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Volumn 9, Issue 9, 2011, Pages 1487-1501

Characterization of a novel serine protease inhibitor gene from a marine metagenome

Author keywords

Functional characterization; Sequenced based screening; Serine protease inhibitor; Uncultured marine microorganisms

Indexed keywords

CHYMOTRYPSIN A; ELASTASE; PROTEIN SPI1C; RECOMBINANT PROTEIN; SERINE PROTEINASE INHIBITOR; TRYPSIN; UNCLASSIFIED DRUG;

EID: 80053322521     PISSN: None     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md9091487     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins, P. Serpin structure, mechanism, and function. Chem. Rev. 2002, 102, 4751-4803.
    • (2002) Chem. Rev. , vol.102 , pp. 4751-4803
    • Gettins, P.1
  • 3
    • 67650713938 scopus 로고    scopus 로고
    • Conformational pathology of the serpins: Themes, variations, and therapeutic strategies
    • Gooptu, B.; Lomas, D.A. Conformational pathology of the serpins: Themes, variations, and therapeutic strategies. Annu. Rev. Biochem. 2009, 78, 147-176.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 147-176
    • Gooptu, B.1    Lomas, D.A.2
  • 5
    • 68949119950 scopus 로고    scopus 로고
    • Exosite determinants of serpin specificity
    • Gettins, P.G.W.; Olson, S.T. Exosite determinants of serpin specificity. J. Biol. Chem. 2009, 284, 20441-20445.
    • (2009) J. Biol. Chem. , vol.284 , pp. 20441-20445
    • Gettins, P.G.W.1    Olson, S.T.2
  • 6
    • 55949106824 scopus 로고    scopus 로고
    • Biological activities of C1 inhibitor
    • Davis, A.E., III; Mejia, P.; Lu, F. Biological activities of C1 inhibitor. Mol. Immunol. 2008, 45, 4057-4063.
    • (2008) Mol. Immunol. , vol.45 , pp. 4057-4063
    • Davis III, A.E.1    Mejia, P.2    Lu, F.3
  • 7
    • 33644859395 scopus 로고    scopus 로고
    • Active-site distortion is sufficient for proteinase inhibition by serpins
    • Dementiev, A.; Dobo, J.; Gettins, P.G.W. Active-site distortion is sufficient for proteinase inhibition by serpins. J. Biol. Chem. 2006, 281, 3452-3457.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3452-3457
    • Dementiev, A.1    Dobo, J.2    Gettins, P.G.W.3
  • 8
    • 0028955325 scopus 로고
    • Granzyme B is inhibited by the cowpox virus serpin cytokine response modifier A
    • Quan, L.T.; Caputo, A.; Bleackley, R.C.; Pickup, D.J.; Salvesen, G.S. Granzyme B is inhibited by the cowpox virus serpin cytokine response modifier A. J. Biol. Chem. 1995, 270, 10377-10379.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10377-10379
    • Quan, L.T.1    Caputo, A.2    Bleackley, R.C.3    Pickup, D.J.4    Salvesen, G.S.5
  • 9
    • 0032515939 scopus 로고    scopus 로고
    • Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: A kinetic analysis
    • DOI 10.1021/bi972521d
    • Schick, C.; Pemberton, P.A.; Shi, G.P.; Kamachi, Y.; Cataltepe, S.; Bartuski, A.J.; Gornstein, E.R.; Brömme, D.; Chapman, H.A.; Silverman, G.A. Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: A kinetic analysis. Biochemistry 1998, 37, 5258-5266. (Pubitemid 28176527)
    • (1998) Biochemistry , vol.37 , Issue.15 , pp. 5258-5266
    • Schick, C.1    Pemberton, P.A.2    Shi, G.-P.3    Kamachi, Y.4    Cataltepe, S.5    Bartuski, A.J.6    Gornstein, E.R.7    Bromme, D.8    Chapman, H.A.9    Silverman, G.A.10
  • 10
    • 0030794907 scopus 로고    scopus 로고
    • Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): Engineering of inhibitors with altered specificities
    • Scheidig, A.J.; Hynes, T.R.; Pelletier, L.A.; Wells, J.A.; Kossiakoff, A.A. Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): Engineering of inhibitors with altered specificities. Protein Sci. 1997, 6, 1806-1824. (Pubitemid 27391262)
