메뉴 건너뛰기




Volumn 34, Issue 4, 2001, Pages 347-354

Novel α-Glucosidase from Extreme Thermophile Thermus caldophilus GK24

Author keywords

Glucosidase; Gene cloning; Thermostable enzyme; Thermus sp; Transglucosylation

Indexed keywords


EID: 0035617859     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (28)

References (36)
  • 1
    • 0031934403 scopus 로고    scopus 로고
    • Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermatoga maritama
    • Bibel, M., Brettl, C., Gosslar, U., Kriegshauser, G. and Liebl, W. (1998) Isolation and analysis of genes for amylolytic enzymes of the hyperthermophilic bacterium Thermatoga maritama. FEMS Microbiol. Lett. 158, 9-15.
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 9-15
    • Bibel, M.1    Brettl, C.2    Gosslar, U.3    Kriegshauser, G.4    Liebl, W.5
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248.
    • (1976) Anal. Biochem. , vol.72 , pp. 248
    • Bradford, M.M.1
  • 3
    • 3042882508 scopus 로고    scopus 로고
    • A thermostable xylose isomerase from Thermus thermophilus
    • Chang, C., Park, B. C., Lee, D. S. and Suh, S. W. (1998) A thermostable xylose isomerase from Thermus thermophilus. J. Biochem. Mol. Biol. 31, 600-603.
    • (1998) J. Biochem. Mol. Biol. , vol.31 , pp. 600-603
    • Chang, C.1    Park, B.C.2    Lee, D.S.3    Suh, S.W.4
  • 4
    • 0014235959 scopus 로고
    • Assay of intestinal disaccharidases
    • Dahlqvist, A. (1968) Assay of intestinal disaccharidases. Anal. Biochem. 22, 99.
    • (1968) Anal. Biochem. , vol.22 , pp. 99
    • Dahlqvist, A.1
  • 5
    • 0024026526 scopus 로고
    • Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrose-isomaltase complex
    • Hoefsloot, L. H., Hoogeveen-Westerveld, M., Kroos, M. A., van Beeumen, J., Reuser, A. J. J. and Oostra, B. A. (1989) Primary structure and processing of lysosomal alpha-glucosidase; homology with the intestinal sucrose-isomaltase complex. EMBO J. 7, 1697-1704.
    • (1989) EMBO J. , vol.7 , pp. 1697-1704
    • Hoefsloot, L.H.1    Hoogeveen-Westerveld, M.2    Kroos, M.A.3    Van Beeumen, J.4    Reuser, A.J.J.5    Oostra, B.A.6
  • 6
    • 0022473663 scopus 로고
    • Primary structure of the maltase gene of the MAL6 locus of Saccharomyces carlsbergensis
    • Hong, S. H. and Mamur, J. (1986) Primary structure of the maltase gene of the MAL6 locus of Saccharomyces carlsbergensis. Gene 41, 75.
    • (1986) Gene , vol.41 , pp. 75
    • Hong, S.H.1    Mamur, J.2
  • 7
    • 0022504432 scopus 로고
    • The sucrase-isomaltase complex: Primary structure, membrane orientation, and evolution of stalked, intrinsic brush-border protein
    • Hunzuiker, W., Spiess, M., Semensa, G. and Lodish, H. F. (1986) The sucrase-isomaltase complex: primary structure, membrane orientation, and evolution of stalked, intrinsic brush-border protein. Cell 46, 227.
    • (1986) Cell , vol.46 , pp. 227
    • Hunzuiker, W.1    Spiess, M.2    Semensa, G.3    Lodish, H.F.4
  • 8
    • 0026040317 scopus 로고
    • Comparison of the domain-level organization of starch hydrolases and related enzymes
    • Jesperson, H. M., MacGregor, E. A., Sierks, M. R. and Svensson, B. (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
  • 10
  • 12
    • 0031591105 scopus 로고    scopus 로고
    • Cloning analysis of the DNA polymerase encoding gene from Thermus caldophilus GK24
    • Kwon, S. T., Kim, J. S., Park, J. H., Kim, H. K. and Lee, D. S. (1997) Cloning analysis of the DNA polymerase encoding gene from Thermus caldophilus GK24. Mol. Cells 7, 264-271.
