메뉴 건너뛰기




Volumn 67, Issue 2, 2007, Pages 164-173

The action mode of Thermus aquaticus YT-1 4-α-glucanotransferase and its chimeric enzymes introduced with starch-binding domain on amylose and amylopectin

Author keywords

4 glucanotransferase; Amylopectin; Amylose; Cyclo amylose; Starch binding domain (SBD); Thermus aquaticus YT 1

Indexed keywords

AMINO ACIDS; CATALYSIS; DECAY (ORGANIC); GENES; NUCLEIC ACIDS; PROTEINS;

EID: 33751005820     PISSN: 01448617     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.carbpol.2006.05.018     Document Type: Article
Times cited : (78)

References (40)
  • 1
    • 1542495429 scopus 로고    scopus 로고
    • Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 1 with maltooligosaccharides demonstrate the role of domain N acting as a starch-binding domain
    • Abe A., Tonozuka T., Sakano Y., and Kamitori S. Complex structures of Thermoactinomyces vulgaris R-47 α-amylase 1 with maltooligosaccharides demonstrate the role of domain N acting as a starch-binding domain. Journal of Molecular Biology 335 (2004) 811-822
    • (2004) Journal of Molecular Biology , vol.335 , pp. 811-822
    • Abe, A.1    Tonozuka, T.2    Sakano, Y.3    Kamitori, S.4
  • 3
    • 0037375065 scopus 로고    scopus 로고
    • A cycloamylose-froming hyperthermostable 4-α-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli
    • Bhuiyan S.H., Kitaoka M., and Hayashi K. A cycloamylose-froming hyperthermostable 4-α-glucanotransferase of Aquifex aeolicus expressed in Escherichia coli. Journal of Molecular Catalysis B-Enzymatic 22 (2003) 45-53
    • (2003) Journal of Molecular Catalysis B-Enzymatic , vol.22 , pp. 45-53
    • Bhuiyan, S.H.1    Kitaoka, M.2    Hayashi, K.3
  • 4
    • 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. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 5
    • 0033545898 scopus 로고    scopus 로고
    • Thermodynamics of reversible and irreversible unfolding and domain interactions of glucoamylase from Aspergillus niger studied by differential scanning and isothermal titration calorimetry
    • Christensen T., Svensson B., and Sigurskjold B. Thermodynamics of reversible and irreversible unfolding and domain interactions of glucoamylase from Aspergillus niger studied by differential scanning and isothermal titration calorimetry. Biochemistry 38 (1999) 6300-6310
    • (1999) Biochemistry , vol.38 , pp. 6300-6310
    • Christensen, T.1    Svensson, B.2    Sigurskjold, B.3
  • 7
    • 0000888610 scopus 로고
    • Organization of starch granules
    • Whistler R.L., BeMiller J.N., and Paschall E.F. (Eds), Academic Press, Orlando, FL
    • French D. Organization of starch granules. In: Whistler R.L., BeMiller J.N., and Paschall E.F. (Eds). Starch chemistry and technology. 2nd ed. (1984), Academic Press, Orlando, FL 184
    • (1984) Starch chemistry and technology. 2nd ed. , pp. 184
    • French, D.1
  • 8
    • 0035834494 scopus 로고    scopus 로고
    • Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose
    • Giardina T., Gunning A.P., Juge N., Faulds C.B., Furniss C.S., Svensson B., et al. Both binding sites of the starch-binding domain of Aspergillus niger glucoamylase are essential for inducing a conformational change in amylose. Journal of Molecular Biology 313 (2001) 1149-1159
    • (2001) Journal of Molecular Biology , vol.313 , pp. 1149-1159
    • Giardina, T.1    Gunning, A.P.2    Juge, N.3    Faulds, C.B.4    Furniss, C.S.5    Svensson, B.6
  • 9
    • 0030730274 scopus 로고    scopus 로고
    • Molecular analysis of a Clostridium butyricum NCIMB 7423 gene encoding 4-α-glucanotransferase and characterization of the recombinant enzyme produced in Escherichia coli
