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Volumn 44, Issue 27, 2005, Pages 9456-9461

Kinetic studies of site-directed mutational isomalto-dextranase-catalyzed hydrolytic reactions on a 27 MHz quartz-crystal microbalance

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTALS; ENZYMES; HYDROLYSIS; MUTAGENESIS; QUARTZ;

EID: 21844462328     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050079q     Document Type: Article
Times cited : (23)

References (37)
  • 1
    • 0003518480 scopus 로고
    • John Wiley & Sons, New York
    • Segel, H. (1975) Enzyme Kinetics, John Wiley & Sons, New York.
    • (1975) Enzyme Kinetics
    • Segel, H.1
  • 2
    • 0004197262 scopus 로고
    • CRC Press, Boca Raton, FL
    • Kuby, S. A., Ed. (1991) A Study of Enzymes. Vol. 1, CRC Press, Boca Raton, FL.
    • (1991) A Study of Enzymes , vol.1
    • Kuby, S.A.1
  • 3
    • 0001686879 scopus 로고
    • Determination of neuraminic (sialic) acid, glucose and fructose in spinal fluid
    • Papadopoulos, N. M., and Hess, W. C. (1960) Determination of Neuraminic (Sialic) Acid, Glucose and Fructose in Spinal Fluid, Arch. Biochem. Biophys. 88, 167-171.
    • (1960) Arch. Biochem. Biophys. , vol.88 , pp. 167-171
    • Papadopoulos, N.M.1    Hess, W.C.2
  • 4
    • 0025766291 scopus 로고
    • Miniaturization of three carbohydrate analyses using a microsample plate reader
    • Fox, J. D., and Robyt, J. F. (1991) Miniaturization of Three Carbohydrate Analyses Using a Microsample Plate Reader, Anal. Biochem. 195, 93-96.
    • (1991) Anal. Biochem. , vol.195 , pp. 93-96
    • Fox, J.D.1    Robyt, J.F.2
  • 5
    • 33750423631 scopus 로고
    • Note on sugar determination
    • Somogyi, M. (1952) Note on Sugar Determination, J. Biol. Chem. 195, 375-380.
    • (1952) J. Biol. Chem. , vol.195 , pp. 375-380
    • Somogyi, M.1
  • 6
    • 0000674033 scopus 로고
    • A photometric adaptation of the somogyi method for the determination of glucose
    • Nelson, N. (1944) A Photometric Adaptation of the Somogyi Method for the Determination of Glucose, J. Biol. Chem. 153, 375-380.
    • (1944) J. Biol. Chem. , vol.153 , pp. 375-380
    • Nelson, N.1
  • 7
    • 0026767570 scopus 로고
    • Stopped-flow fluorescence and steady-state kinetic studies of ligand-binding reactions of glucoamylase from Aspergillus niger
    • Olsen, K., Svensson, B., and Christensen, U. (1992) Stopped-Flow Fluorescence and Steady-State Kinetic Studies of Ligand-Binding Reactions of Glucoamylase from Aspergillus niger, Eur. J. Biochem. 209, 777-784.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 777-784
    • Olsen, K.1    Svensson, B.2    Christensen, U.3
  • 8
    • 0015986805 scopus 로고
    • A bacterial dextranase releasing only isomaltose from dextrans
    • Sawai, T., Toriyama, K., and Yano, K. (1974) A Bacterial Dextranase Releasing Only Isomaltose from Dextrans, J. Biochem. 75, 105-112.
    • (1974) J. Biochem. , vol.75 , pp. 105-112
    • Sawai, T.1    Toriyama, K.2    Yano, K.3
  • 9
    • 85004246984 scopus 로고
    • An isomalto-dextranase accompanied by isopullulanase activity from Arthrobacter globiformis T6
    • Okada, G., Takayanagi, T., Miyahara, S., and Sawai, T. (1988) An Isomalto-Dextranase Accompanied by Isopullulanase Activity from Arthrobacter globiformis T6, Agric. Biol. Chem. 52, 829-836.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 829-836
    • Okada, G.1    Takayanagi, T.2    Miyahara, S.3    Sawai, T.4
  • 10
    • 0004714822 scopus 로고
    • Purification and some properties of the isomaltodextranase of actinomadura strain R10 and comparison with that of Arthrobacter globiformis T6
    • Sawai, T., Ohara, S., Ichimi, Y., Okaji, S., Hisada, K., and Fukaya, N. (1981) Purification and Some Properties of the Isomaltodextranase of Actinomadura Strain R10 and Comparison with that of Arthrobacter globiformis T6, Carbohydr. Res. 89, 289-299.
