A heterotetrameric alpha-amylase inhibitor from emmer (Triticum dicoccon Schrank) seeds

Phytochemistry

Volumn 88, Issue , 2013, Pages 6-14

  Capocchi, A ^a   Muccilli, V ^b   Cunsolo, V ^b   Saletti, R ^b   Foti, S ^b   Fontanini, D ^a  

^a UNIVERSITY OF PISA   (Italy)

^b UNIVERSITY OF CATANIA   (Italy)

Author keywords

CM protein; Heterotetrameric amylase inhibitor; Homology modeling; Kinetic study; Tandem mass spectrometry; Triticum dicoccon

Indexed keywords

AMYLASE; ENZYME INHIBITOR; PLANT EXTRACT;

ANIMAL; ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; DRUG ANTAGONISM; DRUG EFFECT; ENZYME ACTIVATION; HUMAN; ISOLATION AND PURIFICATION; MASS SPECTROMETRY; PLANT SEED; SEQUENCE HOMOLOGY; SWINE; WHEAT;

ALPHA-AMYLASES; ANIMALS; ENZYME ACTIVATION; ENZYME INHIBITORS; HUMANS; MASS SPECTROMETRY; MODELS, MOLECULAR; PLANT EXTRACTS; SEEDS; SEQUENCE HOMOLOGY; SWINE; TRITICUM;

SUS; TRITICUM AESTIVUM; TRITICUM DICOCCON; TRITICUM TURGIDUM SUBSP. DURUM;

EID: 84874350295     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2012.12.010     Document Type: Article

References (43)

