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Volumn 57, Issue 19, 2009, Pages 9218-9225

Kinetic analysis and mechanism on the inhibition of chlorogenic acid and its components against porcine pancreas α-amylase isozymes I and II

Author keywords

amylase inhibitor; Caffeic acid; Chlorogenic acid; Enzyme kinetics; Mixed type inhibition

Indexed keywords

AMYLASE; CHLOROGENIC ACID; ENZYME INHIBITOR; ISOENZYME;

EID: 70349931377     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9017383     Document Type: Article
Times cited : (116)

References (41)
  • 1
    • 0003906557 scopus 로고
    • The influence of coffee bean maturity on the content of chlorogenic acids, caffeine and trigonelline
    • Clifford, M. N.; Kazi, T. The influence of coffee bean maturity on the content of chlorogenic acids, caffeine and trigonelline. Food Chem. 1987, 26, 59-69.
    • (1987) Food Chem. , vol.26 , pp. 59-69
    • Clifford, M.N.1    Kazi, T.2
  • 2
    • 33645760745 scopus 로고    scopus 로고
    • Characterization by LC-MSn of four new classes of chlorogenic acid in green coffee beans: Dimethoxycinnamoylquinic acids, diferuloylquinic acids, and feruloyl-dimethoxycinnamoylquinic acids
    • Clifford, M. N.; Knight, S.; Surucu, B.; Kuhnert, N. T. Characterization by LC-MSn of four new classes of chlorogenic acid in green coffee beans: Dimethoxycinnamoylquinic acids, diferuloylquinic acids, and feruloyl- dimethoxycinnamoylquinic acids. J. Agric. Food Chem. 2006, 54, 1957-1969.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 1957-1969
    • Clifford, M.N.1    Knight, S.2    Surucu, B.3    Kuhnert, N.T.4
  • 3
    • 0032989507 scopus 로고    scopus 로고
    • Chlorogenic acids and other cinnaniates: Nature, occurrence and dietary burden
    • Clifford, M. N. Chlorogenic acids and other cinnaniates: Nature, occurrence and dietary burden. J. Sci. Food Agric. 1999, 79, 362-372.
    • (1999) J. Sci. Food Agric. , vol.79 , pp. 362-372
    • Clifford, M.N.1
  • 4
    • 0034824561 scopus 로고    scopus 로고
    • Caffeine, trigonelline, chlorogenic acids and sucrose diversity in wild Coffea arabica L. and C. eanephora P. accessions
    • Ky, C.-L.; Louarn, J.; Dussert, S.; Guyot, B.; Hamon, S.; Noirot, M. Caffeine, trigonelline, chlorogenic acids and sucrose diversity in wild Coffea arabica L. and C. eanephora P. accessions. Food Chem. 2001, 75, 223-230.
    • (2001) Food Chem. , vol.75 , pp. 223-230
    • Ky, C.-L.1    Louarn, J.2    Dussert, S.3    Guyot, B.4    Hamon, S.5    Noirot, M.6
  • 5
    • 0003187515 scopus 로고
    • Nomenclature of cyclitos
    • IUPAC
    • IUPAC. Nomenclature of cyclitos. Biochem. J. 1916, 153, 23-31.
    • (1916) Biochem. J. , vol.153 , pp. 23-31
  • 7
    • 0000924927 scopus 로고
    • Antioxidative caffeoylquinic acid derivatives in the roots of burdock. (Arctium lappa L.)
    • Maruta, Y.; Kawabata, J.; Niki, R. Antioxidative caffeoylquinic acid derivatives in the roots of burdock. (Arctium lappa L.). J. Agric, Food Chem. 1995, 43, 2592-2595.