    • Goda S.K., Eissa O., Akhtar M., and Minton N.P. Molecular analysis of a Clostridium butyricum NCIMB 7423 gene encoding 4-α-glucanotransferase and characterization of the recombinant enzyme produced in Escherichia coli. Microbiology 143 (1997) 3287-3294
    • (1997) Microbiology , vol.143 , pp. 3287-3294
    • Goda, S.K.1    Eissa, O.2    Akhtar, M.3    Minton, N.P.4
  • 10
    • 84989102482 scopus 로고
    • Sedimentation field-flow fractionation combined with multi-angle laser-light scattering applied for characterization of starch polymers
    • Hanselmann R., Ehrat M., and Widmer H.M. Sedimentation field-flow fractionation combined with multi-angle laser-light scattering applied for characterization of starch polymers. Starch 47 (1995) 345-349
    • (1995) Starch , vol.47 , pp. 345-349
    • Hanselmann, R.1    Ehrat, M.2    Widmer, H.M.3
  • 12
    • 33750994988 scopus 로고    scopus 로고
    • IUBMB (International Union of Biochemistry and Molecular Biology) (1992). Enzyme nomenclature.
  • 13
    • 33644530353 scopus 로고    scopus 로고
    • The activity of barely α-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase
    • Juge N., Nøhr J., Gal-Coëffet M.-F., Kramhøft B., Furniss C.S.M., Planchot V., et al. The activity of barely α-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase. Biochimica Biophysica Acta 1764 (2006) 275-284
    • (2006) Biochimica Biophysica Acta , vol.1764 , pp. 275-284
    • Juge, N.1    Nøhr, J.2    Gal-Coëffet, M.-F.3    Kramhøft, B.4    Furniss, C.S.M.5    Planchot, V.6
  • 15
    • 22844456591 scopus 로고    scopus 로고
    • Complex formation of large-ring cyclodextrins with iodine in aqueous solution as revealed by isothermal titration calorimetry
    • Kitamura S., Nakatani K., Takaha T., and Okada S. Complex formation of large-ring cyclodextrins with iodine in aqueous solution as revealed by isothermal titration calorimetry. Macromolecular Rapid Communications 20 (1999) 612-615
    • (1999) Macromolecular Rapid Communications , vol.20 , pp. 612-615
    • Kitamura, S.1    Nakatani, K.2    Takaha, T.3    Okada, S.4
  • 16
    • 33750978489 scopus 로고    scopus 로고
    • Klavons, J.A., Dintzis, F.R., & Millard, M.M. (1997). Hydrodynamic chromatography and laser light scattering measurements of high molecular weight waxy maize amylopectins. Abstracts of Papers of the American Chemical Society, 213, 85-AGFD Part 1.
  • 17
    • 0032976301 scopus 로고    scopus 로고
    • The concept of the α-amylase family: structural similarity and common catalytic mechanism
    • Kuriki T., and Imanaka T. The concept of the α-amylase family: structural similarity and common catalytic mechanism. Journal of Bioscience and Bioengineering 87 (1999) 557-565
    • (1999) Journal of Bioscience and Bioengineering , vol.87 , pp. 557-565
    • Kuriki, T.1    Imanaka, T.2
  • 18
    • 0020421336 scopus 로고
    • Identification of base mismatches recognized by the heteroduplex-DNA-repair system of Streptococcus pneumoniae
    • Lacks S.A., Dunn J.J., and Greenberg B. Identification of base mismatches recognized by the heteroduplex-DNA-repair system of Streptococcus pneumoniae. Cell 31 (1982) 327-336
    • (1982) Cell , vol.31 , pp. 327-336
    • Lacks, S.A.1    Dunn, J.J.2    Greenberg, B.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 33244458226 scopus 로고    scopus 로고
    • Effects of α-glucanotransferase treatment on the thermo-reversibility and freeze-thaw stability of a rice starch gel
    • Lee K.Y., Kim Y.R., Park K.H., and Lee H.K. Effects of α-glucanotransferase treatment on the thermo-reversibility and freeze-thaw stability of a rice starch gel. Carbohydrate Polymers 63 (2006) 347-354
    • (2006) Carbohydrate Polymers , vol.63 , pp. 347-354
