메뉴 건너뛰기




Volumn 57, Issue , 2012, Pages 45-53

Isolation and characterization of novel variants of BBI coding genes from the legume Lathyrus sativus

Author keywords

Bowman Birk isoforms; Comparative modeling; Grass pea; Inhibitory properties; Proteolytic enzymes; Reactive site; Recombinant proteins

Indexed keywords

BOWMAN BIRK INHIBITOR; VEGETABLE PROTEIN;

EID: 84861829400     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2012.05.001     Document Type: Article
Times cited : (11)

References (41)
  • 1
    • 0034086003 scopus 로고    scopus 로고
    • Characterization of potato proteinase inhibitor II reactive site mutants
    • Beekwilder J., Schipper B., Bakker P., Bosch D., Jongsma M. Characterization of potato proteinase inhibitor II reactive site mutants. Eur. J. Biochem. 2000, 267:1975-1984.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1975-1984
    • Beekwilder, J.1    Schipper, B.2    Bakker, P.3    Bosch, D.4    Jongsma, M.5
  • 3
    • 0022017412 scopus 로고
    • The Bowman-Birk inhibitor. Trypsin-and chymotrypsin-inhibitor from soybeans
    • Birk Y. The Bowman-Birk inhibitor. Trypsin-and chymotrypsin-inhibitor from soybeans. Int. J. Pept. Prot. Res. 1985, 25:113-131.
    • (1985) Int. J. Pept. Prot. Res. , vol.25 , pp. 113-131
    • Birk, Y.1
  • 4
    • 74849134012 scopus 로고    scopus 로고
    • Bowman-Birk inhibitors in lentil: heterologous expression, functional characterisation and anti-proliferative properties in human colon cancer cells
    • Caccialupi P., Ceci L.R., Siciliano R.A., Pignone D., Clemente A., Sonnante G. Bowman-Birk inhibitors in lentil: heterologous expression, functional characterisation and anti-proliferative properties in human colon cancer cells. Food Chem. 2010, 120:1058-1066.
    • (2010) Food Chem. , vol.120 , pp. 1058-1066
    • Caccialupi, P.1    Ceci, L.R.2    Siciliano, R.A.3    Pignone, D.4    Clemente, A.5    Sonnante, G.6
  • 5
    • 0019611431 scopus 로고
    • Detection and partial characterization of subtilism inhibitors in legume seeds by isoelectric focusing
    • Chavan J.K., Hejgaard J. Detection and partial characterization of subtilism inhibitors in legume seeds by isoelectric focusing. J. Sci. Food Agr. 1981, 32:857-862.
    • (1981) J. Sci. Food Agr. , vol.32 , pp. 857-862
    • Chavan, J.K.1    Hejgaard, J.2
  • 6
    • 33745077071 scopus 로고    scopus 로고
    • Biological significance of polymorphism in legume protease inhibitors from the Bowman-Birk family
    • Clemente A., Domoney C. Biological significance of polymorphism in legume protease inhibitors from the Bowman-Birk family. Curr. Protein Pept. Sci. 2006, 7:201-216.
    • (2006) Curr. Protein Pept. Sci. , vol.7 , pp. 201-216
    • Clemente, A.1    Domoney, C.2
  • 7
    • 77649316496 scopus 로고    scopus 로고
    • The cytotoxic effect of Bowman-Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases
    • Clemente A., Moreno F.J., Marín-Manzano M.C., Jiménez E., Domoney C. The cytotoxic effect of Bowman-Birk isoinhibitors, IBB1 and IBBD2, from soybean (Glycine max) on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases. Mol. Nutr. Food Res. 2010, 54:396-405.
    • (2010) Mol. Nutr. Food Res. , vol.54 , pp. 396-405
    • Clemente, A.1    Moreno, F.J.2    Marín-Manzano, M.C.3    Jiménez, E.4    Domoney, C.5
  • 8
    • 79960338571 scopus 로고    scopus 로고
    • Bowman-Birk inhibitors from legumes and human gastrointestinal health: current status and perspective
    • Clemente A., Sonnante G., Domoney C. Bowman-Birk inhibitors from legumes and human gastrointestinal health: current status and perspective. Curr. Protein Pept. Sci. 2011, 12:358-373.
    • (2011) Curr. Protein Pept. Sci. , vol.12 , pp. 358-373
    • Clemente, A.1    Sonnante, G.2    Domoney, C.3
  • 9
    • 1842856051 scopus 로고    scopus 로고
    • Purification and characterization of proteinase inhibitors from wild soja (Glycine soja) seeds
