메뉴 건너뛰기




Volumn 43, Issue 44, 2004, Pages 14047-14056

Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; BIOCHEMISTRY; CATALYSTS; CRYSTAL STRUCTURE; ENZYME KINETICS; STARCH;

EID: 8344244671     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048489m     Document Type: Article
Times cited : (43)

References (32)
  • 1
    • 0001283165 scopus 로고
    • Action patterns of various exo-amylases and the anomeric configurations of their products
    • Nakakuki, T., Azuma, K., and Kainuma, K. (1984) Action patterns of various exo-amylases and the anomeric configurations of their products, Carbohydr. Res. 128, 297-310.
    • (1984) Carbohydr. Res. , vol.128 , pp. 297-310
    • Nakakuki, T.1    Azuma, K.2    Kainuma, K.3
  • 2
    • 0030823127 scopus 로고    scopus 로고
    • Crystal structures of a mutant maltotetraoseforming exo-amylase cocrystallized with maltopentaose
    • Yoshioka, Y., Hasegawa, K., Matsuura, Y., Katsube, Y., and Kubota, M. (1997) Crystal structures of a mutant maltotetraoseforming exo-amylase cocrystallized with maltopentaose, J. Mol. Biol. 271, 619-628.
    • (1997) J. Mol. Biol. , vol.271 , pp. 619-628
    • Yoshioka, Y.1    Hasegawa, K.2    Matsuura, Y.3    Katsube, Y.4    Kubota, M.5
  • 3
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • Henrissat, B., and Davies, G. (1997) Structural and sequence-based classification of glycoside hydrolases, Curr. Opin. Struct. Biol. 7, 637-644.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.2
  • 4
    • 0024299217 scopus 로고
    • Nucleotide sequence of the maltohexaose-producing amylase gene from an alakalophilic Bacillus sp.#707 and structural similarity to liquefying type α-amylases
    • Tsukamoto, A., Kimura, K., Ishii, Y., Takano, T., and Yamane, K. (1988) Nucleotide sequence of the maltohexaose-producing amylase gene from an alakalophilic Bacillus sp.#707 and structural similarity to liquefying type α-amylases, Biochem. Biophys. Res. Commun. 151, 25-31.
    • (1988) Biochem. Biophys. Res. Commun. , vol.151 , pp. 25-31
    • Tsukamoto, A.1    Kimura, K.2    Ishii, Y.3    Takano, T.4    Yamane, K.5
  • 5
    • 8344222941 scopus 로고
    • Plant α-amylases
    • Nakamura, M., Ed. Gakkai-Shuppan Center, Tokyo (in Japanese)
    • Taniguchi, H. (1986) Plant α-amylases, in Amylase (Nakamura, M., Ed.) pp 168-170, Gakkai-Shuppan Center, Tokyo (in Japanese).
    • (1986) Amylase , pp. 168-170
    • Taniguchi, H.1
  • 6
    • 0002309322 scopus 로고
    • The action of some α-amylases on amylose
    • Bird, R., and Hopkins, R. H. (1953) The action of some α-amylases on amylose, Biochem. J. 56, 86-99.
    • (1953) Biochem. J. , vol.56 , pp. 86-99
    • Bird, R.1    Hopkins, R.H.2
  • 8
    • 0028229326 scopus 로고
    • Crystal and molecular structure of barley α-amylase
    • Kadziola, A., Abe, J., Svensson, B., and Haser, R. (1994) Crystal and molecular structure of barley α-amylase, J. Mol. Biol. 239, 104-21.
    • (1994) J. Mol. Biol. , vol.239 , pp. 104-121
    • Kadziola, A.1    Abe, J.2    Svensson, B.3    Haser, R.4
  • 9
    • 0345580183 scopus 로고    scopus 로고
    • Amylose chain behavior in an interacting context. III. Complete occupancy of the AMY2 barley α-amylase cleft and comparison with biochemical data
    • Andre, G., Buleon, A., Haser, R., and Tran, V. (1999) Amylose chain behavior in an interacting context. III. Complete occupancy of the AMY2 barley α-amylase cleft and comparison with biochemical data, Biopolymers 50, 751-62.
    • (1999) Biopolymers , vol.50 , pp. 751-762
    • Andre, G.1    Buleon, A.2    Haser, R.3    Tran, V.4
  • 10
    • 0023810007 scopus 로고
    • Cloning of a gene for maltohexaose producing amylase of an alkalophilic Bacillus and hyper-production of the enzyme in Bacillus subtilis
    • Kimura, K., Tsukamoto, A., Ishii, Y., Takano, T., and Yamane, K. (1988) Cloning of a gene for maltohexaose producing amylase of an alkalophilic Bacillus and hyper-production of the enzyme in Bacillus subtilis, Appl. Microbiol. Biotechnol. 27, 372-7.
    • (1988) Appl. Microbiol. Biotechnol. , vol.27 , pp. 372-377
    • Kimura, K.1    Tsukamoto, A.2    Ishii, Y.3    Takano, T.4    Yamane, K.5
  • 11
    • 0027956666 scopus 로고
    • Four aromatic residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: Effects of replacements on substrate binding and cyclization characteristics
    • Nakamura, A., Haga, K., and Yamane, K. (1994) Four aromatic residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of replacements on substrate binding and cyclization characteristics, Biochemistry 33, 9929-36.