    • (1995) J. Agric, Food Chem. , vol.43 , pp. 2592-2595
    • Maruta, Y.1    Kawabata, J.2    Niki, R.3
  • 8
    • 0037134638 scopus 로고    scopus 로고
    • Identification and characterization of foliar polyphenolic composition in sweetpotato (Ipomoea batatas L) genotypes
    • Islam, M. S.; Yoshimoto, M.; Yahara, S.; Okuno, S.; Ishiguro, K.; Yamakawa, O. Identification and characterization of foliar polyphenolic composition in sweetpotato (Ipomoea batatas L) genotypes. J. Agric. Food Chem. 2002, 50, 3718-3722.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 3718-3722
    • Islam, M.S.1    Yoshimoto, M.2    Yahara, S.3    Okuno, S.4    Ishiguro, K.5    Yamakawa, O.6
  • 9
    • 0030918880 scopus 로고
    • Antioxidant activity of polyphenolics in diets: Rate constants of reactions of chlorogenic acid and caffeic acid with reactive species of oxygen and nitrogen
    • Kono, Y.; Kobayashi, K.; Tagawa, S.; Adachi, K.; Ueda, A.; Sawa, Y.; Shibata, H. Antioxidant activity of polyphenolics in diets: Rate constants of reactions of chlorogenic acid and caffeic acid with reactive species of oxygen and nitrogen. Biochim. Biophys. Acta 1991, 1335, 335-342.
    • (1991) Biochim. Biophys. Acta , vol.1335 , pp. 335-342
    • Kono, Y.1    Kobayashi, K.2    Tagawa, S.3    Adachi, K.4    Ueda, A.5    Sawa, Y.6    Shibata, H.7
  • 10
    • 24744434694 scopus 로고    scopus 로고
    • A phenolic compound, 5-caffeoylquinic acid (chlorogenic acid), is a new type and strong matrix metalloproteinase-9 inhibitor: Isolation and identification from methanol extract of Euonymus alatus
    • Jin, U.-H.; Lee, J.-Y.; Kang, S.-K.; Kim, J.-K.; Park, W.-H.; Kim, J.-G.; Moon, S.-K.; Kim, A.-H. A phenolic compound, 5-caffeoylquinic acid (chlorogenic acid), is a new type and strong matrix metalloproteinase-9 inhibitor: Isolation and identification from methanol extract of Euonymus alatus. Life Sci. 2005, 77, 2760-2769.
    • (2005) Life Sci. , vol.77 , pp. 2760-2769
    • Jin, U.-H.1    Lee, J.-Y.2    Kang, S.-K.3    Kim, J.-K.4    Park, W.-H.5    Kim, J.-G.6    Moon, S.-K.7    Kim, A.-H.8
  • 11
    • 3242797244 scopus 로고    scopus 로고
    • In vitro antioxidative effects and tyrosinase inhibitory activities of seven hydroxycinnamoyl derivatives in green coffee beans
    • Iwai, K.; Kishimoto, N.; Kakino, Y.; Mochida, K.; Fujita, T. In vitro antioxidative effects and tyrosinase inhibitory activities of seven hydroxycinnamoyl derivatives in green coffee beans. J. Agric. Food Chem. 2004, 52, 4893-4898.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 4893-4898
    • Iwai, K.1    Kishimoto, N.2    Kakino, Y.3    Mochida, K.4    Fujita, T.5
  • 12
    • 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. The action pattern of porcine pancreatic α-amylase in relationship to the substrate binding site of the enzyme. J. Biol. Chem. 1970, 245, 3917-3927.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3917-3927
    • Robyt, J.F.1    French, D.2
  • 15
  • 16
    • 0014218572 scopus 로고
    • Isolation of two amylases in porcine pancreas
    • Marchis-Mouren, G.; Pasero, L. Isolation of two amylases in porcine pancreas. Biochim. Biophys. Acta 1961, 140, 366-368.
    • (1961) Biochim. Biophys. Acta , vol.140 , pp. 366-368
    • Marchis-Mouren, G.1    Pasero, L.2
  • 17
    • 0019890472 scopus 로고
    • Amino acid sequence of hog pancreatic α-amylase isoenzyme I
    • Kluh, I. Amino acid sequence of hog pancreatic α-amylase isoenzyme I. FEBS Lett. 1981, 136, 231-234.