    • Deshimaru M., Hanamoto R., Kusano C., Yoshimi S., Terada S. Purification and characterization of proteinase inhibitors from wild soja (Glycine soja) seeds. Biosci. Biotechnol. Biochem. 2002, 66:1897-1903.
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 1897-1903
    • Deshimaru, M.1    Hanamoto, R.2    Kusano, C.3    Yoshimi, S.4    Terada, S.5
  • 10
    • 0028893996 scopus 로고
    • Multiple isoforms of Pisum trypsin inhibitors result from modification of two primary gene products
    • Domoney C., Welham T., Sidebottom C., Firmin J.L. Multiple isoforms of Pisum trypsin inhibitors result from modification of two primary gene products. FEBS Lett. 1995, 360:15-20.
    • (1995) FEBS Lett. , vol.360 , pp. 15-20
    • Domoney, C.1    Welham, T.2    Sidebottom, C.3    Firmin, J.L.4
  • 11
    • 0036007729 scopus 로고    scopus 로고
    • Turner three classes of proteinase inhibitor gene have distinct but overlapping patterns of expression in Pisum sativum plants
    • Domoney C., Welham T., Ellis P.N., Mozzanega L. Turner three classes of proteinase inhibitor gene have distinct but overlapping patterns of expression in Pisum sativum plants. Plant Mol. Biol. 2002, 48:319-329.
    • (2002) Plant Mol. Biol. , vol.48 , pp. 319-329
    • Domoney, C.1    Welham, T.2    Ellis, P.N.3    Mozzanega, L.4
  • 12
    • 56749154097 scopus 로고    scopus 로고
    • Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration
    • Ekici O.D., Paetzel M., Dalbey R.E. Unconventional serine proteases: variations on the catalytic Ser/His/Asp triad configuration. Protein Sci. 2008, 17:2023-2037.
    • (2008) Protein Sci. , vol.17 , pp. 2023-2037
    • Ekici, O.D.1    Paetzel, M.2    Dalbey, R.E.3
  • 13
    • 0033217716 scopus 로고    scopus 로고
    • Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type
    • Gladysheva I.P., Zamolodchikova T.S., Sokolova E.A., Larionova N.I. Interaction between duodenase, a proteinase with dual specificity, and soybean inhibitors of Bowman-Birk and Kunitz type. Biochemistry (Mosc) 1999, 64:1244-1249.
    • (1999) Biochemistry (Mosc) , vol.64 , pp. 1244-1249
    • Gladysheva, I.P.1    Zamolodchikova, T.S.2    Sokolova, E.A.3    Larionova, N.I.4
  • 14
    • 0031698348 scopus 로고    scopus 로고
    • The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor
    • Helland R., Leiros I., Berglund G.I., Willassen N.P., Smalas A.O. The crystal structure of anionic salmon trypsin in complex with bovine pancreatic trypsin inhibitor. Eur. J. Biochem. 1998, 256:317-324.
    • (1998) Eur. J. Biochem. , vol.256 , pp. 317-324
    • Helland, R.1    Leiros, I.2    Berglund, G.I.3    Willassen, N.P.4    Smalas, A.O.5
  • 15
    • 0027220491 scopus 로고
    • Quantitative determination of serine proteinase inhibitor activity using a Radial diffusion assay
    • Jongsma M.A., Bakker P.L., Stiekema W.J. Quantitative determination of serine proteinase inhibitor activity using a Radial diffusion assay. Anal. Biochem. 1993, 212:79-84.
    • (1993) Anal. Biochem. , vol.212 , pp. 79-84
    • Jongsma, M.A.1    Bakker, P.L.2    Stiekema, W.J.3
  • 16
    • 0031741056 scopus 로고    scopus 로고
    • The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent
    • Kennedy A.R. The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent. Am. J. Clin. Nutr. 1998, 68:1406S-1412S.
    • (1998) Am. J. Clin. Nutr. , vol.68
    • Kennedy, A.R.1
  • 17
    • 3142780686 scopus 로고    scopus 로고
    • Molecular mechanism of dimerization of Bowman-Birk inhibitors. Pivotal role of ASP76 in the dimerzation
    • Kumar P., Rao A.G., Hariharaputran S., Chandra N., Gowda L.R. Molecular mechanism of dimerization of Bowman-Birk inhibitors. Pivotal role of ASP76 in the dimerzation. J. Biol. Chem. 2004, 279:30425-30432.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30425-30432
    • Kumar, P.1    Rao, A.G.2    Hariharaputran, S.3    Chandra, N.4    Gowda, L.R.5
  • 18
