메뉴 건너뛰기




Volumn 276, Issue 13, 2009, Pages 3531-3546

Digestive α-amylases of the flour moth Ephestia kuehniella- adaptation to alkaline environment and plant inhibitors

Author keywords

amylase; amylase inhibitor; Alkaline adaptation; Ephestia kuehniella; Plant insect interaction

Indexed keywords

AMYLASE; AMYLASE INHIBITOR; CHLORIDE; COMPLEMENTARY DNA;

EID: 67650445670     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2009.07074.x     Document Type: Article
Times cited : (50)

References (42)
  • 1
    • 0030778420 scopus 로고    scopus 로고
    • α-Amylase family: Molecular biology and evolution
    • DOI 10.1016/S0079-6107(97)00015-1, PII S0079610797000151
    • Janecek S (1997) Alpha-amylase family: molecular biology and evolution. Prog Biophys Mol Biol 67, 67 97. (Pubitemid 27491749)
    • (1997) Progress in Biophysics and Molecular Biology , vol.67 , Issue.1 , pp. 67-97
    • Janecek, S.1
  • 3
    • 0036164521 scopus 로고    scopus 로고
    • Plant α-amylase inhibitors and their interaction with insect α-amylases
    • Franco OL, Rigden DJ, Melo FR Grossi De Sa MF (2002) Plant α-amylase inhibitors and their interaction with insect α-amylases. Eur J Biochem 269, 397 412.
    • (2002) Eur J Biochem , vol.269 , pp. 397-412
    • Franco, O.L.1    Rigden, D.J.2    Melo, F.R.3    Grossi De Sa, M.F.4
  • 5
    • 0031127270 scopus 로고    scopus 로고
    • Molecular cloning of bruchid (Zabrotes subfasciatus) α-amylase cDNA and interactions of the expressed enzyme with bean amylase inhibitors
    • DOI 10.1016/S0965-1748(96)00093-8, PII S0965174896000938
    • Grossi de Sa MF Chrispeels MJ (1997) Molecular cloning of bruchid (Zabrotes subfasciatus) alpha-amylase cDNA and interactions of the expressed enzyme with bean amylase inhibitors. Insect Biochem Mol Biol 27, 271 281. (Pubitemid 27174935)
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , Issue.4 , pp. 271-281
    • Grossi De Sa, M.F.1    Chrispeels, M.J.2
  • 7
    • 0027672394 scopus 로고
    • High pH in the ectoperitrophic space of the larval lepidopteran midgut
    • Gringorten JL, Crawford DN Harvey WR (1993) High pH in the ectoperitrophic space of the larval lepidopteran midgut. J Exp Biol 183, 353 359.
    • (1993) J Exp Biol , vol.183 , pp. 353-359
    • Gringorten, J.L.1    Crawford, D.N.2    Harvey, W.R.3
  • 9
    • 0040057329 scopus 로고
    • Interaction of partially-purified amylases from larval Anagasta kuehniella (Lepidoptera: Pyralidae) with amylase inhibitors from wheat
    • Baker JE (1989) Interaction of partially-purified amylases from larval Anagasta kuehniella (Lepidoptera: Pyralidae) with amylase inhibitors from wheat. Comp Biochem Physiol 93B, 239 246.
    • (1989) Comp Biochem Physiol , vol.93 , pp. 239-246
    • Baker, J.E.1
  • 11
    • 11844261463 scopus 로고    scopus 로고
    • Inhibitory specificity and insecticidal selectivity of α-amylase inhibitor from Phaseolus vulgaris
    • DOI 10.1016/j.phytochem.2004.11.001, PII S0031942204005898
    • Kluh I, Horn M, Hyblova J, Hubert J, Doleckova-Maresova L, Voburka Z, Kudlikova I, Kocourek F Mares M (2005) Inhibitory specificity and insecticidal selectivity of alpha-amylase inhibitor from Phaseolus vulgaris. Phytochemistry 66, 31 39. (Pubitemid 40092723)
    • (2005) Phytochemistry , vol.66 , Issue.1 , pp. 31-39
    • Kluh, I.1    Horn, M.2    Hyblova, J.3    Hubert, J.4    Doleckova-Maresova, L.5    Voburka, Z.6    Kudlikova, I.7    Kocourek, F.8    Mares, M.9
  • 12
    • 0033571485 scopus 로고    scopus 로고
    • Comparative study of the inhibition of alpha-glucosidase, alpha-amylase, and cyclomaltodextrin glucanosyltransferase by acarbose, isoacarbose, and acarviosine-glucose
