메뉴 건너뛰기




Volumn 1814, Issue 10, 2011, Pages 1333-1339

Enzymatic characterization of a serralysin-like metalloprotease from the entomopathogen bacterium, Xenorhabdus

Author keywords

Metalloprotease; Photorhabdus; PrtA peptidase; Serralysin; Xenorhabdus; Zn inhibition

Indexed keywords

COBALT; COPPER; MANGANESE; METALLOPROTEINASE; ZINC;

EID: 80051673277     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.05.008     Document Type: Article
Times cited : (19)

References (40)
  • 1
    • 0021398927 scopus 로고
    • Characterization of inhibitor A, a protease from Bacillus thuringiensis which degrades attacins and cecropins, two classes of antimicrobial proteins in insects
    • G. Dalhammar, and H. Steiner Characterization of inhibitor A, a protease from Bacillus thuringiensis which degrades attacins and cecropins, two classes of antimicrobial proteins in insects Eur. J. Biochem. 139 1984 247 252
    • (1984) Eur. J. Biochem. , vol.139 , pp. 247-252
    • Dalhammar, G.1    Steiner, H.2
  • 2
    • 0030330348 scopus 로고    scopus 로고
    • Tetanus and Botulism neurotoxins, a novel group of zinc-endopeptidases
    • K. Suzuki, J. Bond, Plenum Press New York
    • F. Tonello, S. Morante, O. Rossetto, G. Schiavo, and C. Montecucco Tetanus and Botulism neurotoxins, a novel group of zinc-endopeptidases K. Suzuki, J. Bond, Intracellular Protein Catabolism 1996 Plenum Press New York 251 260
    • (1996) Intracellular Protein Catabolism , pp. 251-260
    • Tonello, F.1    Morante, S.2    Rossetto, O.3    Schiavo, G.4    Montecucco, C.5
  • 4
    • 0015875054 scopus 로고
    • On the specificity of Pseudomonas aeruginosa alkaline proteinase with synthetic substrates
    • K. Morihara, H. Tsuzuki, and T. Oka On the specificity of Pseudomonas aeruginosa alkaline proteinase with synthetic substrates Biochim. Biophys. Acta 309 1973 414 429
    • (1973) Biochim. Biophys. Acta , vol.309 , pp. 414-429
    • Morihara, K.1    Tsuzuki, H.2    Oka, T.3
  • 5
    • 0029072045 scopus 로고
    • Serralysin and related bacterial proteinases
    • A.J. Barret
    • H. Maeda, and K. Morihara Serralysin and related bacterial proteinases A.J. Barret, Methods in Enzymology 248 1995 395 415
    • (1995) Methods in Enzymology , vol.248 , pp. 395-415
    • Maeda, H.1    Morihara, K.2
  • 7
    • 0032729823 scopus 로고    scopus 로고
    • Use of a 49-peptide library for a quantitative and qualitative determination of pseudomonal serralysin specificity
    • D. Louis, J. Bernillon, and J.M. Wallach Use of a 49-peptide library for a quantitative and qualitative determination of pseudomonal serralysin specificity Int. J. Biochem. Cell Biol. 31 1999 1435 1441
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 1435-1441
    • Louis, D.1    Bernillon, J.2    Wallach, J.M.3
  • 9
    • 4544254599 scopus 로고    scopus 로고
    • Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides
    • DOI 10.1128/IAI.72.9.5159-5167.2004
    • R. Belas, J. Manos, and R. Suvanasuthi Proetus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides Infect. Immun. 72 2004 5159 5167 (Pubitemid 39223401)
    • (2004) Infection and Immunity , vol.72 , Issue.9 , pp. 5159-5167
    • Belas, R.1    Manos, J.2    Suvanasuthi, R.3
  • 10
    • 0022514886 scopus 로고
    • Degradation of protease inhibitors, immunoglobulins, and other serum proteins by Serratia protease and its toxicity to fibroblasts in culture
