Watanabe K - Search Results

1

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. Watanabe K, et al. Appl Environ Microbiol. 1996 Jun;62(6):2066-73. doi: 10.1128/aem.62.6.2066-2073.1996. Appl Environ Microbiol. 1996. PMID: 8787404 Free PMC article.

Judging from proline residues occurring in B. coagulans oligo-1,6-glucosidase and the structural requirement for proline substitution (second site of the beta turn and first turn of the alpha helix) (K. Watanabe, T. Masuda, H. Ohashi, H. Mihara, and Y. Suzuki, Eur. …

Judging from proline residues occurring in B. coagulans oligo-1,6-glucosidase and the structural requirement for proline substitution (secon …

2

Identification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6-glucosidase.

Watanabe K, Miyake K, Suzuki Y. Watanabe K, et al. Biosci Biotechnol Biochem. 2001 Sep;65(9):2058-64. doi: 10.1271/bbb.65.2058. Biosci Biotechnol Biochem. 2001. PMID: 11676021 Free article.

3

A thermostable collagenolytic protease with a very large molecular mass produced by thermophilic Bacillus sp. strain MO-1.

Okamoto M, Yonejima Y, Tsujimoto Y, Suzuki Y, Watanabe K. Okamoto M, et al. Among authors: watanabe k. Appl Microbiol Biotechnol. 2001 Oct;57(1-2):103-8. doi: 10.1007/s002530100731. Appl Microbiol Biotechnol. 2001. PMID: 11693905

4

Gene cloning, expression, and crystallization of a thermostable exo-inulinase from Geobacillus stearothermophilus KP1289.

Tsujimoto Y, Watanabe A, Nakano K, Watanabe K, Matsui H, Tsuji K, Tsukihara T, Suzuki Y. Tsujimoto Y, et al. Among authors: watanabe k, watanabe a. Appl Microbiol Biotechnol. 2003 Aug;62(2-3):180-5. doi: 10.1007/s00253-003-1261-3. Epub 2003 Feb 22. Appl Microbiol Biotechnol. 2003. PMID: 12883863

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. Watanabe K, et al. J Mol Biol. 1997 May 30;269(1):142-53. doi: 10.1006/jmbi.1997.1018. J Mol Biol. 1997. PMID: 9193006

6

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. Watanabe K, et al. Eur J Biochem. 1990 Sep 24;192(3):609-20. doi: 10.1111/j.1432-1033.1990.tb19267.x. Eur J Biochem. 1990. PMID: 2120057 Free article.

7

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. Watanabe K, et al. J Bacteriol. 1989 Feb;171(2):1219-22. doi: 10.1128/jb.171.2.1219-1222.1989. J Bacteriol. 1989. PMID: 2644230 Free PMC article.

8

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. Watanabe K, et al. Eur J Biochem. 1994 Dec 1;226(2):277-83. doi: 10.1111/j.1432-1033.1994.tb20051.x. Eur J Biochem. 1994. PMID: 8001545 Free article.

9

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. Kizaki H, et al. Among authors: watanabe k. J Biochem. 1993 Jun;113(6):646-9. doi: 10.1093/oxfordjournals.jbchem.a124097. J Biochem. 1993. PMID: 8370659 Free article.

10

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. Watanabe K, et al. J Biol Chem. 1991 Dec 25;266(36):24287-94. J Biol Chem. 1991. PMID: 1761534 Free article.

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