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Volumn 44, Issue 5, 1996, Pages 629-634

Bacillus stearothermophilus ATCC12016 α-glucosidase specific for α-1,4 bonds of maltosaccharides and α-glucans shows high amino acid sequence similarities to seven α-D-glucohydrolases with different substrate specificity

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS CEREUS; BACILLUS SP.; ESCHERICHIA COLI; GEOBACILLUS STEAROTHERMOPHILUS; GEOBACILLUS THERMOGLUCOSIDASIUS; SACCHAROMYCES PASTORIANUS; STREPTOCOCCUS MUTANS;

EID: 0030019468     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00172496     Document Type: Article
Times cited : (29)

References (23)
  • 1
    • 0021943866 scopus 로고
    • Laboratory methods. Supercoil sequencing: A fast and simple method for sequencing plasmid DNA
    • Chen EY, Seeburg PH (1985) Laboratory methods. Supercoil sequencing: a fast and simple method for sequencing plasmid DNA. DNA 4:165-170
    • (1985) DNA , vol.4 , pp. 165-170
    • Chen, E.Y.1    Seeburg, P.H.2
  • 2
    • 0000499414 scopus 로고
    • Prediction of secondary structure of proteins by means of hydrophobicity profiles
    • Cid H, Bunster M, Arriagada E, Campos M (1982) Prediction of secondary structure of proteins by means of hydrophobicity profiles. FEBS Lett 150:247-254
    • (1982) FEBS Lett , vol.150 , pp. 247-254
    • Cid, H.1    Bunster, M.2    Arriagada, E.3    Campos, M.4
  • 3
    • 0022473663 scopus 로고
    • Primary structure of the maltose gene of the MAL6 locus of Saccharomyces carlsbergensis
    • Hong SH, Murmur J (1986) Primary structure of the maltose gene of the MAL6 locus of Saccharomyces carlsbergensis. Gene 41:75-84
    • (1986) Gene , vol.41 , pp. 75-84
    • Hong, S.H.1    Murmur, J.2
  • 4
    • 0028173219 scopus 로고
    • Parallel β/α-burrels of α-amylase, cyclodextrin glycosyltransferase and oligo-1,6-glucosidase versus the barrel of β-amylase: Evolutionary distance is a reflection of unrelated sequences
    • Janeček S (1994) Parallel β/α-burrels of α-amylase, cyclodextrin glycosyltransferase and oligo-1,6-glucosidase versus the barrel of β-amylase: evolutionary distance is a reflection of unrelated sequences. FEBS Lett 353:119-123
    • (1994) FEBS Lett , vol.353 , pp. 119-123
    • Janeček, S.1
  • 5
    • 1542387105 scopus 로고
    • Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 Å resolution X-ray analysis
    • Tokyo
    • Kizaki H, Hata Y, Watanabe K, Katsube Y, Suzuki Y (1993) Polypeptide folding of Bacillus cereus ATCC7064 oligo-1,6-glucosidase revealed by 3.0 Å resolution X-ray analysis. J Biochem (Tokyo) 205:249-256
    • (1993) J Biochem , vol.205 , pp. 249-256
    • Kizaki, H.1    Hata, Y.2    Watanabe, K.3    Katsube, Y.4    Suzuki, Y.5
  • 6
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 7
    • 0003804882 scopus 로고
    • Oxford University Press, Oxford
    • Lewin B (1994) Gene. 5th ed. Oxford University Press, Oxford, pp 115-119
    • (1994) Gene. 5th Ed. , pp. 115-119
    • Lewin, B.1
  • 8
    • 0021395910 scopus 로고
    • Structure and possible catalytic residues of Taka-amylase A
    • Tokyo
    • Matsuura Y, Kusunoki M, Harada W, Kakudo M (1984) Structure and possible catalytic residues of Taka-amylase A. J Biochem (Tokyo) 95:697-702
    • (1984) J Biochem , vol.95 , pp. 697-702
    • Matsuura, Y.1    Kusunoki, M.2    Harada, W.3    Kakudo, M.4
  • 9
    • 0021837957 scopus 로고
    • Nucleotide sequence of the Bacillus stearothermophilus α-amylase gene
    • Nakajima R, Imanuka T, Aiba S (1985) Nucleotide sequence of the Bacillus stearothermophilus α-amylase gene. J Bacteriol 163:401-406
    • (1985) J Bacteriol , vol.163 , pp. 401-406
    • Nakajima, R.1    Imanuka, T.2    Aiba, S.3
  • 10
    • 0028206870 scopus 로고
    • Structure and expression of a gene coding for thermostable α-glucosidase with a broad substrate specificity from Bacillus sp. SAM1606
    • Nakao M, Nakayamu T, Kakudo A, Inohara M, Hurada M, Omura F, Shibano Y (1994) Structure and expression of a gene coding for thermostable α-glucosidase with a broad substrate specificity from Bacillus sp. SAM1606. Eur J Biochem 220:293-300
    • (1994) Eur J Biochem , vol.220 , pp. 293-300
    • Nakao, M.1    Nakayamu, T.2    Kakudo, A.3    Inohara, M.4    Hurada, M.5    Omura, F.6    Shibano, Y.7