    • (1997) Mol. Cells , vol.7 , pp. 264-271
    • Kwon, S.T.1    Kim, J.S.2    Park, J.H.3    Kim, H.K.4    Lee, D.S.5
  • 13
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F. (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
  • 14
    • 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 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0033411315 scopus 로고    scopus 로고
    • Heterologous expression of lignin peroxidase H2 in Escherichia coli: In vitro refolding and activation
    • Lee, D. and Kim, D. H. (1999) Heterologous expression of lignin peroxidase H2 in Escherichia coli: in vitro refolding and activation. J. Biochem. Mol. Biol. 32, 486-491.
    • (1999) J. Biochem. Mol. Biol. , vol.32 , pp. 486-491
    • Lee, D.1    Kim, D.H.2
  • 16
    • 0348190064 scopus 로고    scopus 로고
    • Temperature-dependent expression of Escherichia coli thioredoxin gene
    • Lee, J. J., Park, E. H., Ahn, K. S. and Lim, C. J. (2000) Temperature-dependent expression of Escherichia coli thioredoxin gene. J. Biochem. Mol. Biol. 33, 166-171.
    • (2000) J. Biochem. Mol. Biol. , vol.33 , pp. 166-171
    • Lee, J.J.1    Park, E.H.2    Ahn, K.S.3    Lim, C.J.4
  • 17
    • 0024514666 scopus 로고
    • A super-secondary structure predicted to be common to several α-1,4-D-glucan-cleaving enzymes
    • MacGregor, E. A. and Svensson, B. (1989) A super-secondary 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
  • 20
    • 0028206870 scopus 로고
    • Structure and expression of gene coding for thermostable α-glucosidase with broad substrate specificity from Bacillus sp. SAM1606
    • Nakao, M., Nakayama, T., Kakudo, A., Inohara, M., Harada, M., Omura, F. and Shibano, Y. (1994b) Structure and expression of gene coding for thermostable α-glucosidase with 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    Nakayama, T.2    Kakudo, A.3    Inohara, M.4    Harada, M.5    Omura, F.6    Shibano, Y.7
  • 21
    • 85007844906 scopus 로고
    • Purification and characterization of α-glucosidase from Torulospora pretoriensis YK-1
    • Oda, Y., Iwamoto, H., Hiromi, K. and Tonomura, K. (1993) Purification and characterization of α-glucosidase from Torulospora pretoriensis YK-1. Biosci. Biotech. Biochem. 57, 1902-1905.
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 1902-1905
    • Oda, Y.1    Iwamoto, H.2    Hiromi, K.3    Tonomura, K.4
  • 22
    • 0029868220 scopus 로고    scopus 로고
    • Molecular cloning of cDNA and analysis of expression of the gene for α-glucosidase from the hypopharyngeal gland of the honeybee Apis mellifera L
    • Ohashi, K., Sawata, M., Takeuchi, H., Natori, S. and Kubo, T. (1996) Molecular cloning of cDNA and analysis of expression of the gene for α-glucosidase from the hypopharyngeal gland of the honeybee Apis mellifera L. Biochem. Biophys. Res. Commun. 221, 380-385.
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 380-385
    • Ohashi, K.1    Sawata, M.2    Takeuchi, H.3    Natori, S.4    Kubo, T.5
  • 23
    • 0027191041 scopus 로고
    • Purification and characterization of Thermus caldophilus GK24 DNA polymerase
    • Park, J. H., Kim, J. S., Kwon, S. and Lee, D. S. (1993) Purification and characterization of Thermus caldophilus GK24 DNA polymerase. Eur. J. Biochem. 214, 135-140.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 135-140
    • Park, J.H.1    Kim, J.S.2    Kwon, S.3    Lee, D.S.4
  • 27
    • 0029972508 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression of a cDNA encoding α-glucosidase from Mucor javanicus