    • Kima MJ, Leeb SB, Leea HS, Leea SY, Baeka JS, Kimc D, Moona TW, Robytd JF Park KH (1999) Comparative study of the inhibition of alpha-glucosidase, alpha-amylase, and cyclomaltodextrin glucanosyltransferase by acarbose, isoacarbose, and acarviosine-glucose. Arch Biochem Biophys 371, 277 283.
    • (1999) Arch Biochem Biophys , vol.371 , pp. 277-283
    • Kima, M.J.1    Leeb, S.B.2    Leea, H.S.3    Leea, S.Y.4    Baeka, J.S.5    Kimc, D.6    Moona, T.W.7    Robytd, J.F.8    Park, K.H.9
  • 13
    • 0029111443 scopus 로고
    • The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes
    • Brayer GD, Luo Y Withers SG (1995) The structure of human pancreatic alpha-amylase at 1.8 A resolution and comparisons with related enzymes. Protein Sci 4, 1730 1742.
    • (1995) Protein Sci , vol.4 , pp. 1730-1742
    • Brayer, G.D.1    Luo, Y.2    Withers, S.G.3
  • 15
    • 33749600412 scopus 로고    scopus 로고
    • Origin and evolution of the Amyrel gene in the α-amylase multigene family of Diptera
    • DOI 10.1007/s10709-005-5578-y
    • Maczkowiak F Da Lage JL (2006) Origin and evolution of the Amyrel gene in the alpha-amylase multigene family of Diptera. Genetica 128, 145 158. (Pubitemid 44544110)
    • (2006) Genetica , vol.128 , Issue.1-3 , pp. 145-158
    • Maczkowiak, F.1    Lage, J.-L.D.2
  • 16
    • 33846218264 scopus 로고    scopus 로고
    • Ancestral sequence evolutionary trace and crystal structure analyses of alkaline α-amylase from Bacillus sp. KSM-1378 to clarify the alkaline adaptation process of proteins
    • DOI 10.1002/prot.21255
    • Shirai T, Igarashi K, Ozawa T, Hagihara H, Kobayashi T, Ozaki K Ito S (2007) Ancestral sequence evolutionary trace and crystal structure analyses of alkaline alpha-amylase from Bacillus sp. KSM-1378 to clarify the alkaline adaptation process of proteins. Proteins 66, 600 610. (Pubitemid 46106764)
    • (2007) Proteins: Structure, Function and Genetics , vol.66 , Issue.3 , pp. 600-610
    • Shirai, T.1    Igarashi, K.2    Ozawa, T.3    Hagihara, H.4    Kobayashi, T.5    Ozaki, K.6    Ito, S.7
  • 17
    • 0023661282 scopus 로고
    • Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A resolution. Role of calcium in structure and activity
    • Buisson G, Duée E, Haser R Payan F (1987) Three dimensional structure of porcine pancreatic alpha-amylase at 2.9 A 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
  • 18
    • 0037039359 scopus 로고    scopus 로고
    • Probing the role of the chloride ion in the mechanism of human pancreatic α-amylase
    • DOI 10.1021/bi0115636
    • Numao S, Maurus R, Sidhu G, Wang Y, Overall CM, Brayer GD Withers SG (2002) Probing the role of the chloride ion in the mechanism of human pancreatic alpha-amylase. Biochemistry 41, 215 225. (Pubitemid 34049397)
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 215-225
    • Numao, S.1    Maurus, R.2    Sidhu, G.3    Wang, Y.4    Overall, C.M.5    Brayer, G.D.6    Withers, S.G.7
  • 19
    • 0034713903 scopus 로고    scopus 로고
    • Structural similarities and evolutionary relationships in chloride-dependent α-amylases
    • DOI 10.1016/S0378-1119(00)00229-8, PII S0378111900002298
    • D'Amico S, Gerday C Feller G (2000) Structural similarities and evolutionary relationships in chloride-dependent α-amylases. Gene 253, 95 105. (Pubitemid 30488890)
    • (2000) Gene , vol.253 , Issue.1 , pp. 95-105
    • D'Amico, S.1    Gerday, C.2    Feller, G.3
  • 22
    • 0035163047 scopus 로고    scopus 로고
    • Apocrine secretion of amylase and exocytosis of trypsin along the midgut of Tenebrio molitor larvae
