메뉴 건너뛰기




Volumn 91, Issue 9, 2009, Pages 1112-1122

Redesigning the reactive site loop of the wheat subtilisin/chymotrypsin inhibitor (WSCI) by site-directed mutagenesis. A protein-protein interaction study by affinity chromatography and molecular modeling

Author keywords

E I complexes; ESI Q TOF mass spectrometry; Time course proteolysis; WSCI mutants

Indexed keywords

ARGININE; ASPARTIC ACID; CHYMOTRYPSIN; CHYMOTRYPSIN INHIBITOR; GLYCINE; HYDROGEN; METHIONINE; PHENYLALANINE; SERINE; SUBTILISIN; THREONINE; TYROSINE; VALINE;

EID: 67849133188     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.05.010     Document Type: Article
Times cited : (3)

References (27)
  • 1
    • 0037300857 scopus 로고    scopus 로고
    • Primary structure and reactive site of a novel wheat proteinase inhibitor of subtilisin and chymotrypsin
    • Poerio E., Di Gennaro S., Di Maro A., Farisei F., Ferranti P., and Parente A. Primary structure and reactive site of a novel wheat proteinase inhibitor of subtilisin and chymotrypsin. Biol. Chem. 384 (2003) 295-304
    • (2003) Biol. Chem. , vol.384 , pp. 295-304
    • Poerio, E.1    Di Gennaro, S.2    Di Maro, A.3    Farisei, F.4    Ferranti, P.5    Parente, A.6
  • 2
    • 28044470978 scopus 로고    scopus 로고
    • Evolutionary mechanisms acting on proteinase inhibitor variability
    • Christeller J.T. Evolutionary mechanisms acting on proteinase inhibitor variability. FEBS J. 272 (2005) 5710-5722
    • (2005) FEBS J. , vol.272 , pp. 5710-5722
    • Christeller, J.T.1
  • 3
  • 4
    • 0342445397 scopus 로고    scopus 로고
    • What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?
    • Laskowski M., and Qasim M.A. What can the structures of enzyme-inhibitor complexes tell us about the structures of enzyme substrate complexes?. Biochim. Biophys. Acta 1477 (2000) 324-337
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 324-337
    • Laskowski, M.1    Qasim, M.A.2
  • 5
    • 33746192088 scopus 로고    scopus 로고
    • Modeling the 3D structure of wheat subtilisin/chymotrypsin inhibitor (WSCI). Probing the reactive site with two susceptible proteinases by time-course analysis and molecular dynamics simulations
    • Facchiano A.M., Costantini S., Di Maro A., Panichi D., Chambery A., Parente A., Di Gennaro S., and Poerio E. Modeling the 3D structure of wheat subtilisin/chymotrypsin inhibitor (WSCI). Probing the reactive site with two susceptible proteinases by time-course analysis and molecular dynamics simulations. Biol. Chem. 387 (2006) 931-940
    • (2006) Biol. Chem. , vol.387 , pp. 931-940
    • Facchiano, A.M.1    Costantini, S.2    Di Maro, A.3    Panichi, D.4    Chambery, A.5    Parente, A.6    Di Gennaro, S.7    Poerio, E.8
  • 6
    • 33745651393 scopus 로고    scopus 로고
    • Genetic engineering of wheat-current challenges and opportunities
    • Bhalla P.L. Genetic engineering of wheat-current challenges and opportunities. Trends Biotechnol. 24 (2006) 305-311
    • (2006) Trends Biotechnol. , vol.24 , pp. 305-311
    • Bhalla, P.L.1
  • 7
    • 0000711035 scopus 로고    scopus 로고
    • Seed storage proteins and approaches for improvement of their nutritional quality by genetic engineering
    • Mandal S., and Mandal R.K. Seed storage proteins and approaches for improvement of their nutritional quality by genetic engineering. Curr. Sci. 79 (2000) 576-589
    • (2000) Curr. Sci. , vol.79 , pp. 576-589
    • Mandal, S.1    Mandal, R.K.2
  • 8
    • 12544257889 scopus 로고    scopus 로고
    • Wheat transformation: current technology and applications to grain development and composition
    • Jones H.D. Wheat transformation: current technology and applications to grain development and composition. J. Cereal Sci. 41 (2005) 137-147
    • (2005) J. Cereal Sci. , vol.41 , pp. 137-147
    • Jones, H.D.1
  • 9
    • 0031149258 scopus 로고    scopus 로고
    • Expression of de novo high-lysine alpha-helical coiled-coil proteins may significantly increase the accumulated levels of lysine in mature seeds of transgenic tobacco plants
    • Keeler S.J., Maloney C.L., Webber P.Y., Patterson C., Hirata L.T., Falco S.C., and Rice J.A. Expression of de novo high-lysine alpha-helical coiled-coil proteins may significantly increase the accumulated levels of lysine in mature seeds of transgenic tobacco plants. Plant Mol. Biol. 34 (1997) 15-29
    • (1997) Plant Mol. Biol. , vol.34 , pp. 15-29
    • Keeler, S.J.1    Maloney, C.L.2    Webber, P.Y.3    Patterson, C.4    Hirata, L.T.5    Falco, S.C.6    Rice, J.A.7
  • 10
    • 0030844328 scopus 로고    scopus 로고
    • Enhanced methionine levels and increased nutritive value of seeds of transgenic lupins (Lupinus angustifolius L.) expressing a sunflower seed albumin gene
    • Molvig L., Tabe L.M., Eggum B.O., Moore A.E., Craig S., Spencer D., and Higgins T.J. Enhanced methionine levels and increased nutritive value of seeds of transgenic lupins (Lupinus angustifolius L.) expressing a sunflower seed albumin gene. Proc. Natl. Acad. Sci. U.S.A. 94 (1997) 8393-8398
