메뉴 건너뛰기




Volumn 238, Issue 2, 1996, Pages 561-569

Crystal structure of pig pancreatic α-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose

Author keywords

acarbose; carbohydrate; inhibitor; X ray structure; amylase

Indexed keywords

ACARBOSE; AMYLASE; AMYLASE INHIBITOR; ISOENZYME; PANCREAS ENZYME;

EID: 0029953633     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0561z.x     Document Type: Article
Times cited : (128)

References (33)
  • 1
    • 0026927353 scopus 로고
    • Solubility, phase transition, kinetic ripening and growth rates of porcine pancreatic α-amylase isoenzymes
    • Boistelle, R., Astier, J. P., Marchis-Mouren, G., Desseaux, V. & Haser, R. (1992) Solubility, phase transition, kinetic ripening and growth rates of porcine pancreatic α-amylase isoenzymes, Crystal Growth 123, 109-120.
    • (1992) Crystal Growth , vol.123 , pp. 109-120
    • Boistelle, R.1    Astier, J.P.2    Marchis-Mouren, G.3    Desseaux, V.4    Haser, R.5
  • 2
    • 0002874339 scopus 로고
    • Solution of the structure of Aspergillus niger acid α-amylase by combined molecular replacement and multiple isomorphous replacement methods
    • Brady, R. L., Brzozowski, A. M., Derewenda, Z. S., Dodson, E. J. & Dodson, G. G. (1991) Solution of the structure of Aspergillus niger acid α-amylase by combined molecular replacement and multiple isomorphous replacement methods, Acta Crystallogr. B47, 527-535.
    • (1991) Acta Crystallogr. , vol.B47 , pp. 527-535
    • Brady, R.L.1    Brzozowski, A.M.2    Derewenda, Z.S.3    Dodson, E.J.4    Dodson, G.G.5
  • 3
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A. T., Kuriyan, J. & Karplus, M. (1987) Crystallographic R factor refinement by molecular dynamics, Science 35, 458-460.
    • (1987) Science , vol.35 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 4
    • 0014969211 scopus 로고
    • Characterization of porcine pancreatic isoamylases: Separation and amino acid composition
    • Cozzone, P., Pasero, L. & Marchis-Mouren, G. (1970) Characterization of porcine pancreatic isoamylases: separation and amino acid composition, Biochim. Biophys. Acta 200, 590-593.
    • (1970) Biochim. Biophys. Acta , vol.200 , pp. 590-593
    • Cozzone, P.1    Pasero, L.2    Marchis-Mouren, G.3
  • 5
    • 0027255897 scopus 로고
    • Substrate recognition at the binding site in mammalian pancreatic α-amylases
    • Ishikawa, K., Matsui, I., Kobayashi, S., Nakatani, H. & Honda, K. (1993) Substrate recognition at the binding site in mammalian pancreatic α-amylases, Biochemistry 32, 6259-6265.
    • (1993) Biochemistry , vol.32 , pp. 6259-6265
    • Ishikawa, K.1    Matsui, I.2    Kobayashi, S.3    Nakatani, H.4    Honda, K.5
  • 7
    • 85027632383 scopus 로고
    • Automatic indexing of rotation diffraction patterns
    • Kabsch, W. (1988) Automatic indexing of rotation diffraction patterns, J. Appl. Crystallogr. 21, 67-71.
    • (1988) J. Appl. Crystallogr. , vol.21 , pp. 67-71
    • Kabsch, W.1
  • 8
    • 0028229326 scopus 로고
    • Crystal and molecular structure of barley α-amylase
    • Kadziola, A., Abe, J., Svensson, B. & Haser, R. (1994) Crystal and molecular structure of barley α-amylase, J. Mol. Biol. 239, 104-121.
    • (1994) J. Mol. Biol. , vol.239 , pp. 104-121
    • Kadziola, A.1    Abe, J.2    Svensson, B.3    Haser, R.4
  • 9
    • 0019890472 scopus 로고
    • Amino acid sequence of hog pancretic α-amylase isoenzyme I
    • Kluh, I. (1981) Amino acid sequence of hog pancretic α-amylase isoenzyme I, FEBS Lett. 136, 231-234.
    • (1981) FEBS Lett. , vol.136 , pp. 231-234
    • Kluh, I.1
  • 10
    • 0028359337 scopus 로고
    • Refined molecular structure of pig pancreatic α-amylase at 2.1 Å resolution
