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Volumn 93, Issue 2, 2011, Pages 321-330

A new tyrosine-specific chymotrypsin-like and angiotensin-degrading serine proteinase from Vipera lebetina snake venom

Author keywords

Angiotensin I and II; cDNA cloning; Chymotrypsin like serine protease; LC MS MS; MALDI TOF MS; Snake venom; Vipera lebetina

Indexed keywords

CHYMOTRYPSIN; COMPLEMENTARY DNA; SERINE PROTEINASE; SNAKE VENOM; UNCLASSIFIED DRUG; VIPERA LEBETINA CHYMOTRYPSIN LIKE PROTEOLYTIC ENZYME;

EID: 78651286582     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.10.004     Document Type: Article
Times cited : (17)

References (45)
  • 1
    • 0033741151 scopus 로고    scopus 로고
    • Snake venom proteins acting on hemostasis
    • S. Braud, C. Bon, and A. Wisner Snake venom proteins acting on hemostasis Biochimie 82 2000 851 859 Review
    • (2000) Biochimie , vol.82 , pp. 851-859
    • Braud, S.1    Bon, C.2    Wisner, A.3
  • 2
    • 0034615556 scopus 로고    scopus 로고
    • Snake venom proteases affecting hemostasis and thrombosis
    • T. Matsui, Y. Fujimura, and K. Titani Snake venom proteases affecting hemostasis and thrombosis Biochim. Biophys. Acta 1477 2000 146 156 Review
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 146-156
    • Matsui, T.1    Fujimura, Y.2    Titani, K.3
  • 3
    • 33646780927 scopus 로고    scopus 로고
    • Serine proteases affecting blood coagulation and fibrinolysis from snake venoms
    • R.M. Kini Serine proteases affecting blood coagulation and fibrinolysis from snake venoms Pathophysiol. Haemost. Thromb. 34 2005 200 204 Review
    • (2005) Pathophysiol. Haemost. Thromb. , vol.34 , pp. 200-204
    • Kini, R.M.1
  • 4
    • 19544377334 scopus 로고    scopus 로고
    • The intriguing world of prothrombin activators from snake venom
    • R.M. Kini The intriguing world of prothrombin activators from snake venom Toxicon 45 2005 1133 1145 Review
    • (2005) Toxicon , vol.45 , pp. 1133-1145
    • Kini, R.M.1
  • 5
    • 33746885464 scopus 로고    scopus 로고
    • Anticoagulant proteins from snake venoms: Structure, function and mechanism
    • R.M. Kini Anticoagulant proteins from snake venoms: structure, function and mechanism Biochem. J. 397 2006 377 387
    • (2006) Biochem. J. , vol.397 , pp. 377-387
    • Kini, R.M.1
  • 6
    • 19544367786 scopus 로고    scopus 로고
    • Snake venom fibrin(ogen)olytic enzymes
    • S. Swenson, and F.S. Markland Jr. Snake venom fibrin(ogen)olytic enzymes Toxicon 45 2005 1021 1039
    • (2005) Toxicon , vol.45 , pp. 1021-1039
    • Swenson, S.1    Markland Jr., F.S.2
  • 7
    • 27744533208 scopus 로고    scopus 로고
    • Snake venomics: Comparative analysis of the venom proteomes of the Tunisian snakes Cerastes cerastes, Cerastes vipera and Macrovipera lebetina
    • A. Bazaa, N. Marrakchi, M. El Ayeb, L. Sanz, and J.J. Calvete Snake venomics: comparative analysis of the venom proteomes of the Tunisian snakes Cerastes cerastes, Cerastes vipera and Macrovipera lebetina Proteomics 5 2005 4223 4235
    • (2005) Proteomics , vol.5 , pp. 4223-4235
    • Bazaa, A.1    Marrakchi, N.2    El Ayeb, M.3    Sanz, L.4    Calvete, J.J.5
  • 8
    • 33846625097 scopus 로고    scopus 로고
    • Snake venomics of Bitis gabonica gabonica. Protein family composition, subunit organization of venom toxins, and characterization of dimeric disintegrins bitisgabonin-1 and bitisgabonin-2