    • (1997) Protein Science , vol.6 , Issue.9 , pp. 1806-1824
    • Scheidig, A.J.1    Hynes, T.R.2    Pelletier, L.A.3    Wells, J.A.4    Kossiakoff, A.A.5
  • 14
    • 76249089297 scopus 로고    scopus 로고
    • Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex
    • Johnson, D.J.; Langdown, J.; Huntington, J.A. Molecular basis of factor IXa recognition by heparin-activated antithrombin revealed by a 1.7-A structure of the ternary complex. Proc. Natl. Acad. Sci. USA 2010, 107, 645-650.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 645-650
    • Johnson, D.J.1    Langdown, J.2    Huntington, J.A.3
  • 15
    • 0032560449 scopus 로고    scopus 로고
    • alpha1-Antitrypsin Protland, a bioengineered serpin highly selective for furin: Application as an antipathogenic agent
    • Jean, F.; Stella, K.; Thomas, L.; Liu, G.; Xiang, Y.; Thomas, G. alpha1-Antitrypsin Protland, a bioengineered serpin highly selective for furin: Application as an antipathogenic agent. Proc. Natl. Acad. Sci. USA 1998, 95, 7293-7298.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7293-7298
    • Jean, F.1    Stella, K.2    Thomas, L.3    Liu, G.4    Xiang, Y.5    Thomas, G.6
  • 18
    • 77952317854 scopus 로고    scopus 로고
    • Exploring microbial diversity for biotechnology: The way forward
    • Singh, B.K. Exploring microbial diversity for biotechnology: The way forward. Trends Biotechnol. 2010, 28, 111-116.
    • (2010) Trends Biotechnol. , vol.28 , pp. 111-116
    • Singh, B.K.1
  • 19
    • 79952093303 scopus 로고    scopus 로고
    • Identification of carbohydrate metabolism genes in the metagenome of a marine biofilm community shown to be dominated by gammaproteobacteria and bacteroidetes
    • Edwards, J.L.; Smith, D.L.; Connolly, J.; McDonald, J.E.; Cox, M.J.; Joint, I.; Edwards, C.; McCarthy, A.J. Identification of carbohydrate metabolism genes in the metagenome of a marine biofilm community shown to be dominated by gammaproteobacteria and bacteroidetes. Genes 2010, 1, 371-384.
    • (2010) Genes , vol.1 , pp. 371-384
    • Edwards, J.L.1    Smith, D.L.2    Connolly, J.3    McDonald, J.E.4    Cox, M.J.5    Joint, I.6    Edwards, C.7    McCarthy, A.J.8
  • 20
    • 70349466430 scopus 로고    scopus 로고
    • Characterization of a highly stable trypsin-like proteinase inhibitor from the seeds of Opuntia streptacantha (O. streptacantha Lemaire)
    • Torres-Castillo, J.A.; Jacobo, C.M.; Blanco-Labra, A. Characterization of a highly stable trypsin-like proteinase inhibitor from the seeds of Opuntia streptacantha (O. streptacantha Lemaire). Phytochemistry 2009, 70, 1374-1381.
    • (2009) Phytochemistry , vol.70 , pp. 1374-1381
    • Torres-Castillo, J.A.1    Jacobo, C.M.2    Blanco-Labra, A.3
  • 22
    • 39649105868 scopus 로고    scopus 로고
    • A novel serine protease inhibitor from Bungarus fasciatus venom
    • Lu, J.; Yang, H.; Yu, H.; Gao, W.; Lai, R.; Liu, J.; Liang, X. A novel serine protease inhibitor from Bungarus fasciatus venom. Peptides 2008, 29, 369-374.
    • (2008) Peptides , vol.29 , pp. 369-374
    • Lu, J.1    Yang, H.2    Yu, H.3    Gao, W.4    Lai, R.5    Liu, J.6    Liang, X.7
  • 23
  • 24
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode, W.; Huber, R. Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 1992, 204, 433-451.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 25
    • 13444263657 scopus 로고    scopus 로고
    • Taiwan cobra chymotrypsin inhibitor: Cloning, functional expression and gene organization
    • Cheng, Y.C.; Yan, F.J.; Chang, L.S. Taiwan cobra chymotrypsin inhibitor: Cloning, functional expression and gene organization. Biochim. Biophys. Acta 2005, 1747, 213-220.
    • (2005) Biochim. Biophys. Acta , vol.1747 , pp. 213-220