    • DOI 10.1016/S0022-1910(00)00098-6, PII S0022191000000986
    • Cristofoletti PT, Ribeiro AF Terra WR (2001) Apocrine secretion of amylase and exocytosis of trypsin along the midgut of Tenebrio molitor larvae. J Insect Physiol 47, 143 155. (Pubitemid 32055320)
    • (2001) Journal of Insect Physiology , vol.47 , Issue.2 , pp. 143-155
    • Cristofoletti, P.T.1    Ribeiro, A.F.2    Terra, W.R.3
  • 23
    • 0035377001 scopus 로고    scopus 로고
    • The peritrophic membrane of Spodoptera frugiperda: Secretion of peritrophins and role in immobilization and recycling digestive enzymes
    • DOI 10.1002/arch.1037
    • Bolognesi R, Ribeiro AF, Terra WR Ferreira C (2001) The peritrophic membrane of Spodoptera frugiperda: secretion of peritrophins and role in immobilization and recycling digestive enzymes. Arch Insect Biochem Physiol 47, 62 75. (Pubitemid 33614318)
    • (2001) Archives of Insect Biochemistry and Physiology , vol.47 , Issue.2 , pp. 62-75
    • Bolognesi, R.1    Ribeiro, A.F.2    Terra, W.R.3    Ferreira, C.4
  • 24
    • 0032528247 scopus 로고    scopus 로고
    • A novel strategy for inhibition of α-amylases: Yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 Å resolution
    • Strobl S, Maskos K, Wiegand G, Huber R, Gomis-Ruth FX Glockshuber R (1998) A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 Å resolution. Structure 6, 911 921. (Pubitemid 28348653)
    • (1998) Structure , vol.6 , Issue.7 , pp. 911-921
    • Strobl, S.1    Maskos, K.2    Wiegand, G.3    Huber, R.4    Gomis-Ruth, F.X.5    Glockshuber, R.6
  • 25
    • 0029128219 scopus 로고
    • Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition
    • Jongsma MA, Bakker PL, Peters J, Bosch D Stiekema WJ (1995) Adaptation of Spodoptera exigua larvae to plant proteinase inhibitors by induction of gut proteinase activity insensitive to inhibition. Proc Natl Acad Sci USA 92, 8041 8045.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8041-8045
    • Jongsma, M.A.1    Bakker, P.L.2    Peters, J.3    Bosch, D.4    Stiekema, W.J.5
  • 26
    • 0344784409 scopus 로고    scopus 로고
    • Characterization of major midgut proteinase cDNAs from Helicoverpa armigera larvae and changes in gene expression in response to four proteinase inhibitors in the diet
    • DOI 10.1016/S0965-1748(97)00074-X, PII S096517489700074X
    • Gatehouse LN, Shannon AL, Burgess EP Christeller JT (1997) Characterization of major midgut proteinase cDNAs from Helicoverpa armigera larvae and changes in gene expression in response to four proteinase inhibitors in the diet. Insect Biochem Mol Biol 27, 929 944. (Pubitemid 28093032)
    • (1997) Insect Biochemistry and Molecular Biology , vol.27 , Issue.11 , pp. 929-944
    • Gatehouse, L.N.1    Shannon, A.L.2    Burgess, E.P.J.3    Christeller, J.T.4
  • 27
    • 1842591814 scopus 로고    scopus 로고
    • Molecular basis of Colorado potato beetle adaptation to potato plant defence at the level of digestive cysteine proteinases
    • DOI 10.1016/j.ibmb.2004.01.003, PII S0965174804000116
    • Gruden K, Kuipers AG, Guncar G, Slapar N, Strukelj B Jongsma MA (2004) Molecular basis of Colorado potato beetle adaptation to potato plant defence at the level of digestive cysteine proteinases. Insect Biochem Mol Biol 34, 365 375. (Pubitemid 38431047)
    • (2004) Insect Biochemistry and Molecular Biology , vol.34 , Issue.4 , pp. 365-375
    • Gruden, K.1    Kuipers, A.G.J.2    Guncar, G.3    Slapar, N.4    Strukelj, B.5    Jongsma, M.A.6
  • 28
    • 0141858719 scopus 로고    scopus 로고
    • Directed evolution of a bacterial α-amylase: Toward enhanced pH-performance and higher specific activity