    • Lee, K.Y.1    Kim, Y.R.2    Park, K.H.3    Lee, H.K.4
  • 21
    • 33750973688 scopus 로고    scopus 로고
    • Lee, M.J. (1997). Cloning of cyclodextrin glucanotransferase gene from B. stearothermophilus ET1 and characterization of its enzymatic properties. M.S. thesis, Seoul National University, Korea.
  • 22
    • 0026660023 scopus 로고
    • Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli
    • Liebl W., Feil R., Gabelsberger J., Kellermann J., and Schleifer K.H. Purification and characterization of a novel thermostable 4-α-glucanotransferase of Thermotoga maritima cloned in Escherichia coli. European Journal of Biochemistry 207 (1992) 81-88
    • (1992) European Journal of Biochemistry , vol.207 , pp. 81-88
    • Liebl, W.1    Feil, R.2    Gabelsberger, J.3    Kellermann, J.4    Schleifer, K.H.5
  • 23
    • 0343312178 scopus 로고
    • Studies on carbohydrate-metabolizing enzymes, part 21, the α-glucosidase and d-enzyme activity of extracts of carrots and tomatoes
    • Manners D.J., and Rowe K.L. Studies on carbohydrate-metabolizing enzymes, part 21, the α-glucosidase and d-enzyme activity of extracts of carrots and tomatoes. Carbohydrate Research 9 (1969) 441-450
    • (1969) Carbohydrate Research , vol.9 , pp. 441-450
    • Manners, D.J.1    Rowe, K.L.2
  • 24
    • 0040433811 scopus 로고
    • Synthèse d'un polysaccharide de type amidon aux dèpens du maltose, en prèsence d'un extrait enzymatique d'origine bacterienne
    • Monod J., and Torriani A.M. Synthèse d'un polysaccharide de type amidon aux dèpens du maltose, en prèsence d'un extrait enzymatique d'origine bacterienne. Comptes Rendus de l'Acadèmie des Sciences 227 (1948) 240-242
    • (1948) Comptes Rendus de l'Acadèmie des Sciences , vol.227 , pp. 240-242
    • Monod, J.1    Torriani, A.M.2
  • 25
    • 0033916432 scopus 로고    scopus 로고
    • Introduction of raw starch-binding domains into Bacillus subtilis alpha-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase
    • Ohdan K., Kuriki T., Takata H., Kaneko H., and Okada S. Introduction of raw starch-binding domains into Bacillus subtilis alpha-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase. Applied and Environmental Microbiology 66 (2000) 3058-3064
    • (2000) Applied and Environmental Microbiology , vol.66 , pp. 3058-3064
    • Ohdan, K.1    Kuriki, T.2    Takata, H.3    Kaneko, H.4    Okada, S.5
  • 27
    • 37049048868 scopus 로고
    • The enzymic synthesis and degradation of starch: the disproportionating enzyme of potato
    • Peat S., Whelan W.J., and Rees W.R. The enzymic synthesis and degradation of starch: the disproportionating enzyme of potato. Journal of the Chemical Society 1956 (1956) 44-53
    • (1956) Journal of the Chemical Society , vol.1956 , pp. 44-53
    • Peat, S.1    Whelan, W.J.2    Rees, W.R.3
  • 29
    • 33750995628 scopus 로고
    • Molecular characterization of malQ, the structural gene for the Escherichia coli
    • Pugsley A.P., and Dubreuil C. Molecular characterization of malQ, the structural gene for the Escherichia coli. European Journal of Biochemistry 69 (1988) 105-115
    • (1988) European Journal of Biochemistry , vol.69 , pp. 105-115
    • Pugsley, A.P.1    Dubreuil, C.2
  • 30
    • 0028762263 scopus 로고
    • Separation and quantitative determination of nanogram quantities of maltodextrins and isomaltodextrins by thin-layer chromatography
    • Robyt J.F., and Mukerjea R. Separation and quantitative determination of nanogram quantities of maltodextrins and isomaltodextrins by thin-layer chromatography. Carbohydrate Research 251 (1994) 187-202
    • (1994) Carbohydrate Research , vol.251 , pp. 187-202