    • (1981) FEBS Lett. , vol.136 , pp. 231-234
    • Kluh, I.1
  • 18
    • 0344948480 scopus 로고
    • Hog pancreatic α-amylase. Peptides from tryptic digest of isoenzyme All
    • Meloun, B.; Kluh, I.; Moravek, L. Hog pancreatic α-amylase. Peptides from tryptic digest of isoenzyme All. Collect. Czech. Chem. Commun. 1980, 45, 2572-2582.
    • (1980) Collect. Czech. Chem. Commun. , vol.45 , pp. 2572-2582
    • Meloun, B.1    Kluh, I.2    Moravek, L.3
  • 19
    • 0029957475 scopus 로고    scopus 로고
    • The mechanism of porcine pancreatic α-amylase. Kinetic evidence for two additional carbohydrate-binding sites
    • (19) Al Kazaz, M.; Desseaux, V.; Marchis-Mouren, G.; Payan, F.; Forest, E; Santimone, M. The mechanism of porcine pancreatic α-amylase: Kinetic evidence for two additional carbohydrate binding sites. Eur. J. Biochem. 1996, 241, 787-796. (Pubitemid 26379381)
    • (1996) European Journal of Biochemistry , vol.241 , Issue.3 , pp. 787-796
    • Alkazaz, M.1    Desseaux, V.2    Marchis-Mouren, G.3    Payan, F.4    Forest, E.5    Santimone, M.6
  • 20
    • 0002247392 scopus 로고
    • Purification and properties of two active components from crystalline preparation of porcine pancreatic α-amylase
    • Sakano, Y.; Takahashi, S.; Kobayashi, T. Purification and properties of two active components from crystalline preparation of porcine pancreatic α-amylase. J. Jpn. Soc. Starch Sci. 1983, 30, 30-37.
    • (1983) J. Jpn. Soc. Starch Sci. , vol.30 , pp. 30-37
    • Sakano, Y.1    Takahashi, S.2    Kobayashi, T.3
  • 21
    • 33750098250 scopus 로고    scopus 로고
    • White bean amylase inhibitor administered orally reduces glycemia in type 2 diabetic rats
    • Tormo, M. A.; Gil-Exojo, I.; Romero de Tejada, A.; Campillo, J. E. White bean amylase inhibitor administered orally reduces glycemia in type 2 diabetic rats. Br. J. Nutr. 2006, 96, 539-544.
    • (2006) Br. J. Nutr. , vol.96 , pp. 539-544
    • Tormo, M.A.1    Gil-Exojo, I.2    Romero De Tejada, A.3    Campillo, J.E.4
  • 22
    • 40949146199 scopus 로고    scopus 로고
    • Chestnut astringent skin extract, an α-amylase inhibitor, retards carbohydrate absorption in rats and humans
    • Tsujita, T.; Yakaku, T.; Suzuki, T. Chestnut astringent skin extract, an α-amylase inhibitor, retards carbohydrate absorption in rats and humans. J. Nutr. Sci. Vitaminal. 2008, 54, 82-88.
    • (2008) J. Nutr. Sci. Vitaminal. , vol.54 , pp. 82-88
    • Tsujita, T.1    Yakaku, T.2    Suzuki, T.3
  • 23
    • 0032520085 scopus 로고    scopus 로고
    • The mechanism of porcine pancreatic α-amylase. Inhibition of maltopentaose hydrolysis by acarbose, maltose and maltotriose
    • (23) Al Kazaz, M.; Desseaux, V.; Marchis-Mouren, G.; Prodanov, E.; Santimone, M. The mechanism of porcine pancreatic α-amylase: Inhibition of maltopentaose hydrolysis by acarbose, maltose and maltotriose. Eur. J. Biochem. 1998, 252, 100-107. (Pubitemid 28089963)
    • (1998) European Journal of Biochemistry , vol.252 , Issue.1 , pp. 100-107
    • Al Kazaz, M.1    Desseaux, V.2    Marchis-Mouren, G.3    Prodanov, E.4    Santimone, M.5
  • 24
    • 1942455756 scopus 로고    scopus 로고
    • Inhibitory Effect of 0.19 α-Amylase Inhibitor from Wheat Kernel on the Activity of Porcine Pancreas α-Amylase and Its Thermal Stability
    • DOI 10.1093/jb/mvh050