    • J.J. Calvete, C. Marcinkiewicz, and L. Sanz Snake venomics of Bitis gabonica gabonica. Protein family composition, subunit organization of venom toxins, and characterization of dimeric disintegrins bitisgabonin-1 and bitisgabonin-2 J. Proteome Res. 6 2007 326 336
    • (2007) J. Proteome Res. , vol.6 , pp. 326-336
    • Calvete, J.J.1    Marcinkiewicz, C.2    Sanz, L.3
  • 9
    • 67049132403 scopus 로고    scopus 로고
    • Exploring the venom proteome of the western diamondback rattlesnake, Crotalus atrox, via snake venomics and combinatorial peptide ligand library approaches
    • J.J. Calvete, E. Fasoli, L. Sanz, E. Boschetti, and P.G. Righetti Exploring the venom proteome of the western diamondback rattlesnake, Crotalus atrox, via snake venomics and combinatorial peptide ligand library approaches J. Proteome Res. 8 2009 3055 3067
    • (2009) J. Proteome Res. , vol.8 , pp. 3055-3067
    • Calvete, J.J.1    Fasoli, E.2    Sanz, L.3    Boschetti, E.4    Righetti, P.G.5
  • 10
    • 19544382337 scopus 로고    scopus 로고
    • Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
    • J.W. Fox, and S.M. Serrano Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases Toxicon 45 2005 969 985
    • (2005) Toxicon , vol.45 , pp. 969-985
    • Fox, J.W.1    Serrano, S.M.2
  • 11
    • 19544394247 scopus 로고    scopus 로고
    • Snake venom serine proteinases: Sequence homology vs. substrate specificity, a paradox to be solved
    • S.M. Serrano, and R.C. Maroun Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved Toxicon 45 2005 1115 1132 Review
    • (2005) Toxicon , vol.45 , pp. 1115-1132
    • Serrano, S.M.1    Maroun, R.C.2
  • 13
    • 0032436007 scopus 로고    scopus 로고
    • Isolation, properties and N-terminal amino acid sequence of a factor v activator from Vipera lebetina (Levantine viper) snake venom
    • E. Siigur, M. Samel, K. Tõnismägi, J. Subbi, T. Reintamm, and J. Siigur Isolation, properties and N-terminal amino acid sequence of a factor V activator from Vipera lebetina (Levantine viper) snake venom Biochim. Biophy. Acta 1429 1998 239 248
    • (1998) Biochim. Biophy. Acta , vol.1429 , pp. 239-248
    • Siigur, E.1    Samel, M.2    Tõnismägi, K.3    Subbi, J.4    Reintamm, T.5    Siigur, J.6
  • 14
    • 0344500853 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of a cDNA for factor v activating enzyme, a coagulant protein from Vipera lebetina snake venom
    • E. Siigur, A. Aaspõllu, and J. Siigur Molecular cloning and sequence analysis of a cDNA for factor V activating enzyme, a coagulant protein from Vipera lebetina snake venom Biochem. Biophys. Res. Commun. 262 1999 328 332
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 328-332
    • Siigur, E.1    Aaspõllu, A.2    Siigur, J.3
  • 15
    • 0036027966 scopus 로고    scopus 로고
    • Biochemical characterization of fibrinogenolytic serine proteinases from Vipera lebetina snake venom
    • M. Samel, J. Subbi, J. Siigur, and E. Siigur Biochemical characterization of fibrinogenolytic serine proteinases from Vipera lebetina snake venom Toxicon 40 2002 51 54
    • (2002) Toxicon , vol.40 , pp. 51-54
    • Samel, M.1    Subbi, J.2    Siigur, J.3    Siigur, E.4
  • 16
    • 0013884969 scopus 로고
    • Proteolytic enzyme activities in a variety of snake venoms
    • A.T. Tu, A. Chua, and G.P. James Proteolytic enzyme activities in a variety of snake venoms Toxicol. Appl. Pharmacol. 8 1966 218 223
    • (1966) Toxicol. Appl. Pharmacol. , vol.8 , pp. 218-223
    • Tu, A.T.1    Chua, A.2    James, G.P.3
  • 17
    • 1542652441 scopus 로고
