메뉴 건너뛰기




Volumn 241, Issue 3, 1996, Pages 787-796

The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites

Author keywords

Acarbose; Amylose; Kinetics; Maltodextrin; Amylase

Indexed keywords

ACARBOSE; AMYLASE; ISOENZYME;

EID: 0029957475     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00787.x     Document Type: Article
Times cited : (56)

References (28)
  • 1
    • 0028920217 scopus 로고
    • Subsite mapping of porcine pancreatic α-amylase I and II using 4-nitrophenyl-α-maltooligosaccharides
    • Ajandouz, E. H. & Marchis-Mouren, G. (1995) Subsite mapping of porcine pancreatic α-amylase I and II using 4-nitrophenyl-α-maltooligosaccharides, Carbohydrate Res. 268, 267-277.
    • (1995) Carbohydrate Res. , vol.268 , pp. 267-277
    • Ajandouz, E.H.1    Marchis-Mouren, G.2
  • 3
    • 0029111443 scopus 로고
    • The structure of human pancreatic α-amylase at 1.8 Å resolution and comparisons with related enzymes
    • Brayer, G. D., Luo, Y. & Withers, S. G. (1995) The structure of human pancreatic α-amylase at 1.8 Å resolution and comparisons with related enzymes. Protein Science 4, 1730-1742.
    • (1995) Protein Science , vol.4 , pp. 1730-1742
    • Brayer, G.D.1    Luo, Y.2    Withers, S.G.3
  • 4
    • 0023661282 scopus 로고
    • Three-dimensional structure of porcine pancreatic α-amylase at 2.9 Å resolution. Role of calcium in structure and activity
    • Buisson, G., Duée, E., Haser, R. & Payan, F. (1987) Three-dimensional structure of porcine pancreatic α-amylase at 2.9 Å resolution. Role of calcium in structure and activity, EMBO J. 6, 3909-3916.
    • (1987) EMBO J. , vol.6 , pp. 3909-3916
    • Buisson, G.1    Duée, E.2    Haser, R.3    Payan, F.4
  • 5
    • 50549188738 scopus 로고
    • The kinetics of enzyme catalyzed reactions with two or more substrates or products
    • Cleland, W. W (1963) The kinetics of enzyme catalyzed reactions with two or more substrates or products, Biochim. Biophys. Acta 67, 173-196.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 173-196
    • Cleland, W.W.1
  • 6
    • 10344224709 scopus 로고
    • Inhibition and activation
    • Butterworths Edit. Camelot press, London
    • Cornish-Bowden, A. (1979) Inhibition and activation, in Fundamentals of enzyme kinetics, pp. 76-77, Butterworths Edit. Camelot press, London.
    • (1979) Fundamentals of Enzyme Kinetics , pp. 76-77
    • Cornish-Bowden, A.1
  • 7
    • 0025997060 scopus 로고
    • Effect of limited proteolysis in the 8th loop of the barrel and of antibodies on porcine pancreas amylase activity
    • Desseaux, V., Payan, F., Ajandouz, E. H., Svensson, B., Haser, R. & Marchis-Mouren, G. (1991) Effect of limited proteolysis in the 8th loop of the barrel and of antibodies on porcine pancreas amylase activity, Biochim. Biophys. Acta 1080, 237-244.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 237-244
    • Desseaux, V.1    Payan, F.2    Ajandouz, E.H.3    Svensson, B.4    Haser, R.5    Marchis-Mouren, G.6
  • 8
    • 0013833244 scopus 로고
    • Determination of reducing sugar with improved precision
    • Dygert, S., Li, L. H., Don Florida, R. & Thoma, J. A. (1965) Determination of reducing sugar with improved precision. Anal. Chem. 13, 367-374.
    • (1965) Anal. Chem. , vol.13 , pp. 367-374
    • Dygert, S.1    Li, L.H.2    Don Florida, R.3    Thoma, J.A.4
  • 9
    • 0015518062 scopus 로고
    • Investigation of the active center of porcine pancreatic α-amylase
    • Elödi, P., Mora, S. & Krysteva, M. (1972). Investigation of the active center of porcine pancreatic α-amylase, Eur. J. Biochem. 24, 577-582.
    • (1972) Eur. J. Biochem. , vol.24 , pp. 577-582
    • Elödi, P.1    Mora, S.2    Krysteva, M.3
  • 10
    • 0025284257 scopus 로고
    • The evolution of the α/β barrel enzymes
    • Farber, G. K. & Petsko, G. A. (1990) The evolution of the α/β barrel enzymes, Trends Biochem. Sci. 15, 228-234.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 228-234
    • Farber, G.K.1    Petsko, G.A.2
  • 11
    • 0029953633 scopus 로고    scopus 로고
    • Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose
    • Gilles, C., Astier, J.-P., Marchis-Mouren, G., Cambillau, C. & Payan, F. (1996) Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose, Eur. J. Biochem. 238, 561-569.
    • (1996) Eur. J. Biochem. , vol.238 , pp. 561-569
    • Gilles, C.1    Astier, J.-P.2    Marchis-Mouren, G.3    Cambillau, C.4    Payan, F.5
  • 12
    • 0016436566 scopus 로고
    • Enzymatic activity of TNB blocked porcine pancreatic α-amylase
    • Granger, M., Abadie, B., Mazzei, Y. & Marchis-Mouren, G. (1975) Enzymatic activity of TNB blocked porcine pancreatic α-amylase. FEBS Lett. 50, 276-278.
    • (1975) FEBS Lett. , vol.50 , pp. 276-278
    • Granger, M.1    Abadie, B.2    Mazzei, Y.3    Marchis-Mouren, G.4
  • 13
    • 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
  • 14
    • 33947472850 scopus 로고
    • A schematic method of deriving the rate laws for enzyme catalyzed reaction
    • King, E. L. & Altman, C. (1956) A schematic method of deriving the rate laws for enzyme catalyzed reaction, J. Phys. Chem. 60, 1375-1378.