    • DOI 10.1110/ps.0384403
    • Bessler C, Schmitt J, Maurer KH Schmid RD (2003) Directed evolution of a bacterial alpha-amylase: toward enhanced pH-performance and higher specific activity. Protein Sci 12, 2141 2149. (Pubitemid 37163349)
    • (2003) Protein Science , vol.12 , Issue.10 , pp. 2141-2149
    • Bessler, C.1    Schmitt, J.2    Maurer, K.-H.3    Schmid, R.D.4
  • 29
    • 0034855331 scopus 로고    scopus 로고
    • The determinants of alpha-amylase pH-activity profiles
    • Nielsen JE, Borchert TV Vriend G (2001) The determinants of alpha-amylase pH-activity profiles. Protein Eng 14, 505 512.
    • (2001) Protein Eng , vol.14 , pp. 505-512
    • Nielsen, J.E.1    Borchert, T.V.2    Vriend, G.3
  • 30
    • 0036241627 scopus 로고    scopus 로고
    • Activity of carbohydrases in the gut of Bibionidae (Diptera) larvae
    • DOI 10.1016/S1164-5563(01)01130-X, PII S116455630101130X
    • Sustr V Frouz J (2002) Activity of carbohydrases in the gut of Bibionidae (Diptera) larvae. Eur J Soil Biol 38, 75 77. (Pubitemid 34463520)
    • (2002) European Journal of Soil Biology , vol.38 , Issue.1 , pp. 75-77
    • Sustr, V.1    Frouz, J.2
  • 33
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura K, Dudley J, Nei M Kumar S (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 24, 1596 1599. (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 34
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4, 406 425.
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 35
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • Schwede T, Kopp J, Guex N Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31, 3381 3385. (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 36
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • Russell RB Barton GJ (1992) Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins 14, 309 323.
    • (1992) Proteins , vol.14 , pp. 309-323
    • Russell, R.B.1    Barton, G.J.2
  • 38
    • 33646940952 scopus 로고    scopus 로고
    • Numerical integration of the cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert JP, Ciccotti G Berendsen HJ (1997) Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J Comput Phys 23, 327 341.
    • (1997) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.3
  • 40
    • 33748390341 scopus 로고    scopus 로고
    • Parametrized models of aqueous free energies of solvation based on pairwise descreening of solute atomic charges from a dielectric medium
    • Hawkins GD, Cramer CJ Truhlar DG (1996) Parametrized models of aqueous free energies of solvation based on pairwise descreening of solute atomic charges from a dielectric medium. J Phys Chem 100, 19824 19839. (Pubitemid 126786901)
    • (1996) Journal of Physical Chemistry , vol.100 , Issue.51 , pp. 19824-19839
    • Hawkins, G.D.1    Cramer, C.J.2    Truhlar, D.G.3
  • 41
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff D, Sharp KA Honig B (1994) Accurate calculation of hydration free energies using macroscopic solvent models. J Phys Chem 98, 1978 1988.
    • (1994) J Phys Chem , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 42
    • 0033468737 scopus 로고    scopus 로고
    • Application of a pairwise generalized Born model to proteins and nucleic acids: Inclusion of salt effects
    • Srinivasan J, Trevathan MW, Beroza P Case DA (1999) Application of a pairwise generalized Born model to proteins and nucleic acids: inclusion of salt effects. Theor Chem Accounts 101, 426 434.
    • (1999) Theor Chem Accounts , vol.101 , pp. 426-434
    • Srinivasan, J.1    Trevathan, M.W.2    Beroza, P.3    Case, D.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.