    • A spectrophotometric determination of trypsin and chymotrypsin
    • G.W. Schwert, and Y. Takenaka A spectrophotometric determination of trypsin and chymotrypsin Biochim. Biophys. Acta 16 1955 570 575
    • (1955) Biochim. Biophys. Acta , vol.16 , pp. 570-575
    • Schwert, G.W.1    Takenaka, Y.2
  • 18
    • 0032053249 scopus 로고    scopus 로고
    • Biochemical characterization of lebetase, a direct-acting fibrinolytic enzyme from Vipera lebetina snake venom
    • J. Siigur, M. Samel, K. Tõnismägi, J. Subbi, E. Siigur, and A.T. Tu Biochemical characterization of lebetase, a direct-acting fibrinolytic enzyme from Vipera lebetina snake venom Thromb. Res. 90 1998 39 49
    • (1998) Thromb. Res. , vol.90 , pp. 39-49
    • Siigur, J.1    Samel, M.2    Tõnismägi, K.3    Subbi, J.4    Siigur, E.5    Tu, A.T.6
  • 19
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating of fibrinolytic activity
    • T. Astrup, and S. Müllertz The fibrin plate method for estimating of fibrinolytic activity Archs. Biochem. Biophys. 40 1952 346 351
    • (1952) Archs. Biochem. Biophys. , vol.40 , pp. 346-351
    • Astrup, T.1    Müllertz, S.2
  • 20
    • 0034991822 scopus 로고    scopus 로고
    • Novel in vitro assays for assessing the haemorrhagic activity of snake venoms and for demonstration of venom metalloproteinase inhibitors
    • A. Bee, R.D.G. Theakston, R.A. Harrison, and S.D. Carter Novel in vitro assays for assessing the haemorrhagic activity of snake venoms and for demonstration of venom metalloproteinase inhibitors Toxicon 39 2001 1429 1434
    • (2001) Toxicon , vol.39 , pp. 1429-1434
    • Bee, A.1    Theakston, R.D.G.2    Harrison, R.A.3    Carter, S.D.4
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0015524317 scopus 로고
    • Isoelectric focusing of proteins in polyacrylamide gels
    • O. Vesterberg Isoelectric focusing of proteins in polyacrylamide gels Biochim. Biophys. Acta 257 1972 11 19
    • (1972) Biochim. Biophys. Acta , vol.257 , pp. 11-19
    • Vesterberg, O.1
  • 24
    • 0034801198 scopus 로고    scopus 로고
    • Use of matrix-assisted laser desorption/ionization time-of-flight mass mapping and nanospray liquid chromatography/electrospray ionization tandem mass spectrometry sequence tag analysis for high sensitivity identification of yeast proteins separated by two-dimensional gel electrophoresis
    • M. Poutanen, L. Salusjärvi, L. Ruohonen, M. Penttilä, and N. Kalkkinen Use of matrix-assisted laser desorption/ionization time-of-flight mass mapping and nanospray liquid chromatography/electrospray ionization tandem mass spectrometry sequence tag analysis for high sensitivity identification of yeast proteins separated by two-dimensional gel electrophoresis Rapid Commun. Mass Spectrom. 15 2001 1685 1692
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1685-1692
    • Poutanen, M.1    Salusjärvi, L.2    Ruohonen, L.3    Penttilä, M.4    Kalkkinen, N.5
  • 26
    • 0030570469 scopus 로고    scopus 로고
    • cDNA cloning and deduced amino acid sequence of fibrinolytic enzyme (Lebetase) from Vipera lebetina snake venom
    • DOI 10.1006/bbrc.1996.1012
    • E. Siigur, A. Aaspollu, A.T. Tu, and J. Siigur cDNA cloning and deduced amino acid sequence of fibrinolytic enzyme (lebetase) from Vipera lebetina snake venom Biochem. Biophys. Res. Commun. 224 1996 229 236 (Pubitemid 26252437)
    • (1996) Biochemical and Biophysical Research Communications , vol.224 , Issue.1 , pp. 229-236
    • Siigur, E.1    Aaspollu, A.2    Tu, A.T.3    Siigur, J.4