    • Robyt, J.F.1    Mukerjea, R.2
  • 32
    • 0024430052 scopus 로고
    • Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes
    • Svensson B., Jespersen H., Sierks M.R., and MacGregor E.A. Sequence homology between putative raw-starch binding domains from different starch-degrading enzymes. Biochemical Journal 264 (1989) 309-311
    • (1989) Biochemical Journal , vol.264 , pp. 309-311
    • Svensson, B.1    Jespersen, H.2    Sierks, M.R.3    MacGregor, E.A.4
  • 33
    • 0028429952 scopus 로고
    • Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability
    • Svensson B. Protein engineering in the α-amylase family: catalytic mechanism, substrate specificity, and stability. Plant Molecular Biology 25 (1994) 141-157
    • (1994) Plant Molecular Biology , vol.25 , pp. 141-157
    • Svensson, B.1
  • 34
    • 0034302052 scopus 로고    scopus 로고
    • Acceptor specificity of 4-α-glucanotransferase from Pyrococcus kodakaraensis KOD1, and synthesis of cycloamylose
    • Tachibana Y., Takaha T., Fujiwara S., Takagi M., and Imanaka T. Acceptor specificity of 4-α-glucanotransferase from Pyrococcus kodakaraensis KOD1, and synthesis of cycloamylose. Journal of Bioscience and Bioengineering 90 (2000) 406-409
    • (2000) Journal of Bioscience and Bioengineering , vol.90 , pp. 406-409
    • Tachibana, Y.1    Takaha, T.2    Fujiwara, S.3    Takagi, M.4    Imanaka, T.5
  • 35
    • 0032810126 scopus 로고    scopus 로고
    • The functions of 4-alpha-glucanotransferases and their use for the production of cyclic glucans
    • Takaha T., and Smith S.M. The functions of 4-alpha-glucanotransferases and their use for the production of cyclic glucans. Biotechnology and Genetic Engineering Reviews 16 (1999) 257-280
    • (1999) Biotechnology and Genetic Engineering Reviews , vol.16 , pp. 257-280
    • Takaha, T.1    Smith, S.M.2
  • 36
    • 0027458378 scopus 로고
    • Disproportionating enzyme (4-α-glucanotransferase; E.C 2.4.1.25) of potato; purification, molecular cloning, and potential role in starch metabolism
    • Takaha T., Yanase M., Takata H., Okada S., and Smith S.M. Disproportionating enzyme (4-α-glucanotransferase; E.C 2.4.1.25) of potato; purification, molecular cloning, and potential role in starch metabolism. Journal of Biological Chemistry 268 (1993) 1391-1396
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 1391-1396
    • Takaha, T.1    Yanase, M.2    Takata, H.3    Okada, S.4    Smith, S.M.5
  • 37
    • 0030062091 scopus 로고    scopus 로고
    • Potato d-enzyme catalyzes the cyclization of amylose to produce cycloamylose, a novel cyclic glucan
    • Takaha T., Yanase M., Takata H., Okada S., and Smith S.M. Potato d-enzyme catalyzes the cyclization of amylose to produce cycloamylose, a novel cyclic glucan. Journal of Biological Chemistry 271 (1996) 2902-2908
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 2902-2908
    • Takaha, T.1    Yanase, M.2    Takata, H.3    Okada, S.4    Smith, S.M.5
  • 39
    • 0032985721 scopus 로고    scopus 로고
    • Thermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: production of cycloamylose
    • Terada Y., Fujii K., Takaha T., and Okada S. Thermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: production of cycloamylose. Applied and Environmental Microbiology 65 (1999) 910-915
    • (1999) Applied and Environmental Microbiology , vol.65 , pp. 910-915
    • Terada, Y.1    Fujii, K.2    Takaha, T.3    Okada, S.4
  • 40
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability source
    • Vieille C., and Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability source. Microbiology and Molecular Biology Reviews 65 (2001) 1-43
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.