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Volumn 10, Issue 2, 2000, Pages 244-250

Cloning and characterization of α-glucosidase gene from thermophilic Bacillus sp. DG0303

Author keywords

Glucosidase; Expression; Gene cloning; Nucleotide sequence; Oligo 1,6 glucosidase

Indexed keywords

ALPHA GLUCOSIDASE;

EID: 0034081939     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (9)

References (27)
  • 1
    • 0017868340 scopus 로고
    • Control of transcription termination
    • Adhya, S. and M. Gottesman. 1978. Control of transcription termination. Annu. Rev. Biochem. 47: 967-996.
    • (1978) Annu. Rev. Biochem. , vol.47 , pp. 967-996
    • Adhya, S.1    Gottesman, M.2
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0025270515 scopus 로고
    • Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida
    • Consevage, M. W. and A. T. Phillips. 1990. Sequence analysis of the hutH gene encoding histidine ammonia-lyase in Pseudomonas putida. J. Bacteriol. 172: 2224-2229.
    • (1990) J. Bacteriol. , vol.172 , pp. 2224-2229
    • Consevage, M.W.1    Phillips, A.T.2
  • 5
    • 0001785135 scopus 로고
    • Thermostabilization of proteins
    • Gupta, M. N. 1991. Thermostabilization of proteins. Biotechnol. Appl. Biochem. 14: 1-11.
    • (1991) Biotechnol. Appl. Biochem. , vol.14 , pp. 1-11
    • Gupta, M.N.1
  • 6
    • 0026040317 scopus 로고
    • Comparison of the domain-level organization of starch hydrolases and related enzymes
    • Jesperson, H. M., E. A. MacGregor, M. R. Sierks, and B. Svensson. 1991. Comparison of the domain-level organization of starch hydrolases and related enzymes. Biochem. J. 280: 51-55.
    • (1991) Biochem. J. , vol.280 , pp. 51-55
    • Jesperson, H.M.1    MacGregor, E.A.2    Sierks, M.R.3    Svensson, B.4
  • 7
    • 0032087621 scopus 로고    scopus 로고
    • Clustered proline residues around the active-site cleft in thermostable oligo-1,6-glucosidase of Bacillus flavocaldarius KP1228
    • Kashiwabara, S., Y. Matsuki, T. Kishimoto, and Y. Suzuki. 1998. Clustered proline residues around the active-site cleft in thermostable oligo-1,6-glucosidase of Bacillus flavocaldarius KP1228. Biosci. Biotechnol. Biochem. 62: 1093-1102.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1093-1102
    • Kashiwabara, S.1    Matsuki, Y.2    Kishimoto, T.3    Suzuki, Y.4
  • 9
    • 0027479986 scopus 로고
    • Enzymes from high-temperature microorganisms
    • Kelly, R. M. and S. H. Brown. 1993. Enzymes from high-temperature microorganisms. Curr. Opinion Biotechnol. 4: 188-192.
    • (1993) Curr. Opinion Biotechnol. , vol.4 , pp. 188-192
    • Kelly, R.M.1    Brown, S.H.2
  • 10
    • 0027176843 scopus 로고
    • Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 resolution X-ray analysis
    • Kizaki, H., Y. Hata, K. Watanabe, Y. Katsube, and Y. Suzuki. 1993. Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 resolution X-ray analysis. J. Biochem. (Tokyo) 113: 646-649.
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 646-649
    • Kizaki, H.1    Hata, Y.2    Watanabe, K.3    Katsube, Y.4    Suzuki, Y.5
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227: 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 12
    • 85006100126 scopus 로고
    • Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: Molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli. Biosci
    • Lee, S. H., H. Taguchi, E. Yoshimura, E. Minagawa, S. Kaminogawa, T. Ohta, and H. Matsuzawa. 1994. Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: Molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli. Biosci. Biotechnol. Biochem. 58: 1490-1495.
    • (1994) Biotechnol. Biochem. , vol.58 , pp. 1490-1495
    • Lee, S.H.1    Taguchi, H.2    Yoshimura, E.3    Minagawa, E.4    Kaminogawa, S.5    Ohta, T.6    Matsuzawa, H.7
  • 13
    • 0024514666 scopus 로고
    • A supersecondary structure predicted to be common to several α-1,4-D-glucan-cleaving enzymes
    • MacGregor, E. A. and B. Svensson. 1989. A supersecondary structure predicted to be common to several α-1,4-D-glucan-cleaving enzymes. Biochem. J. 259: 145-152.
    • (1989) Biochem. J. , vol.259 , pp. 145-152
    • MacGregor, E.A.1    Svensson, B.2
  • 14
    • 85010439719 scopus 로고
    • A procedure for the isolation of deoxyribonucleic acid from microorganisms
    • Marmur, J. 1961. A procedure for the isolation of deoxyribonucleic acid from microorganisms. J. Mol. Biol. 3: 208-218.
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 15