  • 27
    • 33746265435 scopus 로고    scopus 로고
    • L-amino acid oxidase from Vipera lebetina venom: Isolation, characterization, effects on platelets and bacteria
    • K. Tõnismägi, M. Samel, K. Trummal, G. Ronnholm, J. Siigur, N. Kalkkinen, and E. Siigur L-amino acid oxidase from Vipera lebetina venom: isolation, characterization, effects on platelets and bacteria Toxicon 48 2006 227 237
    • (2006) Toxicon , vol.48 , pp. 227-237
    • Tõnismägi, K.1    Samel, M.2    Trummal, K.3    Ronnholm, G.4    Siigur, J.5    Kalkkinen, N.6    Siigur, E.7
  • 29
    • 67650253842 scopus 로고    scopus 로고
    • Purification, characterization, and cDNA cloning of acidic platelet aggregation inhibiting phospholipases A(2) from the snake venom of Vipera lebetina (Levantine viper)
    • H. Vija, M. Samel, E. Siigur, A. Aaspõllu, K. Trummal, K. Tõnismägi, J. Subbi, and J. Siigur Purification, characterization, and cDNA cloning of acidic platelet aggregation inhibiting phospholipases A(2) from the snake venom of Vipera lebetina (Levantine viper) Toxicon 54 2009 429 439
    • (2009) Toxicon , vol.54 , pp. 429-439
    • Vija, H.1    Samel, M.2    Siigur, E.3    Aaspõllu, A.4    Trummal, K.5    Tõnismägi, K.6    Subbi, J.7    Siigur, J.8
  • 31
    • 67349253023 scopus 로고    scopus 로고
    • VGD and MLD-motifs containing heterodimeric disintegrin viplebedin-2 from Vipera lebetina snake venom. Purification and cDNA cloning
    • H. Vija, M. Samel, E. Siigur, A. Aaspõllu, K. Tõnismägi, K. Trummal, J. Subbi, and J. Siigur VGD and MLD-motifs containing heterodimeric disintegrin viplebedin-2 from Vipera lebetina snake venom. Purification and cDNA cloning Comp. Biochem. Physiol. B. 153 2009 253 260
    • (2009) Comp. Biochem. Physiol. B. , vol.153 , pp. 253-260
    • Vija, H.1    Samel, M.2    Siigur, E.3    Aaspõllu, A.4    Tõnismägi, K.5    Trummal, K.6    Subbi, J.7    Siigur, J.8
  • 32
    • 0025818718 scopus 로고
    • Purification and characterization of lebetase, a fibrinolytic enzyme from Vipera lebetina (snake) venom
    • E. Siigur, and J. Siigur Purification and characterization of lebetase, a fibrinolytic enzyme from Vipera lebetina (snake) venom Biochim. Biophys. Acta 1074 1991 223 229
    • (1991) Biochim. Biophys. Acta , vol.1074 , pp. 223-229
    • Siigur, E.1    Siigur, J.2
  • 33
    • 0018292828 scopus 로고
    • Thrombocytin, a serine protease from Bothrops atrox venom. 1. Purification and characterization of the enzyme
    • E.P. Kirby, S. Niewiarowski, K. Stocker, C. Kettner, E. Shaw, and T.M. Brudzynski Thrombocytin, a serine protease from Bothrops atrox venom. 1. Purification and characterization of the enzyme Biochemistry 18 1979 3564 3570 (Pubitemid 9255094)
    • (1979) Biochemistry , vol.18 , Issue.16 , pp. 3564-3570
    • Kirby, E.P.1    Niewiarowski, S.2    Stocker, K.3
  • 34
    • 0029060817 scopus 로고
    • Cerastocytin, a new thrombin-like platelet activator from the venom of the Tunisian viper Cerastes cerastes
    • N. Marrakchi, R.B. Zingali, H. Karoui, C. Bon, and M. el Ayeb Cerastocytin, a new thrombin-like platelet activator from the venom of the Tunisian viper Cerastes cerastes Biochim. Biophys. Acta 1244 1995 147 156
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 147-156
    • Marrakchi, N.1    Zingali, R.B.2    Karoui, H.3    Bon, C.4    El Ayeb, M.5
  • 35
    • 0029005343 scopus 로고
    • Purification, characterization, and amino acid sequence of a serine proteinase, PA-BJ, with platelet-aggregating activity from the venom of Bothrops jararaca