    • (24) Oneda, H.; Lee, S.; Inouye, K. Inhibitory effect of 0.19 α-amylase inhibitor from wheat kernel on the activity of porcine pancreas α-amylase and its thermal stability. J. Biochem. 2004, 135, 421-427. (Pubitemid 38506768)
    • (2004) Journal of Biochemistry , vol.135 , Issue.3 , pp. 421-427
    • Oneda, H.1    Lee, S.2    Inouye, K.3
  • 25
    • 0037023972 scopus 로고    scopus 로고
    • Inhibitory effects of plant phenols on the activity of selected enzymes
    • DOI 10.1021/jf011714b
    • (25) Rohn, S.; Rawel, H. M.; Kroll, J. Inhibitory effects of plant phenols on the activity of selected enzymes. J. Agric. Food Chem. 2002, 50, 3566-3571. (Pubitemid 34579292)
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.12 , pp. 3566-3571
    • Rohn, S.1    Rawel, H.M.2    Kroll, J.3
  • 26
    • 0015975824 scopus 로고
    • The allosteric activation of mammalian alpha-amylase by chloride
    • Levitzki, A.; Steer, M. L. The allosteric activation of mammalian alpha-amylase by chloride. Eur. J. Biochem. 1974, 41, 171-180.
    • (1974) Eur. J. Biochem. , vol.41 , pp. 171-180
    • Levitzki, A.1    Steer, M.L.2
  • 27
    • 0025953024 scopus 로고
    • Substrate-selective activation of histidine-modified porcine pancreatic α-amylase by chloride ion
    • Yamashita, H.; Nakatani, H.; Tonomura, B. Substrate-selective activation of histidine-modified porcine pancreatic α-amylase by chloride ion. J. Biochem. 1991, 110, 605-607.
    • (1991) J. Biochem. , vol.110 , pp. 605-607
    • Yamashita, H.1    Nakatani, H.2    Tonomura, B.3
  • 28
    • 0002035802 scopus 로고
    • Rapid equilibrium partial and mixed-type inhibition
    • John Wiley & Sons: New York
    • Segel, I. H. Rapid Equilibrium Partial and Mixed-Type Inhibition. In Enzyme Kinetics; John Wiley & Sons: New York, 1975; pp 161-226.
    • (1975) Enzyme Kinetics , pp. 161-226
    • Segel, I.H.1
  • 29
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors
    • Cornish-Bowden, A. A simple graphical method for determining the inhibition constants of mixed, uncompetitive and non-competitive inhibitors. Biochem. J. 1974, 137, 143-144.
    • (1974) Biochem. J. , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1
  • 30
    • 0029863639 scopus 로고    scopus 로고
    • Effect of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts
    • (30) Inouye, K.; Lee, S.-B.; Tonomura, B. Effects of amino acid residues at the cleavable site of substrates on the remarkable activation of thermolysin by salts. Biochem. J. 1996, 315, 133-138. (Pubitemid 26113544)
    • (1996) Biochemical Journal , vol.315 , Issue.1 , pp. 133-138
    • Inouye, K.1    Lee, S.-B.2    Tonomura, B.3
  • 31
    • 0028129002 scopus 로고
    • A spectrophotometric study on the interaction of thermolysin with chloride and bromide ions, and the state of tryptophyl residue 115
    • (31) Inouye, K.; Kuzuya, K.; Tonomura, B. A spectrophotometry study on the interaction of thermolysin with chloride and bromide ions, and the states of tryptophyl residue 115. J. Biochem, 1994, 116, 530-535. (Pubitemid 24294779)
    • (1994) Journal of Biochemistry , vol.116 , Issue.3 , pp. 530-535
    • Inouye, K.1    Kuzuya, K.2    Tonomura, B.3
  • 32
    • 0036947384 scopus 로고    scopus 로고
    • Inhibitory effects of alcohols on thermolysin activity as examined using a fluorescent substrate
    • (32) Muta, Y.; Inouye, K. Inhibitory effects of alcohols on thermolysin activity as examined using a fluorescent substrate. J. Biochem, 2002, 132, 945-951. (Pubitemid 36090661)