    • (1981) Carbohydr. Res. , vol.89 , pp. 289-299
    • Sawai, T.1    Ohara, S.2    Ichimi, Y.3    Okaji, S.4    Hisada, K.5    Fukaya, N.6
  • 11
    • 0027984019 scopus 로고
    • Molecular cloning and expression of an isomalto-dextranase gene from Arthrobacter globiformis T6
    • Iwai, A., Ito, H., Mizuno, T., Mori, H., Matsui, H., Honma, M., Okada, G., and Chiba, S. (1994) Molecular Cloning and Expression of an Isomalto-Dextranase Gene from Arthrobacter globiformis T6, J. Bacteriol. 176, 7730-7734.
    • (1994) J. Bacteriol. , vol.176 , pp. 7730-7734
    • Iwai, A.1    Ito, H.2    Mizuno, T.3    Mori, H.4    Matsui, H.5    Honma, M.6    Okada, G.7    Chiba, S.8
  • 12
    • 0037827688 scopus 로고    scopus 로고
    • Crystal structure of rice α-galactosidase complexed with D-galactose
    • Fujimoto, Z., Kaneko, S., Momma, M., Kobayashi, H., and Mizuno, H. (2003) Crystal Structure of Rice α-Galactosidase Complexed with D-Galactose, J. Biol. Chem. 278, 20313-20318.
    • (2003) J. Biol. Chem. , vol.278 , pp. 20313-20318
    • Fujimoto, Z.1    Kaneko, S.2    Momma, M.3    Kobayashi, H.4    Mizuno, H.5
  • 13
    • 0036124422 scopus 로고    scopus 로고
    • The 1.9 Å structure of α-n-acetylgalactosaminidase: Molecular basis of glycosidase deficiency diseases
    • Garman, S. C., Hannick, L., Zhu, A., and Garboczi, D. N. (2002) The 1.9 Å Structure of α-n-Acetylgalactosaminidase: Molecular Basis of Glycosidase Deficiency Diseases, Structure 10, 425-434.
    • (2002) Structure , vol.10 , pp. 425-434
    • Garman, S.C.1    Hannick, L.2    Zhu, A.3    Garboczi, D.N.4
  • 14
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. (1991) A Classification of Glycosyl Hydrolases based on Amino Acid Sequence Similarities, Biochem. J. 280, 309-316.
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 15
    • 0029392961 scopus 로고
    • Families, superfamilies and subfamilies of glycosyl hydrolases
    • Henrissat, B., and Romeu, A. (1995) Families, Superfamilies and Subfamilies of Glycosyl Hydrolases, Biochem. J. 311, 350-351.
    • (1995) Biochem. J. , vol.311 , pp. 350-351
    • Henrissat, B.1    Romeu, A.2
  • 17
    • 1442299241 scopus 로고    scopus 로고
    • The molecular defect leading to fabry disease: Structure of human α-galactosidase
    • Garman, S. C., and Garboczi, D. N. (2004) The Molecular Defect Leading to Fabry Disease: Structure of Human α-Galactosidase, J. Mol. Biol. 19, 319-335.
    • (2004) J. Mol. Biol. , vol.19 , pp. 319-335
    • Garman, S.C.1    Garboczi, D.N.2
  • 18
    • 1542315193 scopus 로고    scopus 로고
    • Direct monitoring of enzymatic glucan hydrolyses on a 27-MHz quartz-crystal microbalance
    • (a) Nishino, H., Nihira, T., Mori, T., and Okahata, Y. (2004) Direct Monitoring of Enzymatic Glucan Hydrolyses on a 27-MHz Quartz-Crystal Microbalance, J. Am. Chem. Soc. 126, 2264-2265;
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2264-2265
    • Nishino, H.1    Nihira, T.2    Mori, T.3    Okahata, Y.4
  • 19
    • 8844239893 scopus 로고    scopus 로고
    • Kinetic studies of amylopectin cleavage reactions catalyzed by phosphorylase b using a 27 MHz quartz crystal microbalance
    • (b) Nishino, H., Murakawa, A., Mori, T., and Okahata, Y. (2004) Kinetic Studies of Amylopectin Cleavage Reactions Catalyzed by Phosphorylase b using a 27 MHz Quartz Crystal Microbalance, J. Am. Chem. Soc. 726, 14752-14757.
    • (2004) J. Am. Chem. Soc. , vol.726 , pp. 14752-14757
    • Nishino, H.1    Murakawa, A.2    Mori, T.3    Okahata, Y.4
  • 20
    • 84951279351 scopus 로고
    • Verwendung von schwingquarzen zur wagung dunner schichten und zur microwagang
    • Sauerbrey, G. (1959) Verwendung von Schwingquarzen zur Wagung dunner Schichten und zur Microwagang, Z. Phys. 155, 206-222.