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski M., Kato I. Protein inhibitors of proteinases. Annu. Rev. Biochem. 1980, 49:593-626.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 19
    • 0001483373 scopus 로고    scopus 로고
    • Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds
    • Li de la Sierra I., Quillien L., Flecker P., Gueguen J., Brunie S. Dimeric crystal structure of a Bowman-Birk protease inhibitor from pea seeds. Mol. Biol. 1999, 285:1195-1207.
    • (1999) Mol. Biol. , vol.285 , pp. 1195-1207
    • Li de la Sierra, I.1    Quillien, L.2    Flecker, P.3    Gueguen, J.4    Brunie, S.5
  • 21
    • 0344655676 scopus 로고    scopus 로고
    • High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds
    • Luckett S. High-resolution structure of a potent, cyclic proteinase inhibitor from sunflower seeds. J. Mol. Biol. 1999, 290:525-533.
    • (1999) J. Mol. Biol. , vol.290 , pp. 525-533
    • Luckett, S.1
  • 23
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona J.J., Craik C.S. Structural basis of substrate specificity in the serine proteases. Protein Sci. 1995, 4:337-360.
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 24
    • 1942510393 scopus 로고    scopus 로고
    • Polymorphism of trypsin and chymotrypsin binding loops in Bowmann-Birk inhibitors from common bean
    • Piergiovanni A.R., Galasso I. Polymorphism of trypsin and chymotrypsin binding loops in Bowmann-Birk inhibitors from common bean. Plant Sci. 2004, 166:1525-1531.
    • (2004) Plant Sci. , vol.166 , pp. 1525-1531
    • Piergiovanni, A.R.1    Galasso, I.2
  • 25
    • 77955096900 scopus 로고    scopus 로고
    • Computational approaches for protein function prediction: a combined strategy from multiple sequence alignment to molecular docking-based virtual screening
    • Pierri C.L., Parisi G., Porcelli V. Computational approaches for protein function prediction: a combined strategy from multiple sequence alignment to molecular docking-based virtual screening. Biochim. Biophys. Acta 2010, 1804:1695-1712.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 1695-1712
    • Pierri, C.L.1    Parisi, G.2    Porcelli, V.3
  • 26
    • 27144523783 scopus 로고    scopus 로고
    • The catalytic triad of serine peptidases
    • Polgár L. The catalytic triad of serine peptidases. Cell. Mol. Life Sci. 2005, 62:2161-2172.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2161-2172
    • Polgár, L.1
  • 28
    • 23844454955 scopus 로고    scopus 로고
    • Structural features and molecular evolution of Bowman-Birk protease inhibitors and their potential application
    • Qi R.F., Song Z.W., Chi C.W. Structural features and molecular evolution of Bowman-Birk protease inhibitors and their potential application. Acta Biochim. Biophys. Sin. (Shanghai) 2005, 37:283-292.
    • (2005) Acta Biochim. Biophys. Sin. (Shanghai) , vol.37 , pp. 283-292
    • Qi, R.F.1    Song, Z.W.2    Chi, C.W.3
  • 29
    • 33747399034 scopus 로고    scopus 로고
    • Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens culinaris, L) seeds
    • Ragg E.M., Galbusera V., Scarafoni A., Negri A., Tedeschi G., Consonni A., Sessa F., Duranti M. Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens culinaris, L) seeds. FEBS J. 2006, 273:4024-4239.
    • (2006) FEBS J. , vol.273 , pp. 4024-4239
    • Ragg, E.M.1    Galbusera, V.2    Scarafoni, A.3    Negri, A.4    Tedeschi, G.5    Consonni, A.6    Sessa, F.7    Duranti, M.8
  • 30
    • 77955771956 scopus 로고    scopus 로고
    • New properties of the soybean trypsin inhibitor: inhibition of human neutrophil elastase and its effect on acute pulmonary injury
    • Ribeiro J.K.C., Cunha D.D.S., Fook J.M.S.L.L., Sales M.P. New properties of the soybean trypsin inhibitor: inhibition of human neutrophil elastase and its effect on acute pulmonary injury. Eur. J. Pharmacol. 2010, 644:238-244.
    • (2010) Eur. J. Pharmacol. , vol.644 , pp. 238-244
