) Evidence for two structural genes for alkaline phosphatase in Bacillus subtilis. J. Bacteriol. 172, 735.
    • (1990) J. Bacteriol. , vol.172 , pp. 735
    • Hulett, F.M.1    Bookstein, C.2    Jensen, K.3
  • 14
    • 0023057844 scopus 로고
    • Nucleotide sequence and organization of Bacillus subtilis RNA polymerase major sigma (sigma-43) operon
    • Wang, L.-F. and Doy, R.H. (1986) Nucleotide sequence and organization of Bacillus subtilis RNA polymerase major sigma (sigma-43) operon. Nucleic Acids Res. 14, 4293.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4293
    • Wang, L.-F.1    Doy, R.H.2
  • 15
    • 0025963835 scopus 로고
    • Identification of four unique clones encoding 10 kDa proteins from Bacillus that cause phenotypic complementation of a phoA mutant strain of Escherichia coli
    • Lee, J.K., Edwards, C.W. and Hulett, F.M. (1991a) Identification of four unique clones encoding 10 kDa proteins from Bacillus that cause phenotypic complementation of a phoA mutant strain of Escherichia coli. J. Gen. Microbiol. 137, 667.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 667
    • Lee, J.K.1    Edwards, C.W.2    Hulett, F.M.3
  • 16
    • 0025753449 scopus 로고
    • Bacillus licheniformis APaseI gene promoter: A strong well-regulated promoter in B. subtilis
    • Lee, J.K., Edwards, C.W. and Hulett, F.M. (1991b). Bacillus licheniformis APaseI gene promoter: a strong well-regulated promoter in B. subtilis. J. Gen. Microbiol. 137, 1127.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 1127
    • Lee, J.K.1    Edwards, C.W.2    Hulett, F.M.3
  • 17
    • 0344103377 scopus 로고
    • Genetics
    • (Howard, C.R., Ed.), New York, Plenum
    • Ferrari, E. and Hoch, J.A. (1989) Genetics. In: Bacillus (Howard, C.R., Ed.), pp. 57-72. New York, Plenum.
    • (1989) In: Bacillus , pp. 57-72
    • Ferrari, E.1    Hoch, J.A.2
  • 19
    • 0025194335 scopus 로고
    • The Bacillus subtilis 168 alkaline phosphatase III gene: The impact of a phoAIII mutation on total alkaline phosphatase synthesis
    • Bookstein, C., Edwards, C.E., Kapp, N.V. and Hulett, F.M. (1990) The Bacillus subtilis 168 alkaline phosphatase III gene: the impact of a phoAIII mutation on total alkaline phosphatase synthesis. J. Bacteriol. 172, 3730.
    • (1990) J. Bacteriol. , vol.172 , pp. 3730
    • Bookstein, C.1    Edwards, C.E.2    Kapp, N.V.3    Hulett, F.M.4
  • 21
    • 0017342488 scopus 로고
    • Biochemical localization of the alkaline phosphatase of Bacillus licheniformis as a function of culture age
    • Glynn, J.A., Schaffel, S.D., McNicholas, J.M. and Hulett, F.M. (1977) Biochemical localization of the alkaline phosphatase of Bacillus licheniformis as a function of culture age. J. Bacteriol. 129, 1010.
    • (1977) J. Bacteriol. , vol.129 , pp. 1010
    • Glynn, J.A.1    Schaffel, S.D.2    McNicholas, J.M.3    Hulett, F.M.4
  • 22
    • 0019430107 scopus 로고
    • A soluble alkaline phosphatase from Bacillus licheniformis MC14: histochemical localization, purification and characterization and comparison with the membrane-associated alkaline phosphatase
    • Hansa, J.G., Laporta, M., Kuna, A., Reimschuessel, R. and Hulett, F.M. (1981) A soluble alkaline phosphatase from Bacillus licheniformis MC14: histochemical localization, purification and characterization and comparison with the membrane-associated alkaline phosphatase. Biochim. Biophys. Acta 675, 390.
    • (1981) Biochim. Biophys. Acta , vol.675 , pp. 390
    • Hansa, J.G.1    Laporta, M.2    Kuna, A.3    Reimschuessel, R.4    Hulett, F.M.5
  • 23
    • 0019394517 scopus 로고
    • 125I localization of salt-extractable alkaline phosphatase on the cytoplasmic membrane of Bacillus licheniformis
    • 125I localization of salt-extractable alkaline phosphatase on the cytoplasmic membrane of Bacillus licheniformis. J. Bacteriol. 145, 934.