    • (1994) Biochemistry , vol.33 , pp. 9929-9936
    • Nakamura, A.1    Haga, K.2    Yamane, K.3
  • 12
    • 0031059866 scopus 로고    scopus 로고
    • (Carter, Jr., C. W., and Sweet, R. M., Eds.) Methods in Enzymology, 276, Macromolecular Crystallography, Academic Press, New York
    • Otwinowski, Z., and Minor, W. (1997) in Processing of X-ray Diffraction Data Collected in Oscillation Mode (Carter, Jr., C. W., and Sweet, R. M., Eds.) Methods in Enzymology, 276, Macromolecular Crystallography, part A, pp 307-26, Academic Press, New York.
    • (1997) Processing of X-ray Diffraction Data Collected in Oscillation Mode , Issue.PART A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 14
    • 0037837789 scopus 로고    scopus 로고
    • Kinetic stabilization of Bacillus licheniformis α-amylase through introduction of hydrophobic residues at the surface
    • Machius, M., Declerck, N., Huber, R., and Wiegand, G. (2003) Kinetic stabilization of Bacillus licheniformis α-amylase through introduction of hydrophobic residues at the surface, J. Biol. Chem. 278, 11546-53.
    • (2003) J. Biol. Chem. , vol.278 , pp. 11546-11553
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 15
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, A. R., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, A.R.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 16
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution
    • Gilson, M. K., Sharp, K. A., and Honig, B. H. (1987) Calculating the electrostatic potential of molecules in solution, J. Comput. Chem. 9, 327-35.
    • (1987) J. Comput. Chem. , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.H.3
  • 17
    • 33751385054 scopus 로고
    • Macroscopic models of aqueous solutions: Biological and chemical applications
    • Honig, B., Sharp, K., and Yang, A. (1993) Macroscopic models of aqueous solutions: biological and chemical applications, J. Phys. Chem. 97, 1101-9.
    • (1993) J. Phys. Chem. , vol.97 , pp. 1101-1109
    • Honig, B.1    Sharp, K.2    Yang, A.3
  • 18
    • 0015606538 scopus 로고
    • A thermophilic extracellular α-amylase from Bacillus licheniformis
    • Narimasa, S. (1973) A thermophilic extracellular α-amylase from Bacillus licheniformis, Arch. Biochem. Biophys. 155, 290-8.
    • (1973) Arch. Biochem. Biophys. , vol.155 , pp. 290-298
    • Narimasa, S.1
  • 19
    • 0014669304 scopus 로고
    • The extracellular α-amylase of Bacillus stearothermophilus
    • Pfueller, S. L., and Elliott, W. H. (1969) The extracellular α-amylase of Bacillus stearothermophilus, J. Biol. Chem. 244, 48-54.
    • (1969) J. Biol. Chem. , vol.244 , pp. 48-54
    • Pfueller, S.L.1    Elliott, W.H.2
  • 20
    • 0021395910 scopus 로고
    • Structure and possible catalytic residues of Taka-amylase A
    • Matsuura, Y., Kusunoki, M., Harada, W., and Kakudo, M. (1984) Structure and possible catalytic residues of Taka-amylase A, J. Biochem. (Tokyo) 95, 697-702.
    • (1984) J. Biochem. (Tokyo) , vol.95 , pp. 697-702
    • Matsuura, Y.1    Kusunoki, M.2    Harada, W.3    Kakudo, M.4
  • 21
    • 13144305048 scopus 로고    scopus 로고
    • Activation of Bacillus licheniformis α-amylase through disorder→ order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad
    • Machius, M., Declerck, N., Huber, R., and Wiegand, G. (1998) Activation of Bacillus licheniformis α-amylase through disorder→ order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad, Structure 6, 281-92.
    • (1998) Structure , vol.6 , pp. 281-292
    • Machius, M.1    Declerck, N.2    Huber, R.3    Wiegand, G.4
  • 22
    • 0035050561 scopus 로고    scopus 로고
    • Crystal structure of Bacillus stearothermophilus α-amylase: Possible factors determining the thermostability
    • Suvd, D., Fujimoto, Z., Takase, K., Matsumura, M., and Mizuno, H. (2001) Crystal structure of Bacillus stearothermophilus α-amylase: possible factors determining the thermostability, J. Biochem. (Tokyo) 129, 461-8.
    • (2001) J. Biochem. (Tokyo) , vol.129 , pp. 461-468
    • Suvd, D.1    Fujimoto, Z.2    Takase, K.3    Matsumura, M.4    Mizuno, H.5
  • 23
    • 0032571332 scopus 로고    scopus 로고
    • Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose
    • Fujimoto, Z., Takase, K., Doui, N., Momma, M., Matsumoto, T., and Mizuno, H. (1998) Crystal structure of a catalytic-site mutant α-amylase from Bacillus subtilis complexed with maltopentaose, J. Mol. Biol. 277, 393-407.