    • (1959) Z. Phys. , vol.155 , pp. 206-222
    • Sauerbrey, G.1
  • 21
    • 25444471937 scopus 로고
    • Hybridization of nucleic acids immobilized on a quartz-crystal microbalance
    • (a) Okahata, Y., Matsunobu, Y., Ijiro, K., Mukai, M., Murakami, A., and Makino, K. (1992) Hybridization of Nucleic Acids Immobilized on a Quartz-Crystal Microbalance, J. Am. Chem. Soc. 114, 8299-8300;
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 8299-8300
    • Okahata, Y.1    Matsunobu, Y.2    Ijiro, K.3    Mukai, M.4    Murakami, A.5    Makino, K.6
  • 22
    • 1542606746 scopus 로고    scopus 로고
    • Kinetic measurements of DNA hybridization on an oligonucleotide- immobilized 27 MHz quartz-crystal microbalance
    • (b) Okahata, Y., Kawase, M., Niikura, K., Ohtake, F., Furusawa, H., and Ebara, Y. (1998) Kinetic Measurements of DNA Hybridization on an Oligonucleotide-Immobilized 27 MHz Quartz-Crystal Microbalance, Anal. Chem. 70, 1288-1296.
    • (1998) Anal. Chem. , vol.70 , pp. 1288-1296
    • Okahata, Y.1    Kawase, M.2    Niikura, K.3    Ohtake, F.4    Furusawa, H.5    Ebara, Y.6
  • 23
    • 0032554641 scopus 로고    scopus 로고
    • Kinetic studies of sequence-specific binding of GCN4-bZIP peptides to DNA stands immobilized on a 27 MHz quartz-crystal microbalance
    • (a) Okahata, Y., Niikura, K., Sugiura, Y., Sawada, M., and Morii, T. (1998) Kinetic Studies of Sequence-Specific Binding of GCN4-bZIP Peptides to DNA Stands immobilized on a 27 MHz Quartz-Crystal Microbalance, Biochemistry 37, 5666-5672;
    • (1998) Biochemistry , vol.37 , pp. 5666-5672
    • Okahata, Y.1    Niikura, K.2    Sugiura, Y.3    Sawada, M.4    Morii, T.5
  • 24
    • 0035957288 scopus 로고    scopus 로고
    • Design and characterization of asparagine- and lysine-containing alanine-based helical peptides that bind selectively to A-T base-pairs of oligonucleotides immobilized on a 27 MHz quartz crystal microbalance
    • (b) Matsuno, H., Niikura, K., and Okahata, Y. (2001) Design and Characterization of Asparagine- and Lysine-Containing Alanine-Based Helical Peptides That Bind Selectively to A-T Base-Pairs of Oligonucleotides Immobilized on a 27 MHz Quartz Crystal Microbalance, Biochemistry 40, 3615-3622;
    • (2001) Biochemistry , vol.40 , pp. 3615-3622
    • Matsuno, H.1    Niikura, K.2    Okahata, Y.3
  • 25
    • 0037123408 scopus 로고    scopus 로고
    • Binding kinetics of the toroidal-shaped PCNA to DNA strands on a 27 MHz quartz-crystal microbalance
    • (c) Furusawa, H., Kitamura, Y., Hagiwara, N., Tsurimoto, T., and Okahata, Y. (2002) Binding Kinetics of the Toroidal-Shaped PCNA to DNA Strands on a 27 MHz Quartz-Crystal Microbalance, ChemPhysChem., 446-448.
    • (2002) ChemPhysChem , pp. 446-448
    • Furusawa, H.1    Kitamura, Y.2    Hagiwara, N.3    Tsurimoto, T.4    Okahata, Y.5
  • 26
    • 0028592578 scopus 로고
    • A kinetic study of concanavalin A binding to glycolipid monolayers by using a quartz-crystal microbalance
    • (a) Ebara, Y., and Okahata, Y. (1994) A Kinetic Study of Concanavalin A Binding to Glycolipid Monolayers by Using a Quartz-Crystal Microbalance, J. Am. Chem. Soc. 116, 11209-11212;
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11209-11212
    • Ebara, Y.1    Okahata, Y.2
  • 27
    • 0033877424 scopus 로고    scopus 로고
    • DNA hybridization at the air-water interface
    • (b) Ebara, Y., Mizutani, K., and Okahata, Y. (2000) DNA Hybridization at the Air-Water Interface, Langmuir 16, 2416-2418.