    • Larson, S. B., Greenwood, A., Cascio, D., Day, J. & McPherson, A. (1994) Refined molecular structure of pig pancreatic α-amylase at 2.1 Å resolution, J. Mol. Biol. 235, 1560-1584.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1560-1584
    • Larson, S.B.1    Greenwood, A.2    Cascio, D.3    Day, J.4    McPherson, A.5
  • 12
    • 0015975824 scopus 로고
    • The allosteric activation of mammalian α-amylase by chloride
    • Levitzki, A. & Steer, M. L. (1974) The allosteric activation of mammalian α-amylase by chloride, Eur. J. Biochem. 41, 171-180.
    • (1974) Eur. J. Biochem. , vol.41 , pp. 171-180
    • Levitzki, A.1    Steer, M.L.2
  • 13
    • 0001099937 scopus 로고
    • Traitement statistique des erreurs dans la détermination des structures cristallines
    • Luzzatti, P. V. (1952) Traitement statistique des erreurs dans la détermination des structures cristallines, Acta Crystallogr. 5, 802-810.
    • (1952) Acta Crystallogr. , vol.5 , pp. 802-810
    • Luzzatti, P.V.1
  • 14
    • 0028933531 scopus 로고
    • Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution
    • Machius, M., Wiegand, G. & Huber, R. (1995) Crystal structure of calcium-depleted Bacillus licheniformis α-amylase at 2.2 Å resolution, J. Mol. Biol. 246, 545-559.
    • (1995) J. Mol. Biol. , vol.246 , pp. 545-559
    • Machius, M.1    Wiegand, G.2    Huber, R.3
  • 16
    • 0344948480 scopus 로고
    • Hog pancreatic α-amylase peptides from tryptic digest of isoenzyme All
    • Meloun, B., Kluh, I. & Moravella, L. (1980) Hog pancreatic α-amylase peptides from tryptic digest of isoenzyme All, Collect. Czech. Chem. Commun. 45, 2572-2582.
    • (1980) Collect. Czech. Chem. Commun. , vol.45 , pp. 2572-2582
    • Meloun, B.1    Kluh, I.2    Moravella, L.3
  • 17
    • 0002351177 scopus 로고
    • AMoRe: A new package for molecular replacement
    • (Dodson, E. J., Grower, S. & Wolf, W., eds) Science and Engineering Reserach Council, London
    • Navaza, J. (1992) AMoRe: A new package for molecular replacement, in Proceedings of the CCP4 study weekend (Dodson, E. J., Grower, S. & Wolf, W., eds) pp. 87-91, Science and Engineering Reserach Council, London.
    • (1992) Proceedings of the CCP4 Study Weekend , pp. 87-91
    • Navaza, J.1
  • 18
  • 19
    • 49449124644 scopus 로고
    • Preliminary X-ray investigation on a new crystalline variety of porcine pancreatic α-amylase
    • Pierrot, M., Astier, J. P., Abadie, B. & Marchis-Mouren, G. (1977) Preliminary X-ray investigation on a new crystalline variety of porcine pancreatic α-amylase, FEBS Lett. 79, 105-108.
    • (1977) FEBS Lett. , vol.79 , pp. 105-108
    • Pierrot, M.1    Astier, J.P.2    Abadie, B.3    Marchis-Mouren, G.4
  • 20
    • 0021766528 scopus 로고
    • Subsite profile of the active center of porcine pancreatic α-amylase. Kinetic studies using maltooligosaccharides as substrates
    • Prodanov, E., Seigner, C. & Marchis-Mouren, G. (1984) Subsite profile of the active center of porcine pancreatic α-amylase. Kinetic studies using maltooligosaccharides as substrates, Biochem. Biophys. Res. Commun. 122, 75-81.
    • (1984) Biochem. Biophys. Res. Commun. , vol.122 , pp. 75-81
    • Prodanov, E.1    Seigner, C.2    Marchis-Mouren, G.3
  • 21
    • 0027296794 scopus 로고
    • Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution
    • Qian, M., Haser, H. & Payan, F. (1993) Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution, J. Mol. Biol. 231, 785-799.
    • (1993) J. Mol. Biol. , vol.231 , pp. 785-799
    • Qian, M.1    Haser, H.2    Payan, F.3
  • 22
    • 0028198814 scopus 로고
    • The active center of a mammalian α-amylase. Structure of the complex of a pancrearic α-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution
    • Qian, M., Buisson, G., Duée, E., Haser, H. & Payan, F. (1994) The active center of a mammalian α-amylase. Structure of the complex of a pancrearic α-amylase with a carbohydrate inhibitor refined to 2.2 Å resolution, Biochemistry 33, 6284-6294.
    • (1994) Biochemistry , vol.33 , pp. 6284-6294
    • Qian, M.1    Buisson, G.2    Duée, E.3    Haser, H.4    Payan, F.5
  • 23
    • 0028966756 scopus 로고
    • Carbohydrate binding sites in a pancreatic α-amylase - Substrate complex, derived from X-ray structure analysis at 2.1 Å resolution
    • Qian, M., Haser, H. & Payan, F. (1995) Carbohydrate binding sites in a pancreatic α-amylase - substrate complex, derived from X-ray structure analysis at 2.1 Å resolution, Protein Sci. 4, 747-755.
    • (1995) Protein Sci. , vol.4 , pp. 747-755
    • Qian, M.1    Haser, H.2    Payan, F.3
  • 24
    • 84911304823 scopus 로고
    • Protein-carbohydrate interactions: Basic molecular features
    • Quiocho, F. A. (1989) Protein-carbohydrate interactions: basic molecular features, Pure Appl. Chem. 61, 1293-1306.
    • (1989) Pure Appl. Chem. , vol.61 , pp. 1293-1306
    • Quiocho, F.A.1
  • 25
    • 0014939925 scopus 로고
    • The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme
    • Robyt, J. F. & French, D. (1970a) The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme, J. Biol. Chem. 245, 3917-3927.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3917-3927
    • Robyt, J.F.1    French, D.2
  • 26
    • 0014803288 scopus 로고
    • Multiple attack and polarity of action of porcine pancreatic α-amylase
    • Robyt, J. F. & French, D. (1970b) Multiple attack and polarity of action of porcine pancreatic α-amylase, Arch. Biochem. Biophys. 13, 622-670.
    • (1970) Arch. Biochem. Biophys. , vol.13 , pp. 622-670
    • Robyt, J.F.1    French, D.2
  • 29
    • 0015605979 scopus 로고
    • The metal specificity of mammalian α-amylases as revealed by enzyme activity and structural probes
    • Steer, M. & Levitzki, A. (1973) The metal specificity of mammalian α-amylases as revealed by enzyme activity and structural probes, FEBS Lett. 31, 89-92.
    • (1973) FEBS Lett. , vol.31 , pp. 89-92
    • Steer, M.1    Levitzki, A.2
  • 30
    • 0000843244 scopus 로고
    • Structure and molecular model refinement of A, oryzae α-amylase: An application of the simulated-annealing method
    • Swift, H. J., Brady, L., Derewenda, Z. S., Dodson, E. J., Dodson, G. G., Turkenburg, J. P. & Wilkinson, A. J. (1991) Structure and molecular model refinement of A, oryzae α-amylase: an application of the simulated-annealing method, Acta Crystallogr. B47, 535-544.
    • (1991) Acta Crystallogr. , vol.B47 , pp. 535-544
    • Swift, H.J.1    Brady, L.2    Derewenda, Z.S.3    Dodson, E.J.4    Dodson, G.G.5    Turkenburg, J.P.6    Wilkinson, A.J.7
  • 32
    • 0001244369 scopus 로고
    • The active site of porcine pancreatic α-amylase: Factor contributing to catalysis
    • Wakim, J., Robinson, M. & Thoma, J. A. (1969) The active site of porcine pancreatic α-amylase: factor contributing to catalysis, Carbohydr. Res. 10, 487-503.
    • (1969) Carbohydr. Res. , vol.10 , pp. 487-503
    • Wakim, J.1    Robinson, M.2    Thoma, J.A.3
  • 33
    • 0028962770 scopus 로고
    • The crystal structure of porcine pancreatic α-amylase in complex with the microbial inhibitor Tendamistat
    • Wiegand, G., Epp, O. & Huber, R. (1995) The crystal structure of porcine pancreatic α-amylase in complex with the microbial inhibitor Tendamistat, J. Mol. Biol. 247, 99-110.
    • (1995) J. Mol. Biol. , vol.247 , pp. 99-110
    • Wiegand, G.1    Epp, O.2    Huber, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.