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177 related items for PubMed ID: 2120057

  • 1. Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene.
    Watanabe K, Kitamura K, Iha H, Suzuki Y.
    Eur J Biochem; 1990 Sep 24; 192(3):609-20. PubMed ID: 2120057
    [Abstract] [Full Text] [Related]

  • 2. Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006.
    Watanabe K, Chishiro K, Kitamura K, Suzuki Y.
    J Biol Chem; 1991 Dec 25; 266(36):24287-94. PubMed ID: 1761534
    [Abstract] [Full Text] [Related]

  • 3. Identification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6-glucosidase.
    Watanabe K, Miyake K, Suzuki Y.
    Biosci Biotechnol Biochem; 2001 Sep 25; 65(9):2058-64. PubMed ID: 11676021
    [Abstract] [Full Text] [Related]

  • 4. Cloning and expression in Escherichia coli of an extremely thermostable oligo-1,6-glucosidase gene from Bacillus thermoglucosidasius.
    Watanabe K, Iha H, Ohashi A, Suzuki Y.
    J Bacteriol; 1989 Feb 25; 171(2):1219-22. PubMed ID: 2644230
    [Abstract] [Full Text] [Related]

  • 5. The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization.
    Watanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y.
    J Mol Biol; 1997 May 30; 269(1):142-53. PubMed ID: 9193006
    [Abstract] [Full Text] [Related]

  • 6. Analysis of the critical sites for protein thermostabilization by proline substitution in oligo-1,6-glucosidase from Bacillus coagulans ATCC 7050 and the evolutionary consideration of proline residues.
    Watanabe K, Kitamura K, Suzuki Y.
    Appl Environ Microbiol; 1996 Jun 30; 62(6):2066-73. PubMed ID: 8787404
    [Abstract] [Full Text] [Related]

  • 7. Clustered proline residues around the active-site cleft in thermostable oligo-1,6-glucosidase of Bacillus flavocaldarius KP1228.
    Kashiwabara S, Matsuki Y, Kishimoto T, Suzuki Y.
    Biosci Biotechnol Biochem; 1998 Jun 30; 62(6):1093-102. PubMed ID: 9692189
    [Abstract] [Full Text] [Related]

  • 8. Oligo-1,6-glucosidase from a thermophile, Bacillus thermoglucosidasius KP1006, was efficiently produced by combinatorial expression of GroEL in Escherichia coli.
    Watanabe K, Fujiwara H, Inui K, Suzuki Y.
    Biotechnol Appl Biochem; 2002 Feb 30; 35(1):35-43. PubMed ID: 11834128
    [Abstract] [Full Text] [Related]

  • 9. [Cloning and expression in Escherichia coli of oligo-1,6-glucosidase gene from Bacillus subtilis HB002].
    Jiang S, Ma L.
    Wei Sheng Wu Xue Bao; 2002 Apr 30; 42(2):145-52. PubMed ID: 12557389
    [Abstract] [Full Text] [Related]

  • 10. Assignment of Bacillus thermoamyloliquefaciens KP1071 alpha-glucosidase I to an exo-alpha-1,4-glucosidase, and its striking similarity to bacillary oligo-1,6-glucosidases in N-terminal sequence and in structural parameters calculated from the amino acid composition.
    Suzuki Y, Yonezawa K, Hattori M, Takii Y.
    Eur J Biochem; 1992 Apr 01; 205(1):249-56. PubMed ID: 1555585
    [Abstract] [Full Text] [Related]

  • 11. Overproduction, purification and crystallization of Bacillus cereus oligo-1,6-glucosidase.
    Watanabe K, Kitamura K, Hata Y, Katsube Y, Suzuki Y.
    FEBS Lett; 1991 Sep 23; 290(1-2):221-3. PubMed ID: 1915879
    [Abstract] [Full Text] [Related]

  • 12. Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 A resolution X-ray analysis.
    Kizaki H, Hata Y, Watanabe K, Katsube Y, Suzuki Y.
    J Biochem; 1993 Jun 23; 113(6):646-9. PubMed ID: 8370659
    [Abstract] [Full Text] [Related]

  • 13. Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule.
    Watanabe K, Masuda T, Ohashi H, Mihara H, Suzuki Y.
    Eur J Biochem; 1994 Dec 01; 226(2):277-83. PubMed ID: 8001545
    [Abstract] [Full Text] [Related]

  • 14. Structure and expression of a gene coding for thermostable alpha-glucosidase with a broad substrate specificity from Bacillus sp. SAM1606.
    Nakao M, Nakayama T, Kakudo A, Inohara M, Harada M, Omura F, Shibano Y.
    Eur J Biochem; 1994 Mar 01; 220(2):293-300. PubMed ID: 8125087
    [Abstract] [Full Text] [Related]

  • 15. Purification and characterization of Bacillus coagulans oligo-1,6-glucosidase.
    Suzuki Y, Tomura Y.
    Eur J Biochem; 1986 Jul 01; 158(1):77-83. PubMed ID: 3089779
    [Abstract] [Full Text] [Related]

  • 16. Phosphatidylinositol-specific phospholipase C of Bacillus cereus: cloning, sequencing, and relationship to other phospholipases.
    Kuppe A, Evans LM, McMillen DA, Griffith OH.
    J Bacteriol; 1989 Nov 01; 171(11):6077-83. PubMed ID: 2509427
    [Abstract] [Full Text] [Related]

  • 17. Phospholipase C and haemolytic activities of Clostridium perfringens alpha-toxin cloned in Escherichia coli: sequence and homology with a Bacillus cereus phospholipase C.
    Leslie D, Fairweather N, Pickard D, Dougan G, Kehoe M.
    Mol Microbiol; 1989 Mar 01; 3(3):383-92. PubMed ID: 2546005
    [Abstract] [Full Text] [Related]

  • 18. Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus.
    Yamada A, Tsukagoshi N, Udaka S, Sasaki T, Makino S, Nakamura S, Little C, Tomita M, Ikezawa H.
    Eur J Biochem; 1988 Aug 01; 175(2):213-20. PubMed ID: 2841128
    [Abstract] [Full Text] [Related]

  • 19. Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli.
    Hussain M, Carlino A, Madonna MJ, Lampen JO.
    J Bacteriol; 1985 Oct 01; 164(1):223-9. PubMed ID: 3930467
    [Abstract] [Full Text] [Related]

  • 20. Cloning of the beta-amylase gene from Bacillus cereus and characteristics of the primary structure of the enzyme.
    Nanmori T, Nagai M, Shimizu Y, Shinke R, Mikami B.
    Appl Environ Microbiol; 1993 Feb 01; 59(2):623-7. PubMed ID: 8434930
    [Abstract] [Full Text] [Related]

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