    • Cheng, Y.C.1    Yan, F.J.2    Chang, L.S.3
  • 26
    • 0034523345 scopus 로고    scopus 로고
    • Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function
    • DOI 10.1101/gr.GR-1478R
    • Irving, J.A.; Pike, R.N.; Lesk, A.M.; Whisstock, J.C. Phylogeny of the serpin superfamily: Implications of patterns of amino acid conservation for structure and function. Genome Res. 2000, 10, 1845-1864. (Pubitemid 32049132)
    • (2000) Genome Research , vol.10 , Issue.12 , pp. 1845-1864
    • Irving, J.A.1    Pike, R.N.2    Lesk, A.M.3    Whisstock, J.C.4
  • 27
    • 78751614085 scopus 로고    scopus 로고
    • Regulation of proteases by protein inhibitors of the serpin superfamily
    • Olson, S.T.; Gettins, P.G. Regulation of proteases by protein inhibitors of the serpin superfamily. Prog. Mol. Biol. Transl. Sci. 2011, 99, 185-240.
    • (2011) Prog. Mol. Biol. Transl. Sci. , vol.99 , pp. 185-240
    • Olson, S.T.1    Gettins, P.G.2
  • 28
    • 0004136246 scopus 로고    scopus 로고
    • 3rd ed.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, Suffolk, NY, USA
    • Sambrook, J.; Russell, D.W. Molecular Cloning: A Laboratory Manual, 3rd ed.; Cold Spring Harbor Laboratory Press: Cold Spring Harbor, Suffolk, NY, USA, 2001.
    • (2001) Molecular Cloning: A Laboratory Manual
    • Sambrook, J.1    Russell, D.W.2
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • DOI 10.1016/0003-2697(87)90587-2
    • Schägger, H.; 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. 1987, 166, 368-379. (Pubitemid 18004907)
    • (1987) Analytical Biochemistry , vol.166 , Issue.2 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 30
    • 84855988613 scopus 로고    scopus 로고
    • Available online accessed on 20 August 2010
    • ExPASy Translate. Available online: http://www.expasy.org/tools/dna.html (accessed on 20 August 2010).
  • 31
    • 84855991363 scopus 로고    scopus 로고
    • Available online accessed on 10 August 2010
    • NCBI Entres. Available online: http://www.ncbi.nlm.nih.gov/Entrez/ (accessed on 10 August 2010).
  • 32
    • 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. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol. Biol. Evol. 2007, 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
  • 33
    • 0015338074 scopus 로고
    • A new assay for cathepsin B1 and other thiol proteinases
    • Barrett, A.J. A new assay for cathepsin B1 and other thiol proteinases. Anal. Biochem. 1972, 47, 280-293.
    • (1972) Anal. Biochem. , vol.47 , pp. 280-293
    • Barrett, A.J.1
  • 34
    • 0015875083 scopus 로고
    • An improvement in the Hummel chymotrypsin assay
    • Kang, S.H.; Fuchs, M.S. An improvement in the Hummel chymotrypsin assay. Anal. Biochem. 1973, 54, 262-265.
    • (1973) Anal. Biochem. , vol.54 , pp. 262-265
    • Kang, S.H.1    Fuchs, M.S.2
  • 35
    • 0035069853 scopus 로고    scopus 로고
    • Kinetic and structural properties of two isoforms of trypsin isolated from the viscera of Japanese anchovy, Engraulis japonicus
    • Ahsan, M.N.; Watabe, S. Kinetic and structural properties of two isoforms of trypsin isolated from the viscera of Japanese anchovy, Engraulis japonicus. J. Protein Chem. 2001, 20, 49-58.
    • (2001) J. Protein Chem. , vol.20 , pp. 49-58
    • Ahsan, M.N.1    Watabe, S.2
  • 36
    • 70349993601 scopus 로고    scopus 로고
    • ShotgunFunctionalizeR: An R-package for functional comparison of metagenomes
    • Kristiansson, E.; Hugenholtz, P.; Dalevi, D. ShotgunFunctionalizeR: An R-package for functional comparison of metagenomes. Bioinformatics 2009, 25, 2737-2738.
    • (2009) Bioinformatics , vol.25 , pp. 2737-2738
    • Kristiansson, E.1    Hugenholtz, P.2    Dalevi, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.