    • (2002) Journal of Biochemistry , vol.132 , Issue.6 , pp. 945-951
    • Muta, Y.1    Inouye, K.2
  • 33
    • 0035054059 scopus 로고    scopus 로고
    • Interactions of human matrix metalloproteinase 7 (Matrilysin) with the inhibitors thiorphan and R-94138
    • (33) Oneda, H.; Inouye, K. Interactions of human matrix metalloproteinase 7 (matrilysin) with the inhibitors thiorphan and R-94138. J. Biochem. 2001, 129, 429-435. (Pubitemid 32304118)
    • (2001) Journal of Biochemistry , vol.129 , Issue.3 , pp. 429-435
    • Oneda, H.1    Inouye, K.2
  • 35
    • 0023040231 scopus 로고
    • Crystallography structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin
    • Tronrud, D. E.; Monzingo, A. F.; Matthews, B. W. Crystallography structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysin. Eur. J. Biochem. 1986, 157, 261-268.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 261-268
    • Tronrud, D.E.1    Monzingo, A.F.2    Matthews, B.W.3
  • 36
    • 0009830401 scopus 로고
    • Inhibitors and activators
    • Butterworths: London
    • Cornish-Bowden, A. Inhibitors and Activators. In Principles of Enzyme Kinetics; Butterworths: London, 1976; pp 52-70.
    • (1976) Principles of Enzyme Kinetics , pp. 52-70
    • Cornish-Bowden, A.1
  • 37
    • 0038647540 scopus 로고    scopus 로고
    • Inhibitory effects of green tea catechins on the activity of human matrix metalloproteinase 7 (matrilysin)
    • DOI 10.1093/jb/mvg073
    • (37) Oneda, H.; Shiihara, M.; Inouye, K. Inhibitory effects of green tea catechins on the activity of human matrix metalloproteinases 7 (matrilysin). J. Biochem. 2003, 133, 571-576. (Pubitemid 36759463)
    • (2003) Journal of Biochemistry , vol.133 , Issue.5 , pp. 571-576
    • Oneda, H.1    Shiihara, M.2    Inouye, K.3
  • 38
    • 0003408336 scopus 로고
    • Strain, distortion, and conformation change
    • McGraw-Hill: New York
    • Jencks, W. P. Strain, Distortion, and Conformation Change. In Catalysis in Chemistry and Enzymology; McGraw-Hill: New York, 1969; pp 282-320.
    • (1969) Catalysis in Chemistry and Enzymology , pp. 282-320
    • Jencks, W.P.1
  • 39
    • 0035107447 scopus 로고    scopus 로고
    • Entropy-enthalpy compensation: Fact or artifact?
    • DOI 10.1110/ps.37801
    • (39) Sharp, K. Entropy-enthalpy compensation: Fact or artifact? Protein Sci. 2001, 10, 661-667. (Pubitemid 32221155)
    • (2001) Protein Science , vol.10 , Issue.3 , pp. 661-667
    • Sharp, K.1
  • 40
    • 0036120608 scopus 로고    scopus 로고
    • Enthalpy-entropy compensation: A phantom phenomenon
    • Cornish-Bowden, A. Enthalpy-entropy compensation: a phantom phenomenon. J. Biosci. 2002, 27, 121-126.
    • (2002) J. Biosci. , vol.27 , pp. 121-126
    • Cornish-Bowden, A.1
  • 41
    • 0141751492 scopus 로고    scopus 로고
    • Mechanism of porcine pancreatic α-amylase: Inhibition of amylase and maltopentaose hydrolysis by various inhibitors
    • Desseaux, V.; Koukiekolo, R.; Moreau, Y.; Santimore, M.; MarchisMouren, G. Mechanism of porcine pancreatic α-amylase: inhibition of amylase and maltopentaose hydrolysis by various inhibitors. Biologia (Bratislava) 2002, 57, 163-170.
    • (2002) Biologia (Bratislava) , vol.57 , pp. 163-170
    • Desseaux, V.1    Koukiekolo, R.2    Moreau, Y.3    Santimore, M.4    Marchismouren, G.5


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