1. N. Alam, S. Gourinath, S. Dey, A. Srinivasan, and T.P. Singh Substrate-inhibitor interactions in the kinetics of α-amylase inhibition by ragi α-amylase/trypsin inhibitor (RATI) and its various N-terminal fragments Biochemistry 40 2001 4229 4233 (Pubitemid 32319569)
2. P.J. Barbosa Pereira, V. Lozanov, A. Patthy, R. Huber, W. Bode, S. Pongor, and S. Strobl Specific inhibition of insect α-amylases: yellow meal worm α-amylase in complex with the Amaranth alpha-amylase inhibitor at 2.0 Å resolution Structure 7 1999 1079 1088 (Pubitemid 29436505)
3. Bieth, J., 1974. Some kinetic consequences of the tight binding of protein-proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants. Bayer-Symposium V "Proteinase Inhibitors", pp. 463-469.
4. C. Bompard-Gilles, P. Rosseau, P. Rouge, and F. Payan Substrate mimicry in the active center of the mammalian α-amylase: structural analysis of an enzyme-inhibitor complex Structure 4 1996 1441 1452 (Pubitemid 27050277)
5. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
6. V. Buonocore, M.G. De Biasi, P. Giardina, E. Poerio, and V. Silano Purification and properties of an α-amylase tetrameric inhibitor from wheat kernel Biochim. Biophys. Acta 831 1985 40 48
7. V. Buonocore, F. Gramenzi, W. Pace, T. Petrucci, E. Poerio, and V. Silano Interaction of wheat monomeric and dimeric protein inhibitors with α-amylase from yellow mealworm (Tenebrio molitor L: larva) Biochem. J. 187 1980 637 645
8. C. Chothia, and A.M. Lesk The relation between the divergence of sequence and structure in proteins EMBO J. 5 1986 823 826
9. D. Fontanini, A. Capocchi, V. Muccilli, F. Saviozzi, V. Cunsolo, R. Saletti, S. Foti, and L. Galleschi Dimeric inhibitors of human salivary α-amylase from emmer (Triticum dicoccon Schrank) seeds JAFC 55 2007 10452 10460
10. D. Fontanini, A. Capocchi, F. Saviozzi, and L. Galleschi Simplified electrophoretic assay for human salivary α -amylase inhibitor detection in cereal seed flours JAFC 55 2007 4334 4339 (Pubitemid 46932627)
11. O.L. Franco, D.J. Rigden, F.R. Melo, and M.F. Grossi-de-Sá Plant α-amylase inhibitors and their interaction with insect α-amylases. Structure, function and potential for crop protection Eur. J. Biochem. 269 2002 397 412 (Pubitemid 34127998)
12. O.L. Franco, D.J. Rigden, F.R. Melo, C. Bloch Jr., C.P. Silva, and M.F. Grossi-de-Sá Activity of wheat α-amylase inhibitors towards bruchid α-amylases and structural explanation of observed specificities Eur. J. Biochem. 267 2000 2166 2173 (Pubitemid 30220061)
13. F. García-Maroto, C. Marana, M. Mena, F. García-Olmedo, and P. Carbonero Cloning of cDNA and chromosomal location of genes encoding the three types of subunits of the wheat tetrameric inhibitor of insect α-amylases Plant Mol. Biol. 14 1990 845 853
14. F. García-Olmedo, G. Salcedo, R. Sánchez-Monge, L. Gomez, J. Rojo, and P. Carbonero Plant proteinaceous inhibitors of proteinases and α-amylases Oxf. Surv. Plant Mol. Cell Biol. 4 1987 275 334
15. A. Goldstein The mechanism of enzyme-inhibitor-substrate reactions J. Gen. Physiol. 27 1944 529 580
16. L. Gomez, R. Sánchez-Monge, F. García-Olmedo, and G. Salcedo Wheat tetrameric inhibitors of insect α-amylases: alloploid heterosis at the molecular level PNAS 86 1989 3242 3246
17. L. Gomez, R. Sánchez-Monge, C. Lopez-Otin, and G. Salcedo Wheat inhibitors of heterologous α-amylases. Characterization of major components from the monomeric class Plant Physiol. 96 1991 768 774 (Pubitemid 21914081)
18. T.A. Hall BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT Nucleic Acids Symp. Ser. 4 1999 95 98
19. J. Iulek, O.L. Franco, M. Silva, C.T. Slivinski, C. Bloch Jr., D.J. Rigden, and M.F. Grossi-de-Sá Purification, biochemical characterization and partial primary structure of a new α-amylase inhibitor from Secale cereale (rye) Int. J. Biochem. Cell Biol. 32 2000 1195 1204 (Pubitemid 32008307)
20. F. Kiefer, K. Arnold, M. Künzli, L. Bordoli, and T. Schwede The SWISS-MODEL repository and associated resources Nucleic Acids Res. 37 2009 D387 D392
21. E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797 PDBePISA. http://www.ebi.ac.uk/ msd-srv/prot-int/pistart.html (Pubitemid 47321791)