    • (2000) Langmuir , vol.16 , pp. 2416-2418
    • Ebara, Y.1    Mizutani, K.2    Okahata, Y.3
  • 28
    • 0032569186 scopus 로고    scopus 로고
    • Direct monitoring of DNA polymerase reactions on a quartz-crystal microbalance
    • (a) Niikura, K., Matsuno, H., and Okahata, Y. (1998) Direct Monitoring of DNA Polymerase Reactions on a Quartz-Crystal Microbalance, J. Am. Chem. Soc. 120, 8537-8538;
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8537-8538
    • Niikura, K.1    Matsuno, H.2    Okahata, Y.3
  • 29
    • 0035800523 scopus 로고    scopus 로고
    • Direct monitoring and kinetic studies of DNA polymerase reactions on a DNA-immobilized quartz-crystal microbalance
    • (b) Matsuno, H., Niikura, K., and Okahata, Y. (2001) Direct Monitoring and Kinetic Studies of DNA Polymerase Reactions on a DNA-immobilized Quartz-Crystal Microbalance, Chem. Eur. J. 7, 3305-3312;
    • (2001) Chem. Eur. J. , vol.7 , pp. 3305-3312
    • Matsuno, H.1    Niikura, K.2    Okahata, Y.3
  • 30
    • 14044256601 scopus 로고    scopus 로고
    • Kinetic studies of DNA cleavage reactions catalyzed by an ATP-dependent deoxyribonuclease on a 27-MHz quartz-crystal Microbalance
    • in press
    • (c) Matsuno, H., Furusawa, H., and Okahata, Y. (2005) Kinetic Studies of DNA Cleavage Reactions Catalyzed by an ATP-Dependent Deoxyribonuclease on a 27-MHz Quartz-Crystal Microbalance, Biochemistry (in press).
    • (2005) Biochemistry
    • Matsuno, H.1    Furusawa, H.2    Okahata, Y.3
  • 32
    • 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
  • 33
    • 0030213338 scopus 로고    scopus 로고
    • Bifunctional labeling reagent for oligosaccharides to incorporate both chromophore and biotin groups
    • Shinohara, Y., Sota, H., Gotoh, M., Hasebe, M., Tosu, M., Nakao, I., Hasegawa, Y., and Shiga, M. (1996) Bifunctional Labeling Reagent for Oligosaccharides to Incorporate both Chromophore and Biotin Groups, Anal. Chem. 68, 2573-2579.
    • (1996) Anal. Chem. , vol.68 , pp. 2573-2579
    • Shinohara, Y.1    Sota, H.2    Gotoh, M.3    Hasebe, M.4    Tosu, M.5    Nakao, I.6    Hasegawa, Y.7    Shiga, M.8
  • 34
    • 0034663962 scopus 로고    scopus 로고
    • Identification of Asp-130 as the catalytic nucleophile in the main α-galactosidase from Phanerochaete chrysosporium, a family 27 glycosyl hydrolase
    • Hart, D. O., He, S., Chany, C. J., II, Withers, S. G., Sims, P. F. G., Sinnott, M. L., and Brumer, H., III (2000) Identification of Asp-130 as the Catalytic Nucleophile in the Main α-Galactosidase from Phanerochaete chrysosporium, a Family 27 Glycosyl Hydrolase, Biochemistry 39, 9826-9836.
    • (2000) Biochemistry , vol.39 , pp. 9826-9836
    • Hart, D.O.1    He, S.2    Chany II, C.J.3    Withers, S.G.4    Sims, P.F.G.5    Sinnott, M.L.6    Brumer III, H.7
  • 35
    • 0032717219 scopus 로고    scopus 로고
    • Roles of catalytic residues in α-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase
    • Hasegawa, K., Kubota, M., and Matsuura, Y. (1999) Roles of Catalytic Residues in α-Amylases as Evidenced by the Structures of the Product-complexed Mutants of a Maltotetraose-forming Amylase, Protein Eng. 12, 819-824.
    • (1999) Protein Eng. , vol.12 , pp. 819-824
    • Hasegawa, K.1    Kubota, M.2    Matsuura, Y.3
  • 37
    • 3343023811 scopus 로고    scopus 로고
    • Site-directed mutagenesis establishes aspartic acids-227 and -342 as essential for enzyme activity in an isomalto-dextranase from Arthrobacter globiformis
    • Tochihara, T., Sasaki, K., Araki, O., Morimoto, N., Watanabe, K., Hatada, Y., Ito, S., Ito, H., and Matsui, H. (2004) Site-Directed Mutagenesis Establishes Aspartic Acids-227 and -342 as Essential for Enzyme Activity in an Isomalto-dextranase from Arthrobacter globiformis, Biotechnol. Lett. 26, 659-664.
    • (2004) Biotechnol. Lett. , vol.26 , pp. 659-664
    • Tochihara, T.1    Sasaki, K.2    Araki, O.3    Morimoto, N.4    Watanabe, K.5    Hatada, Y.6    Ito, S.7    Ito, H.8    Matsui, H.9


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