    • S.M. Serrano, R. Mentele, C.A. Sampaio, and E. Fink Purification, characterization, and amino acid sequence of a serine proteinase, PA-BJ, with platelet-aggregating activity from the venom of Bothrops jararaca Biochemistry 34 1995 7186 7193
    • (1995) Biochemistry , vol.34 , pp. 7186-7193
    • Serrano, S.M.1    Mentele, R.2    Sampaio, C.A.3    Fink, E.4
  • 36
    • 47249125425 scopus 로고    scopus 로고
    • New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom
    • H.S. Chen, J.M. Chen, C.W. Lin, K.H. Khoo, and I.H. Tsai New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom FEBS J. 275 2008 3944 3958
    • (2008) FEBS J. , vol.275 , pp. 3944-3958
    • Chen, H.S.1    Chen, J.M.2    Lin, C.W.3    Khoo, K.H.4    Tsai, I.H.5
  • 38
    • 0035876166 scopus 로고    scopus 로고
    • Molecular markers of serine protease evolution
    • M.M. Krem, and E. Di Cera Molecular markers of serine protease evolution EMBO J. 20 2001 3036 3045
    • (2001) EMBO J. , vol.20 , pp. 3036-3045
    • Krem, M.M.1    Di Cera, E.2
  • 39
    • 0021930156 scopus 로고
    • Bovine chymotrypsinogen A. X-ray crystal structure analysis and refinement of a new crystal form at 1.8 resolution
    • D. Wang, W. Bode, and R. Huber Bovine chymotrypsinogen A. X-ray crystal structure analysis and refinement of a new crystal form at 1.8 resolution J. Mol. Biol. 185 1985 595 624
    • (1985) J. Mol. Biol. , vol.185 , pp. 595-624
    • Wang, D.1    Bode, W.2    Huber, R.3
  • 40
    • 0017257628 scopus 로고
    • Stability and specificity of protein-protein interactions: The case of the trypsin-trypsin inhibitor complexes
    • J. Janin, and C. Chothia Stability and specificity of protein-protein interactions: the case of the trypsin-trypsin inhibitor complexes J. Mol. Biol. 100 1976 197 211
    • (1976) J. Mol. Biol. , vol.100 , pp. 197-211
    • Janin, J.1    Chothia, C.2
  • 41
    • 0033559558 scopus 로고    scopus 로고
    • Structural and energetic determinants of the S1-site specificity of serine proteinases
    • H. Czapinska, and J. Otlewski Structural and energetic determinants of the S1-site specificity of serine proteinases Eur. J. Biochem. 260 1999 571 595
    • (1999) Eur. J. Biochem. , vol.260 , pp. 571-595
    • Czapinska, H.1    Otlewski, J.2
  • 42
    • 0028133496 scopus 로고
    • Converting trypsin to chymotrypsin: Residue 172 is a substrate specificity determinant
    • DOI 10.1021/bi00195a017
    • L. Hedstrom, J.J. Perona, and W.J. Rutter Converting trypsin to chymotrypsin: residue 172 is a substrate specificity determinant Biochemistry 33 1994 8757 8763 (Pubitemid 24255069)
    • (1994) Biochemistry , vol.33 , Issue.29 , pp. 8757-8763
    • Hedstrom, L.1    Perona, J.J.2    Rutter, W.J.3
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.J. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucl. Acids Res. 22 1994 4673 4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.J.2    Gibson, T.J.3
  • 44
    • 34547657601 scopus 로고    scopus 로고
    • Enzymatic pathways of the brain renin-angiotensin system: Unsolved problems and continuing challenges
    • V.T. Karamyan, and R.C. Speth Enzymatic pathways of the brain renin-angiotensin system: unsolved problems and continuing challenges Regul. Peptides 143 2007 15 27
    • (2007) Regul. Peptides , vol.143 , pp. 15-27
    • Karamyan, V.T.1    Speth, R.C.2


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