    • 0033574176 scopus 로고    scopus 로고
    • Characterization of psychrophilic alanine racemase from Bacillus psychrosaccharolyticus
    • Okubo, Y., K. Yokoigawa, N. Esaki, K. Soda, and H. Kawai. 1999. Characterization of psychrophilic alanine racemase from Bacillus psychrosaccharolyticus. Biochem. Biophys. Res. Commun. 256: 333-340.
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 333-340
    • Okubo, Y.1    Yokoigawa, K.2    Esaki, N.3    Soda, K.4    Kawai, H.5
  • 16
    • 0031855739 scopus 로고    scopus 로고
    • Purification and characterization of a Bacillus sp. DG0303 thermostable α-glucosidase with oligo-1,6-glucosidase activity
    • Park, J.-S., I.-H. Kim, and Y.-E. Lee. 1998. Purification and characterization of a Bacillus sp. DG0303 thermostable α-glucosidase with oligo-1,6-glucosidase activity. J. Microbiol. Biotechnol. 8: 270-276.
    • (1998) J. Microbiol. Biotechnol. , vol.8 , pp. 270-276
    • Park, J.-S.1    Kim, I.-H.2    Lee, Y.-E.3
  • 17
    • 0024120513 scopus 로고
    • A cell-associated oligo-1,6-α-glucosidase from an extremely thermophilic anaerobic bacterium, Thermoanaerobium Tok6-B1
    • Plant, A. R., S. Parrat, R. M. Daniel, and H. W. Morgan. 1988. A cell-associated oligo-1,6-α-glucosidase from an extremely thermophilic anaerobic bacterium, Thermoanaerobium Tok6-B1. Biochem. J. 255: 865-868.
    • (1988) Biochem. J. , vol.255 , pp. 865-868
    • Plant, A.R.1    Parrat, S.2    Daniel, R.M.3    Morgan, H.W.4
  • 18
    • 0023157613 scopus 로고
    • Sequence of the Ampullariella sp. strain 3876 gene coding for xylose isomerase
    • Saari, G. C., A. A. Kumar, G. H. Kawasaki, M. Y. Insley, and P. J. Ohara. 1987. Sequence of the Ampullariella sp. strain 3876 gene coding for xylose isomerase. J. Bacteriol. 169: 612-618.
    • (1987) J. Bacteriol. , vol.169 , pp. 612-618
    • Saari, G.C.1    Kumar, A.A.2    Kawasaki, G.H.3    Insley, M.Y.4    Ohara, P.J.5
  • 21
    • 0001767586 scopus 로고
    • A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases
    • Suzuki, Y., K. Oishi, H. Nakano, and T. Nagayama. 1987. A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases. Appl. Microbiol. Biotechnol. 26: 546-551.
    • (1987) Appl. Microbiol. Biotechnol. , vol.26 , pp. 546-551
    • Suzuki, Y.1    Oishi, K.2    Nakano, H.3    Nagayama, T.4
  • 22
    • 0029893110 scopus 로고    scopus 로고
    • Thermozymes: Identifying molecular determinants of protein structural and functional stability
    • Vieille, C. and J. G. Zeikus. 1996. Thermozymes: Identifying molecular determinants of protein structural and functional stability. Trends Biotechnol. 14: 183-190.
    • (1996) Trends Biotechnol. , vol.14 , pp. 183-190
    • Vieille, C.1    Zeikus, J.G.2
  • 23
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira, J. and J. Messing. 1987. Production of single-stranded plasmid DNA. Methods Enzymol. 153: 1-11.
    • (1987) Methods Enzymol. , vol.153 , pp. 1-11
    • Vieira, J.1    Messing, J.2
  • 24
    • 0002015548 scopus 로고
    • Thermostable enzyme production
    • Wasserman, B. P. 1984. Thermostable enzyme production. Food Technol. 38: 78-89.
    • (1984) Food Technol. , vol.38 , pp. 78-89
    • Wasserman, B.P.1
  • 25
    • 0026316725 scopus 로고
    • 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., K. Chishiro, K. Kitamura, and Y. Suzuki. 1991. 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. J. Biol. Chem. 266: 24287-24294.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24287-24294
    • Watanabe, K.1    Chishiro, K.2    Kitamura, K.3    Suzuki, Y.4
  • 26
    • 0025158414 scopus 로고
    • Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene
    • Watanabe, K., K. Kitamura, H. Iha, and Y. Suzuki. 1990. Primary structure of the oligo-1,6-glucosidase of Bacillus cereus ATCC7064 deduced from the nucleotide sequence of the cloned gene. Eur. J. Biochem. 192: 609-620.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 609-620
    • Watanabe, K.1    Kitamura, K.2    Iha, H.3    Suzuki, Y.4
  • 27
    • 0028130117 scopus 로고
    • Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule
    • Watanabe, K., T. Masuda, H. Ohashi, H. Mihara, and Y. Suzuki. 1994. Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule. Eur. J. Biochem. 226: 277-283.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 277-283
    • Watanabe, K.1    Masuda, T.2    Ohashi, H.3    Mihara, H.4    Suzuki, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.