22. B.H. Kuntal, P. Aparoy, and P. Reddanna Easy Modeller: a graphical interface to MODELLER BMC Res. Notes 3 2010 226 230
23. U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
24. M.A. Larkin, G. Blackshields, N.P.R. Brown Chenna, P.A. McGettigan, H. McWilliam, F. Valentin, I.M. Wallace, A. Wilm, R. Lopez, J.D. Thompson, T.J. Gibson, and D.G. Higgins ClustalW and ClustalX version 2 Bioinformatics 23 2007 2947 2948
25. R.A. Laskowski, M.W. MacArthur, D.S. Moss, and J.M. Thornton PROCHECK: a program to check the stereochemical quality of protein structures J. Appl. Crystal. 26 1993 283 291
26. V. Nahoum, F. Farisei, V. Le-Berre-Anton, M.P. Egloff, P. Rouge, F. Poerio, and F. Payan A plant-seed inhibitor of two classes of α-amylases: X-ray analysis of Tenebrio molitor larvae α-amylase in complex with the bean Phaseolus vulgaris inhibitor Acta Crystallogr. D55 1999 360 362 (Pubitemid 29053858)
27. V. Nahoum, G. Roux, V. Anton, P. Rouge, H. Puigserver, H. Bischoff, B. Henrissat, and F. Payan Crystal structures of human pancreatic α-amylase in complex with carbohydrate and proteinaceous inhibitors Biochem. J. 346 2000 201 208 (Pubitemid 30113838)
28. Y. Oda, T. Matsunaga, K. Fukuyama, T. Miyazaki, and T. Morimoto Tertiary and quaternary structures of 0.19 α-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 Å resolution Biochemistry 36 1997 13503 13511 (Pubitemid 27481596)
29. F. Payan Structural basis for the inhibition of mammalian and insect α-amylases by plant protein inhibitors Biochim. Biophys. Acta 1696 2004 171 180 (Pubitemid 38199847)
30. M.C. Peitsch Protein modeling by E-mail Bio/Technology 13 1995 658 660
31. E.F. Pettersen, T.D. Goddard, C.C. Huang, G.S. Couch, D.M. Greenblatt, E.C. Meng, and T.E. Ferrin UCSF Chimera-a visualization system for exploratory research and analysis J. Comput. Chem. 25 2004 1605 1612 http://www.cgl.ucsf. edu/chimera
32. U. Pieper, B.M. Webb, D.T. Barkan, D. Schneidman-Duhovny, A. Schlessinger, H. Braberg, Z. Yang, E.C. Meng, E.F. Pettersen, C.C. Huang, R.S. Datta, P. Sampathkumar, M.S. Madhusudhan, K. Sjölander, T.E. Ferrin, S.K. Burley, and A. Sali MODBASE, a database of annotated comparative protein structure models and associated resources Nucleic Acids Res. 37 2009 D347 D354
33. G. Salcedo, R. Sánchez-Monge, G. García-Casado, A. Amentia, L. Gomez, and D. Barber The cereal α-amylase/trypsin inhibitor family associated with bakers' asthma and food allergy E.N.C. Mills, P.R. Shewry, Plant Food Allergens 2004 Blackwell Publishing Company Oxford 70 86
34. A. Šali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815 (Pubitemid 24007801)
35. R. Sánchez-Monge, L. Gomez, D. Barber, C. Lopez-Otin, A. Armentia, and G. Salcedo Wheat and barley allergens associated with baker's asthma Biochem. J. 281 1992 401 405
36. R. Sánchez-Monge, L. Gomez, F. García-Olmedo, and G. Salcedo New dimeric inhibitor of heterologous α-amylases encoded by a duplicated gene in the short arm of chromosome 3B of wheat (Triticum aestivum L.) Eur. J. Biochem. 183 1989 37 40
37. R. Sánchez-Monge, L. Gomez, F. García-Olmedo, and G.A. Salcedo Tetrameric inhibitor of insect amylase from barley FEBS Lett. 207 1986 105 107
38. A. Shevchenko, M. Wilm, O. Vorm, and M. Mann Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels Anal. Chem. 68 1996 850 858
39. V. Silano, M. Furia, L. Gianfreda, A. Macri, R. Palescandolo, A. Rab, V. Scardi, E. Stella, and F. Valfre Inhibition of amylases from different origins by albumins from the wheat kernel Biochim. Biophys. Acta 391 1975 170 178
40. S. Strobl, K. Maskos, G. Wiegand, R. Hubert, F.X. Gomis-Ruth, and R. Glockshuber 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 2004 911 921
41. A. Tovchigrecko, and I.A. Vakser GRAMM-X public web server for protein-protein docking Nucleic Acids Res. 34 2006 W310 314
42. R.M. Zacharius, T.E. Zell, J.H. Morrison, and J.J. Woodlock Glycoprotein staining following electrophoresis on acrylamide gels Anal. Biochem. 30 1969 148 152
43. G. Zoccatelli, C. Dalla Pellegrina, S. Mosconi, M. Consolini, G. Veneri, R. Chignola, A. Peruffo, and C. Rizzi Full-fledged proteomic analysis of bioactive wheat amylase inhibitors by a 3-D analytical technique: identification of a new heterodimeric aggregation states Electrophoresis 28 2007 460 466