    • (1998) J. Mol. Biol. , vol.277 , pp. 393-407
    • Fujimoto, Z.1    Takase, K.2    Doui, N.3    Momma, M.4    Matsumoto, T.5    Mizuno, H.6
  • 24
    • 0033614827 scopus 로고    scopus 로고
    • X-ray structure of novamyl, the five-domain "maltogenic" α-amylase from Bacillus Stearothermophilus: Maltose and acarbose complexes at 1.7Å resolution
    • Dauter, Z., Dauter, M., Brzozowski, A. M., Christensen, S., Borchert, T. V., Beier, L., Wilson, K. S., and Davies, G. J. (1999) X-ray structure of novamyl, the five-domain "maltogenic" α-amylase from Bacillus Stearothermophilus: maltose and acarbose complexes at 1.7Å resolution, Biochemistry 38, 8385-92.
    • (1999) Biochemistry , vol.38 , pp. 8385-8392
    • Dauter, Z.1    Dauter, M.2    Brzozowski, A.M.3    Christensen, S.4    Borchert, T.V.5    Beier, L.6    Wilson, K.S.7    Davies, G.J.8
  • 25
    • 0030513264 scopus 로고    scopus 로고
    • X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp.1011. Comparison of two independent molecules at 1.8Å resolution
    • Harata, K., Haga, K., Nakamura, A., Aoyagi, M., and Yamane, K. (1996) X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp.1011. Comparison of two independent molecules at 1.8Å resolution, Acta Crystallogr. D52, 1136-45.
    • (1996) Acta Crystallogr. , vol.D52 , pp. 1136-1145
    • Harata, K.1    Haga, K.2    Nakamura, A.3    Aoyagi, M.4    Yamane, K.5
  • 26
    • 0032497955 scopus 로고    scopus 로고
    • Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase
    • Mosi, R., Sham, H., Uitdehaag, J. C. M., Ruiterkamp, R., Dijkstra, B. W., and Withers, S. G. (1998) Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase, Biochemistry 37, 17192-8.
    • (1998) Biochemistry , vol.37 , pp. 17192-17198
    • Mosi, R.1    Sham, H.2    Uitdehaag, J.C.M.3    Ruiterkamp, R.4    Dijkstra, B.W.5    Withers, S.G.6
  • 27
    • 1342283143 scopus 로고    scopus 로고
    • Effects of essential carbohydrate/aromatic stacking interaction with Tyr100 and Phe259 on substrate binding of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp. 1011
    • Haga, K., Kanai, R., Sakamoto, O., Aoyagi, M., Harata, K., and Yamane K. (2003) Effects of essential carbohydrate/aromatic stacking interaction with Tyr100 and Phe259 on substrate binding of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp. 1011, J. Biochem. (Tokyo) 134, 881-91.
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 881-891
    • Haga, K.1    Kanai, R.2    Sakamoto, O.3    Aoyagi, M.4    Harata, K.5    Yamane, K.6
  • 29
    • 0028198814 scopus 로고
    • The active center of a mammalian a-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-Å resolution
    • Qian, M., Haser, R., Buisson, G., Duee, E., and Payan, F. (1994) The active center of a mammalian a-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-Å resolution, Biochemistry 33, 6284-94.
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Haser, R.2    Buisson, G.3    Duee, E.4    Payan, F.5
  • 30
    • 0037042199 scopus 로고    scopus 로고
    • Action pattern and subsite mapping of Bacillus licheniformis α-amylase (BLA) with modified maltooligosaccharide substrates
    • Kandra, L., Gyemant, G., Remenyik, J., Hovanszki, G., and Liptak, A. (2002) Action pattern and subsite mapping of Bacillus licheniformis α-amylase (BLA) with modified maltooligosaccharide substrates, FEBS Lett. 518, 79-82.
    • (2002) FEBS Lett. , vol.518 , pp. 79-82
    • Kandra, L.1    Gyemant, G.2    Remenyik, J.3    Hovanszki, G.4    Liptak, A.5
  • 31
    • 0017896120 scopus 로고
    • Digestion of barley starch granules by the combined action of α- and β-amylases purified from barley and barley malt
    • Maeda, I., Kiribuchi, S., and Nakamura, M. (1978) Digestion of barley starch granules by the combined action of α- and β-amylases purified from barley and barley malt, Agric. Biol. Chem. 42, 259-67.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 259-267
    • Maeda, I.1    Kiribuchi, S.2    Nakamura, M.3
  • 32
    • 1642321719 scopus 로고    scopus 로고
    • Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley α-amylase 1
    • Bak-Jensen, K. S., Andre, G., Gottschalk, T. E., Paes, G., Tran, V., and Svensson, B. (2004) Tyrosine 105 and threonine 212 at outermost substrate binding subsites -6 and +4 control substrate specificity, oligosaccharide cleavage patterns, and multiple binding modes of barley α-amylase 1, J. Biol. Chem. 279, 10093-102.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10093-10102
    • Bak-Jensen, K.S.1    Andre, G.2    Gottschalk, T.E.3    Paes, G.4    Tran, V.5    Svensson, B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.