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 8393-8398
    • Molvig, L.1    Tabe, L.M.2    Eggum, B.O.3    Moore, A.E.4    Craig, S.5    Spencer, D.6    Higgins, T.J.7
  • 12
    • 33748663559 scopus 로고    scopus 로고
    • Particle-bombardment-mediated co-transformation of maize with a lysine rich protein gene (sb401) from potato
    • Wang D., Zhao Q., Zhu D., Ao G., and Yu J. Particle-bombardment-mediated co-transformation of maize with a lysine rich protein gene (sb401) from potato. Euphytica 150 (2005) 75-85
    • (2005) Euphytica , vol.150 , pp. 75-85
    • Wang, D.1    Zhao, Q.2    Zhu, D.3    Ao, G.4    Yu, J.5
  • 14
    • 30344449131 scopus 로고    scopus 로고
    • Seed-specific expression of the lysine-rich protein gene sb401 significantly increases both lysine and total protein content in maize seeds
    • Yu J., Peng P., Zhang X., Zhao Q., Zhu D., Sun X., Liu J., and Ao G. Seed-specific expression of the lysine-rich protein gene sb401 significantly increases both lysine and total protein content in maize seeds. Food Nutr. Bull. 26 (2005) 427-431
    • (2005) Food Nutr. Bull. , vol.26 , pp. 427-431
    • Yu, J.1    Peng, P.2    Zhang, X.3    Zhao, Q.4    Zhu, D.5    Sun, X.6    Liu, J.7    Ao, G.8
  • 15
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter I., and Berger A. On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27 (1967) 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 16
    • 25144446868 scopus 로고    scopus 로고
    • cDNA cloning and heterologous expression of a wheat proteinase inhibitor of subtilisin and chymotrypsin (WSCI) that interferes with digestive enzymes of insect pests
    • Di Gennaro S., Ficca A.G., Panichi D., and Poerio E. cDNA cloning and heterologous expression of a wheat proteinase inhibitor of subtilisin and chymotrypsin (WSCI) that interferes with digestive enzymes of insect pests. Biol. Chem. 386 (2005) 383-389
    • (2005) Biol. Chem. , vol.386 , pp. 383-389
    • Di Gennaro, S.1    Ficca, A.G.2    Panichi, D.3    Poerio, E.4
  • 17
    • 0016700753 scopus 로고
    • Tight-binding inhibitors-I. Kinetic behavior
    • Cha S. Tight-binding inhibitors-I. Kinetic behavior. Biochem. Pharmacol. 24 (1975) 2177-2185
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 2177-2185
    • Cha, S.1
  • 18
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H., and von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 19
    • 0035137983 scopus 로고    scopus 로고
    • Reliable sequence determination of ribosome-inactivating proteins by combining electrospray mass spectrometry and Edman degradation
    • Di Maro A., Ferranti P., Mastronicola M., Polito L., Bolognesi A., Stirpe F., Malorni A., and Parente A. Reliable sequence determination of ribosome-inactivating proteins by combining electrospray mass spectrometry and Edman degradation. J. Mass Spectrom. 36 (2001) 38-46
    • (2001) J. Mass Spectrom. , vol.36 , pp. 38-46
    • Di Maro, A.1    Ferranti, P.2    Mastronicola, M.3    Polito, L.4    Bolognesi, A.5    Stirpe, F.6    Malorni, A.7    Parente, A.8
  • 21
    • 0023729499 scopus 로고
    • Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo
    • McPhalen C.A., and James M.N. Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo. Biochemistry 27 (1988) 6582-6598
    • (1988) Biochemistry , vol.27 , pp. 6582-6598
    • McPhalen, C.A.1    James, M.N.2
  • 22
    • 15244344453 scopus 로고    scopus 로고
    • Modelling of HLA-DQ2 and its interaction with gluten peptides to explain molecular recognition in celiac disease
    • Costantini S., Rossi M., Colonna G., and Facchiano A.M. Modelling of HLA-DQ2 and its interaction with gluten peptides to explain molecular recognition in celiac disease. J. Mol. Graph Model 23 (2005) 419-431
    • (2005) J. Mol. Graph Model , vol.23 , pp. 419-431
    • Costantini, S.1    Rossi, M.2    Colonna, G.3    Facchiano, A.M.4
  • 23
    • 34248570351 scopus 로고    scopus 로고
    • Simulation of conformational changes occurring when a protein interacts with its receptor
    • Costantini S., Colonna G., and Facchiano A.M. Simulation of conformational changes occurring when a protein interacts with its receptor. Comput. Biol. Chem. 31 (2007) 196-206
    • (2007) Comput. Biol. Chem. , vol.31 , pp. 196-206
    • Costantini, S.1    Colonna, G.2    Facchiano, A.M.3
  • 26
    • 0033009569 scopus 로고    scopus 로고
    • Analysis of protein-protein interactions by mutagenesis: direct versus indirect effects
    • Otzen D.E., and Fersht A.R. Analysis of protein-protein interactions by mutagenesis: direct versus indirect effects. Protein Eng. 12 (1999) 41-45
    • (1999) Protein Eng. , vol.12 , pp. 41-45
    • Otzen, D.E.1    Fersht, A.R.2
  • 27
    • 0023652256 scopus 로고
    • Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds
    • McPhalen C.A., and James M.N. Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds. Biochemistry 26 (1987) 261-269
    • (1987) Biochemistry , vol.26 , pp. 261-269
    • McPhalen, C.A.1    James, M.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.