    • Ribeiro, J.K.C.1    Cunha, D.D.S.2    Fook, J.M.S.L.L.3    Sales, M.P.4
  • 31
    • 79960360560 scopus 로고    scopus 로고
    • A Bowman-Birk inhibitor with anti-elastase activity from Lathyrus sativus L. seeds
    • Rocco M., Malorni L., Chambery A., Poerio E., Parente A., Di Maro A. A Bowman-Birk inhibitor with anti-elastase activity from Lathyrus sativus L. seeds. Mol. Biosyst. 2011, 7:2500-2507.
    • (2011) Mol. Biosyst. , vol.7 , pp. 2500-2507
    • Rocco, M.1    Malorni, L.2    Chambery, A.3    Poerio, E.4    Parente, A.5    Di Maro, A.6
  • 32
    • 0000180578 scopus 로고
    • Proteinase inhibitors in plants: genes for improving defenses against insects and pathogens
    • Ryan C.A. Proteinase inhibitors in plants: genes for improving defenses against insects and pathogens. Annu. Rev. Phytopathol. 1990, 28:425-429.
    • (1990) Annu. Rev. Phytopathol. , vol.28 , pp. 425-429
    • Ryan, C.A.1
  • 33
    • 0023375195 scopus 로고
    • The neighbor-joining method: a new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 1987, 4:406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 34
    • 44549085952 scopus 로고    scopus 로고
    • Identification and characterization of a Bowman-Birk inhibitor active towards trypsin but not chymotrypsin in Lupinus albus seeds
    • Scarafoni A., Consonni A., Galbusera V., Negri A., Tedeschi G., Rasmussen P., Magni C., Duranti M. Identification and characterization of a Bowman-Birk inhibitor active towards trypsin but not chymotrypsin in Lupinus albus seeds. Phytochemistry 2008, 69:1820-1825.
    • (2008) Phytochemistry , vol.69 , pp. 1820-1825
    • Scarafoni, A.1    Consonni, A.2    Galbusera, V.3    Negri, A.4    Tedeschi, G.5    Rasmussen, P.6    Magni, C.7    Duranti, M.8
  • 35
    • 16244373035 scopus 로고    scopus 로고
    • Bowman-Birk inhibitors in lens: identification and characterization of two paralogous gene classes in cultivated lentil and wild relatives
    • Sonnante G., De Paolis A., Pignone D. Bowman-Birk inhibitors in lens: identification and characterization of two paralogous gene classes in cultivated lentil and wild relatives. Theor. Appl. Genet. 2005, 110:596-604.
    • (2005) Theor. Appl. Genet. , vol.110 , pp. 596-604
    • Sonnante, G.1    De Paolis, A.2    Pignone, D.3
  • 37
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K., Peterson D., Peterson N., Stecher G., Nei M., Kumar S. MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol. Biol. Evol. 2011, 28:2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 38
    • 33747840389 scopus 로고    scopus 로고
    • GRAMM-X public web server for protein-protein docking
    • Tovchigrechko A., Vakser I. GRAMM-X public web server for protein-protein docking. Nucleic Acids Res. 2006, 34:W310-W314.
    • (2006) Nucleic Acids Res. , vol.34
    • Tovchigrechko, A.1    Vakser, I.2
  • 39
    • 0033963158 scopus 로고    scopus 로고
    • Characterization of recombinant mustard trypsin inhibitor 2 (MTI2) expressed in Pichia pastoris
    • Volpicella M., Schipper A., Jongsma M.A., Spoto N., Gallerani R., Ceci L.R. Characterization of recombinant mustard trypsin inhibitor 2 (MTI2) expressed in Pichia pastoris. FEBS Lett. 2000, 468:137-141.
    • (2000) FEBS Lett. , vol.468 , pp. 137-141
    • Volpicella, M.1    Schipper, A.2    Jongsma, M.A.3    Spoto, N.4    Gallerani, R.5    Ceci, L.R.6
  • 41
    • 0032957934 scopus 로고    scopus 로고
    • Bowman-Birk inhibitor concentrate reduces colon inflammation in mice with dextran sulfate sodium-induced ulcerative colitis
    • Ware J.H., Wan X.S., Newberne P., Kennedy A.R. Bowman-Birk inhibitor concentrate reduces colon inflammation in mice with dextran sulfate sodium-induced ulcerative colitis. Dig. Dis. Sci. 1999, 44:986-990.
    • (1999) Dig. Dis. Sci. , vol.44 , pp. 986-990
    • Ware, J.H.1    Wan, X.S.2    Newberne, P.3    Kennedy, A.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.