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Original Articles

Clustered Proline Residues around the Active-Site Cleft in Thermostable Oligo-1,6-glucosidase of Bacillus flavocaldarius KP1228

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Pages 1093-1102 | Received 30 Oct 1997, Published online: 22 May 2014

  • 1) Y. Suzuki, K. Oishi, H. Nakano, and T. Nagayama, Appl. Microbiol. Biotechnol., 26, 546-551 (1987).
  • 2) Y. Suzuki, Proc. Jpn. Acad. Ser. B Phys. Biol. Sci., 65, 146-148 (1989).
  • 3) E. G. Hutchinson and J. M. Thornton, Protein Sci., 3, 2207-2216 (1994).
  • 4) K. Watanabe, K. Kitamura, and Y. Suzuki, Appl. Environ. Microbiol., 62, 2066-2073 (1996).
  • 5) K. Watanabe, T. Masuda, H. Ohashi, H. Mihara, and Y. Suzuki, Eur. J. Biochem., 226, 277-283 (1994).
  • 6) B. W. Matthews, H. Nicholson, and W. J. Becktel, Proc. Natl. Acad. Sci. USA, 84, 6663-6667 (1987).
  • 7) T. Ueda, T. Tamura, Y. Maeda, Y. Hashimoto, T. Miki, H. Yamada, and T. Imoto, Protein Eng., 6, 183-187 (1993).
  • 8) T. Herning, K. Yutani, Y. Taniyama, and M. Kikuchi, Biochemistry, 30, 9882-9891 (1991).
  • 9) S. Kimura, H. Nakamura, T. Hashimoto, M. Oobatake, and S. Kanaya, J. Biol. Chem., 267, 21535-21542 (1992).
  • 10) K. Ishikawa, S. Kimura, S. Kanaya, K. Morikawa, and H. Nakamura, Protein Eng., 6, 85-91 (1993).
  • 11) F. Hardy, G. Vriend, O. R. Veltman, B. van der Vinne, and V. G. H. Eijsink, FEBS Lett., 317, 89-92 (1993).
  • 12) A. Masui, N. Fujiwara, and T. Imanaka, Appl. Environ. Microbiol., 60, 3579-3584 (1994).
  • 13) E. C. Ohage, W. Graml, M. M. Walter, S. Steinbacher, and B. Steipe, Protein Sci., 6, 233-241 (1997).
  • 14) Y. Okada, N. Yoshigi, H. Sahara, and S. Koshino, Biosci. Biotech. Biochem., 59, 1152-1153 (1995).
  • 15) K. Watanabe, Y. Hata, H. Kizaki, Y. Katsube, and Y. Suzuki, J. Mol. Biol., 269, 142-153 (1997).
  • 16) K. Watanabe, K. Kitamura, H. Iha, and Y. Suzuki, Eur. J. Biochem., 192, 609-620 (1990).
  • 17) K. Watanabe, K. Chishiro, K. Kitamura, and Y. Suzuki, J. Biol. Chem., 266, 24287-24294 (1991).
  • 18) Y. Suzuki, H. Fujii, H. Uemura, and M. Suzuki, Starch/Stärke, 39, 17-23 (1987).
  • 19) O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, J. Biol. Chem., 193, 265-275 (1951).
  • 20) J. Sambrook, E. F. Fritsch, and T. Maniatis, “Molecular Cloning: A Laboratory Manual” 2nd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor 1989.
  • 21) F. Sanger, Science, 214, 1205-1210 (1981).
  • 22) O. K. Laemmli, Nature, 227, 680-685 (1970).
  • 23) H. Towbin, T. Staehelin, and J. Gordon, Proc. Natl. Acad. Sci. USA, 76, 4350-4354 (1979).
  • 24) Y. Suzuki, N. Nakamura, T. Kishigami, and S. Abe, J. Biochem. (Tokyo), 87, 745-751 (1980).
  • 25) M. Rosenberg and D. Court, Annu. Rev. Genet., 13, 319-353 (1979).
  • 26) S. Tsunasawa, J. W. Stewart, and F. Sherman, J. Biol. Chem, 260, 5382-5391 (1985).
  • 27) B. Svensson, Plant Mol. Biol., 25, 141-157 (1994).
  • 28) Y. Takii, K. Takahashi, K. Yamamoto, Y. Sogabe, and Y. Suzuki, Appl. Microbiol. Biotechnol., 44, 629-634 (1996).
  • 29) B. Rost and C. Sander, Proteins: Struct. Funct. Genet., 19, 55-72 (1994).
  • 30) B. Rost and C. Sander, Proteins: Struct. Funct. Genet., 20, 216-226 (1994).
  • 31) M. W. MacArthur and J. M. Thornton, J. Mol. Biol., 218, 397-412 (1991).
  • 32) S. Dasgupta and J. A. Bell, Int. J. Peptide Protein Res., 41, 499-511 (1993).
  • 33) J. S. Richardson and D. C. Richardson, Science, 240, 1648-1652 (1988).
  • 34) R. H. Yun, A. Anderson, and J. Hermans, Proteins: Struct. Funct. Genet., 10, 219-228 (1991).
  • 35) G. von Heijne, J. Mol. Biol., 218, 499-503 (1991).
  • 36) K. Yutani, S. Hayashi, Y. Sugisaki, and K. Ogasahara, Proteins: Struct. Funct. Genet., 9, 90-98 (1991).
  • 37) K. Ogasahara and K. Yutani, Biochemistry, 36, 932-940 (1997).
  • 38) M. Schiffer, C. F. Ainsworth, Y.-L. Deng, G. Johnson, F. H. Pascoe, and D. K. Hanson, J. Mol. Biol., 252, 472-482 (1995).
  • 39) S. M. Howitt, M. Cleeter, L. Hatch, and G. B. Cox, Biochim. Biophys. Acta, 1144, 17-21 (1993).
  • 40) H. Nicholson, D. E. Tronrud, W. J. Becktel, and B. W. Matthews, Biopolymers, 32, 1431-1441 (1992).
  • 41) W. Behammer, Z. Shao, W. Mages, R. Rachel, K. O. Stetter, and R. Schmitt, J. Bacteriol., 177, 6630-6637 (1995).
  • 42) K. Imada, H. Sato, N. Tanaka, Y. Katsube, Y. Matsuura, and T. Oshima, J. Mol. Biol., 222, 725-738 (1991).
  • 43) Y. Suzuki and K. Oishi, Appl. Microbiol. Biotechnol., 31, 32-37 (1989).
  • 44) B. K. Shoichet, W. A. Baase, R. Kuroki, and B. W. Matthews, Proc. Natl. Acad. Sci. USA, 92, 452-456 (1995).
  • 45) A. Shaw and R. Bett, Curr. Opin. Struct. Biol., 6, 546-550 (1996).
  • 46) C. Vieille and J. G. Zeikus, Trends Biotechnol., 14, 183-190 (1996).
  • 47) V. Z. Spassov, A. D. Karshikoff, and R. Ladenstein, Protein Sci., 4, 1516-1527 (1995).
  • 48) R. Sterner, T. Vogl, H.-J. Hinz, F. Penz, R. Hoff, R. Föll, and H. Decker, FEBS Lett., 364, 9-12 (1995).
  • 49) M. Kohlhoff, A. Dahm, and R. Hensel, FEBS Lett., 283, 245-250 (1996).

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