    • (1956) J. Phys. Chem. , vol.60 , pp. 1375-1378
    • King, E.L.1    Altman, C.2
  • 15
    • 0014218572 scopus 로고
    • Isolation of two amylases in porcine pancreas
    • Marchis-Mouren, G. & Pasero, L. (1967) Isolation of two amylases in porcine pancreas. Biochim. Biophys. Acta 140, 366-368.
    • (1967) Biochim. Biophys. Acta , vol.140 , pp. 366-368
    • Marchis-Mouren, G.1    Pasero, L.2
  • 16
    • 0021395910 scopus 로고
    • Structure and possible catalytic residues of Taka-amylase
    • Matsuura, Y., Kusunoki, M., Harada, W. & Kakudo, M. (1984) Structure and possible catalytic residues of Taka-amylase, Biochemistry 95, 697-702.
    • (1984) Biochemistry , vol.95 , pp. 697-702
    • Matsuura, Y.1    Kusunoki, M.2    Harada, W.3    Kakudo, M.4
  • 17
    • 0000145923 scopus 로고
    • Brodbecle, V., ed. Verlag Chemie, Weinheim
    • Müller, L., Junge, B. & Frommer, W. (1980) in Enzyme inhibitors (Brodbecle, V., ed.) pp. 109-122, Verlag Chemie, Weinheim.
    • (1980) Enzyme Inhibitors , pp. 109-122
    • Müller, L.1    Junge, B.2    Frommer, W.3
  • 18
    • 0027296794 scopus 로고
    • Structure and molecular model refinement of pig pancreatic α-amylase at 2.1 Å resolution
    • Qian, M., Haser, R. & 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, R.2    Payan, F.3
  • 19
    • 0028198814 scopus 로고
    • The active center of a mammalian α-amylase. Structure of the complex of a pancreatic α-amylase with a carbohydrate inhibitor refined to 2.2-Å resolution
    • Qian, M., Buisson, G., Duée, E., Haser, R. & Payan, F (1994) The active center of a mammalian α-amylase. Structure of the complex of a pancreatic 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, R.4    Payan, F.5
  • 20
    • 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, R. & 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 Science 4, 747-755.
    • (1995) Protein Science , vol.4 , pp. 747-755
    • Qian, M.1    Haser, R.2    Payan, F.3
  • 21
    • 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. (1970) 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
  • 22
    • 0041663092 scopus 로고
    • Subsite structure and action mode of the α-amylase from Thermoactinomyces vulgaris
    • Sano, M., Sakano, Y. & Kobayashi, T. (1985) Subsite structure and action mode of the α-amylase from Thermoactinomyces vulgaris, Agric. Biol. Chem. 49, 2843.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 2843
    • Sano, M.1    Sakano, Y.2    Kobayashi, T.3
  • 24
    • 0027381121 scopus 로고
    • Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodexrins by nine cellulases
    • Schou, C., Rasmussen, G., Kaltoft, M.-B., Henrissat, B. & Schülein, M. (1993) Stereochemistry, specificity and kinetics of the hydrolysis of reduced cellodexrins by nine cellulases, Eur. J. Biochem. 217, 947-953.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 947-953
    • Schou, C.1    Rasmussen, G.2    Kaltoft, M.-B.3    Henrissat, B.4    Schülein, M.5
  • 25
    • 0021799919 scopus 로고
    • On porcine pancreatic α-amylase action. Kinetic evidence for the binding of two maltooligosaccharide molecules (maltose, maltotriose and o-nitrophenylmaltoside) by inhibition studies. Correlation with the five subsite energy profile
    • Seigner, C., Prodanov, E. & Marchis-Mouren, G. (1985) On porcine pancreatic α-amylase action. Kinetic evidence for the binding of two maltooligosaccharide molecules (maltose, maltotriose and o-nitrophenylmaltoside) by inhibition studies. Correlation with the five subsite energy profile, Eur. J. Biochem. 148, 161-168.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 161-168
    • Seigner, C.1    Prodanov, E.2    Marchis-Mouren, G.3
  • 26
    • 0018175456 scopus 로고
    • Study of the mechanism of action of Taka-amylase A on linear oligosaccharides by product analysis and computer simulation
    • Suganuma, T., Matsuno, R., Ohnishi, M & Hiromi, K. (1978) Study of the mechanism of action of Taka-amylase A on linear oligosaccharides by product analysis and computer simulation, Biochemistry 84, 293-316.
    • (1978) Biochemistry , vol.84 , pp. 293-316
    • Suganuma, T.1    Matsuno, R.2    Ohnishi, M.3    Hiromi, K.4
  • 27
    • 0026657993 scopus 로고
    • Interaction of catalytic-site mutants of Bacillus subtilis alpha-amylase with substrate and acarbose
    • Takase, K. (1992) Interaction of catalytic-site mutants of Bacillus subtilis alpha-amylase with substrate and acarbose, Biochim. Biophys. Acta 1122, 278-282.
    • (1992) Biochim. Biophys. Acta , vol.1122 , pp. 278-282
    • Takase, K.1
  • 28
    • 0021759424 scopus 로고
    • Some aspects of the mechanism of complexation of red kidney bean α-amylase inhibitor and α-amylase
    • Wilcox, E. R. & Whitaker, J. R. (1984) Some aspects of the mechanism of complexation of red kidney bean α-amylase inhibitor and α-amylase, Biochemistry 23, 1783-1791.
    • (1984) Biochemistry , vol.23 , pp. 1783-1791
    • Wilcox, E.R.1    Whitaker, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.