    • (1981) J. Bacteriol. , vol.145 , pp. 934
    • Spencer, D.B.1    Hulett, F.M.2
  • 24
    • 0022551799 scopus 로고
    • Purification and characterization of the secreted alkaline phosphatase of Bacillus licheniformis MC14: identification of a possible precursor
    • Hulett, F.M., Stuckmann, K., Spencer, D.B. and Sanopoulou, T. (1986) Purification and characterization of the secreted alkaline phosphatase of Bacillus licheniformis MC14: identification of a possible precursor. J. Gen. Microbiol. 132, 2387.
    • (1986) J. Gen. Microbiol. , vol.132 , pp. 2387
    • Hulett, F.M.1    Stuckmann, K.2    Spencer, D.B.3    Sanopoulou, T.4
  • 25
    • 0018169535 scopus 로고
    • Alkaline phosphatase from Bacillus licheniformis. Solubility dependent on magnesium, purification and characterization
    • Schaffel, S. and Hulett, F.M. (1978) Alkaline phosphatase from Bacillus licheniformis. Solubility dependent on magnesium, purification and characterization. Biochim. Biophys. Acta 526, 457.
    • (1978) Biochim. Biophys. Acta , vol.526 , pp. 457
    • Schaffel, S.1    Hulett, F.M.2
  • 26
    • 0024539019 scopus 로고
    • Stability-increasing mutants of glucose dehydrogenase from Bacillus megaterium IWG3.
    • Makino, Y., Negoro, S., Urabe, I. and Okada, H. (1989) Stability-increasing mutants of glucose dehydrogenase from Bacillus megaterium IWG3. J. Biol. Chem. 264, 6381.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6381
    • Makino, Y.1    Negoro, S.2    Urabe, I.3    Okada, H.4
  • 27
    • 0022447232 scopus 로고
    • Characterization of the developmentally regulated Bacillus subtilis glucose dehydrogenase gene
    • Lampel, K.A., Uratani, B., Chaudhry, G.R., Ramalye, R.F. and Rudikoff, S. (1986) Characterization of the developmentally regulated Bacillus subtilis glucose dehydrogenase gene. J. Bacteriol. 166, 238.
    • (1986) J. Bacteriol. , vol.166 , pp. 238
    • Lampel, K.A.1    Uratani, B.2    Chaudhry, G.R.3    Ramalye, R.F.4    Rudikoff, S.5
  • 28
    • 0017738195 scopus 로고
    • Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis
    • Fujita, Y.R., Ramaley, R. and Freese, E. (1977) Location and properties of glucose dehydrogenase in sporulating cells and spores of Bacillus subtilis. J. Bacteriol. 132, 282.
    • (1977) J. Bacteriol. , vol.132 , pp. 282
    • Fujita, Y.R.1    Ramaley, R.2    Freese, E.3
  • 29
    • 0021112693 scopus 로고
    • Glycerol protection and purification of Bacillus subtilis glucose dehydrogenase
    • Ramaley, R.F. and Vasantha, N. (1983) Glycerol protection and purification of Bacillus subtilis glucose dehydrogenase. J. Biol. Chem. 258, 12558.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12558
    • Ramaley, R.F.1    Vasantha, N.2
  • 30
    • 0027373184 scopus 로고
    • Modifications in a flexible surface loop modulate the isozyme-specific properties of mammalian alkaline phosphatases
    • Bossi, M., Hoylaerts, M.F. and Mill, N.J.L. (1993) Modifications in a flexible surface loop modulate the isozyme-specific properties of mammalian alkaline phosphatases. J. Biol. Chem. 268, 25409.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25409
    • Bossi, M.1    Hoylaerts, M.F.2    Mill, N.J.L.3
  • 31
    • 0024286552 scopus 로고
    • Structural and functional roles of glycosyl-phosphatidylinositol in membranes
    • Low, M.G. and Saltiel, A.R. (1988) Structural and functional roles of glycosyl-phosphatidylinositol in membranes. Science 239, 268.
    • (1988) Science , vol.239 , pp. 268
    • Low, M.G.1    Saltiel, A.R.2
  • 32
    • 0024438791 scopus 로고
    • Apparent phosphate retrieval system in Bacillus cereus.
    • Guddal, P.H., Hohansen, T., Schulstad, K. and Little, C. (1989) Apparent phosphate retrieval system in Bacillus cereus. J. Bacteriol. 171, 5702.
    • (1989) J. Bacteriol. , vol.171 , pp. 5702
    • Guddal, P.H.1    Hohansen, T.2    Schulstad, K.3    Little, C.4
  • 33
    • 0026638608 scopus 로고
    • Sorting of protein A to the staphylococcal cell wall
    • Schneewind, O., Model, P. and Fischetti, V.A. (1992) Sorting of protein A to the staphylococcal cell wall. Cell 70, 267.
    • (1992) Cell , vol.70 , pp. 267
    • Schneewind, O.1    Model, P.2    Fischetti, V.A.3


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