    • Sugimoto, M. and Suzuki, Y. (1996) Molecular cloning, sequencing, and expression of a cDNA encoding α-glucosidase from Mucor javanicus. J. Biochem. 119, 500-505.
    • (1996) J. Biochem. , vol.119 , pp. 500-505
    • Sugimoto, M.1    Suzuki, Y.2
  • 28
    • 0348192041 scopus 로고
    • A relationship between efficiency of isomaltooligosaccharide hydrolysis and thermostability of six Bacillus oligo-1,6-glucosidases
    • Suzuki, Y. and Oishi, K. (1989) A relationship between efficiency of isomaltooligosaccharide hydrolysis and thermostability of six Bacillus oligo-1,6-glucosidases. Appl. Microbiol. Biotechnol. 31, 32-37.
    • (1989) Appl. Microbiol. Biotechnol. , vol.31 , pp. 32-37
    • Suzuki, Y.1    Oishi, K.2
  • 29
    • 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-glucossidases
    • Suzuki, Y., Aoki, R. and Hayashi, H (1987) A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucossidases. Appl. Microbiol. Biotechnol. 26, 546-551.
    • (1987) Appl. Microbiol. Biotechnol. , vol.26 , pp. 546-551
    • Suzuki, Y.1    Aoki, R.2    Hayashi, H.3
  • 30
    • 0019944510 scopus 로고
    • Assignment of p-nitrophenyl-α-D-glucopyranoside hydrolyzing α-glucosidase of Bacillus cereus ATCC 7064 to an exo-oligo-1,6-glucosidase
    • Suzuki, Y., Aoki, R. and Hayashi H. (1982) Assignment of p-nitrophenyl-α-D-glucopyranoside hydrolyzing α-glucosidase of Bacillus cereus ATCC 7064 to an exo-oligo-1,6-glucosidase. Biochim. Biophys. Acta 704, 476-483.
    • (1982) Biochim. Biophys. Acta , vol.704 , pp. 476-483
    • Suzuki, Y.1    Aoki, R.2    Hayashi, H.3
  • 31
    • 0017096152 scopus 로고
    • Purification and properties of extracellular α-Glucosidase of a thermophile, Bacillus thermoglucosidasius KP 1006
    • Suzuki, Y., Yuki, T., Kishigami, T. and Abe, S. (1976) Purification and properties of extracellular α-Glucosidase of a thermophile, Bacillus thermoglucosidasius KP 1006. Biochim. Biophys. Acta 445, 386-397.
    • (1976) Biochim. Biophys. Acta , vol.445 , pp. 386-397
    • Suzuki, Y.1    Yuki, T.2    Kishigami, T.3    Abe, S.4
  • 32
    • 0020122141 scopus 로고
    • Heat stable and fructose 1,6-biphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium
    • Taguchi, H., Yamashita, M., Matsuzawa, H. and Ohta, T. (1982) Heat stable and fructose 1,6-biphosphate-activated L-lactate dehydrogenase from an extremely thermophilic bacterium. J. Biochem. (Tokyo) 91, 1343-1348.
    • (1982) J. Biochem. (Tokyo) , vol.91 , pp. 1343-1348
    • Taguchi, H.1    Yamashita, M.2    Matsuzawa, H.3    Ohta, T.4
  • 33
    • 0017918825 scopus 로고
    • α-Glucosidase, a membrane-bound enzyme of α-glucan metabolism in Bacillus amyloliquefaciens
    • Urlaub, H. and Wober, G. (1978) α-Glucosidase, a membrane-bound enzyme of α-glucan metabolism in Bacillus amyloliquefaciens. Biochim. Biophys. Acta 522, 161-173.
    • (1978) Biochim. Biophys. Acta , vol.522 , pp. 161-173
    • Urlaub, H.1    Wober, G.2
  • 35
    • 0026316725 scopus 로고
    • Proline residues responsible for thermostability occur with high frequency on the loop regions of extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006
    • Watanabe, K., Chishiro, K., Kitamura, K. and Suzuki, Y. (1991) Proline residues responsible for thermostability occur with high frequency on the loop regions of 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
  • 36
    • 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., Kitamura, K., Iha, H. and Suzuki, Y. (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.