  • 11
    • 0021324568 scopus 로고
    • Improved method for detection of glycosidases in bacterial colonies
    • Paoni NF, Arroyo RL (1984) Improved method for detection of glycosidases in bacterial colonies. Appl Environ Microbiol 47:208-209
    • (1984) Appl Environ Microbiol , vol.47 , pp. 208-209
    • Paoni, N.F.1    Arroyo, R.L.2
  • 12
    • 0028061196 scopus 로고
    • Trehalose-6-phosphate hydrolase of Escherichia coli
    • Rimmele M, Boos W (1994) Trehalose-6-phosphate hydrolase of Escherichia coli. J Bacteriol 176:5654-5664
    • (1994) J Bacteriol , vol.176 , pp. 5654-5664
    • Rimmele, M.1    Boos, W.2
  • 13
    • 0018588890 scopus 로고
    • Regulatory sequences involved in the promotion and termination of RNA transcription
    • Rosenberg M, Court D (1979) Regulatory sequences involved in the promotion and termination of RNA transcription. Annu Rev Genet 13:319-353
    • (1979) Annu Rev Genet , vol.13 , pp. 319-353
    • Rosenberg, M.1    Court, D.2
  • 14
    • 0025361853 scopus 로고
    • Nucleotide sequence of the dextran glucosidase(DexB)gene of Streptococcus mutans
    • Russel RRB, Ferretti JJ (1990) Nucleotide sequence of the dextran glucosidase(DexB)gene of Streptococcus mutans. J Gen Microbiol 136:803-810
    • (1990) J Gen Microbiol , vol.136 , pp. 803-810
    • Russel, R.R.B.1    Ferretti, J.J.2
  • 16
    • 0019769456 scopus 로고
    • Determination of nucleotide sequence in DNA
    • Sanger F (1981) Determination of nucleotide sequence in DNA. Science 214:1205-1210
    • (1981) Science , vol.214 , pp. 1205-1210
    • Sanger, F.1
  • 17
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome-binding sites
    • Shine J, Dalgarno L (1974) The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome-binding sites. Proc Natl Acad Sci USA 71:1342-1346
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 18
    • 0342674201 scopus 로고
    • Assignment of a p-nitrophenyl-α-D-glucopyranoside-hydrolyzing α-glucosidase of Bacillus stearothermophilus ATCC12016 to an novel exo-α-1.4-glucosidase active for oligomaltosaccharides and α-glucans
    • Suzuki Y, Shinji M, Eto N (1984) Assignment of a p-nitrophenyl-α-D-glucopyranoside-hydrolyzing α-glucosidase of Bacillus stearothermophilus ATCC12016 to an novel exo-α-1.4-glucosidase active for oligomaltosaccharides and α-glucans. Biochim Biophys Acta 787:281-289
    • (1984) Biochim Biophys Acta , vol.787 , pp. 281-289
    • Suzuki, Y.1    Shinji, M.2    Eto, N.3
  • 19
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family: Catalytic mechanism, substrate specificity, and stability
    • Svensson B (1994) Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Mol Biol 25:141-157
    • (1994) Plant Mol Biol , vol.25 , pp. 141-157
    • Svensson, B.1
  • 20
    • 0026439111 scopus 로고
    • Cloning and expression of a thermostable exo-α-1,4-glucosidase from Bacillus stearothermophilus ATCC12016 in Escherichia coli
    • Takii Y, Daimon K, Suzuki Y (1992) Cloning and expression of a thermostable exo-α-1,4-glucosidase from Bacillus stearothermophilus ATCC12016 in Escherichia coli. Appl Microbiol Biotechnol 38:243-247
    • (1992) Appl Microbiol Biotechnol , vol.38 , pp. 243-247
    • Takii, Y.1    Daimon, K.2    Suzuki, Y.3
  • 21
    • 0028130117 scopus 로고
    • 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 (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
  • 22
    • 0026475673 scopus 로고
    • Detection of secondary structure elements in proteins by hydrophobic cluster analysis
    • Woodcock S, Mornon SP, Henrissat B (1992) Detection of secondary structure elements in proteins by hydrophobic cluster analysis. Protein Eng 5:629-635
    • (1992) Protein Eng , vol.5 , pp. 629-635
    • Woodcock, S.1    Mornon, S.P.2    Henrissat, B.3
  • 23
    • 0000274849 scopus 로고
    • Nucleotide sequence of alkalophilic Bacillus oligo-1,6-glucosidase gene and the properties of the gene product by Escherichia coli HB101
    • Yamamoto M, Horikoshi K (1990) Nucleotide sequence of alkalophilic Bacillus oligo-1,6-glucosidase gene and the properties of the gene product by Escherichia coli HB101. Denpun Kagaku 37:137-144
    • (1990) Denpun Kagaku , vol.37 , pp. 137-144
    • Yamamoto, M.1    Horikoshi, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.