    • A. Molla, K. Matsumoto, I. Oyamada, T. Katsuki, and H. Maeda Degradation of protease inhibitors, immunoglobulins and other serum proteins by Serratia protease and its toxicity to fibroblast in culture Infect. Immun. 53 1986 522 529 (Pubitemid 16053170)
    • (1986) Infection and Immunity , vol.53 , Issue.3 , pp. 522-529
    • Molla, A.1    Matsumoto, K.2    Oyamada, I.3
  • 11
    • 0023641194 scopus 로고
    • Proteus mirabilis strains of diverse type have IgA protease activity
    • B.W. Senior, M. Alberchtsen, and M.A. Kerr Proteus mirabilis strains of diverse type have IgA protease activity J. Med. Microbiol. 24 1987 175 180 (Pubitemid 17146826)
    • (1987) Journal of Medical Microbiology , vol.24 , Issue.2 , pp. 175-180
    • Senior, B.W.1    Albrechtsen, M.2    Kerr, M.A.3
  • 12
    • 0023930897 scopus 로고
    • Cleavage of immunoglobulin G (IgG) and IgA around the hinge region by proteases from Serratia marcescens
    • A. Molla, T. Kagimoto, and H. Maeda Cleavage of immunoglobulin G (IgG) and IgA around the hinge region by proteases from Serratia Marcescens Infect. Immun. 56 1988 916 920 (Pubitemid 18092150)
    • (1988) Infection and Immunity , vol.56 , Issue.4 , pp. 916-920
    • Molla, A.1    Kagimoto, T.2    Maeda, H.3
  • 13
    • 0023904594 scopus 로고
    • Interdomain cleavage of plasma fibronectin by zinc-metalloproteinase from Serratia marcescens
    • A. Molla, S. Tanase, Y.M. Hong, and H. Maeda Interdomain cleavage of plasma fibronectin by zinc-metalloproteinase from Serratia marcescens Biochim. Biophys. Acta 955 1988 77 85
    • (1988) Biochim. Biophys. Acta , vol.955 , pp. 77-85
    • Molla, A.1    Tanase, S.2    Hong, Y.M.3    Maeda, H.4
  • 14
    • 0023930739 scopus 로고
    • A survey of IgA protease production among clinical isolates of Proteeae
    • B.W. Senior, M. Alberchtsen, and M.A. Kerr A survey of IgA protease production among clinical isolates of Proteeae J. Med. Microbiol. 25 1988 27 31 (Pubitemid 18050658)
    • (1988) Journal of Medical Microbiology , vol.25 , Issue.1 , pp. 27-31
    • Senior, B.W.1    Albrechtsen, M.2    Kerr, M.A.3
  • 15
    • 0025275204 scopus 로고
    • Inactivation of chemotactic activity of C5a by the serratial 56-kilodalton protease
    • T. Oda, Y. Kojima, T. Akaike, S. Ijiri, A. Molla, and H. Maeda Inactivation of chemotactic activity of C5a by the serratial 56-kilodalton protease Infect. Immun. 58 1990 1269 1272 (Pubitemid 20151787)
    • (1990) Infection and Immunity , vol.58 , Issue.5 , pp. 1269-1272
    • Oda, T.1    Kojima, Y.2    Akaike, T.3    Ijiri, S.4    Molla, A.5    Maeda, H.6
  • 16
    • 0026538461 scopus 로고
    • Activation of human plasma prekalikrein by Pseudomonas elastase II. Kinetic analysis and identification of scissile bond of prekalikrein in the activation
    • H. Tanaka, T. Yamamoto, Y. Shibuya, N. Nishino, S. Tanase, Y. Miyauchi, and T. Kambara Activation of human plasma prekalikrein by Pseudomonas elastase II. Kinetic analysis and identification of scissile bond of prekalikrein in the activation Biochim. Biophys. Acta 1138 1992 243 250
    • (1992) Biochim. Biophys. Acta , vol.1138 , pp. 243-250
    • Tanaka, H.1    Yamamoto, T.2    Shibuya, Y.3    Nishino, N.4    Tanase, S.5    Miyauchi, Y.6    Kambara, T.7
  • 17
    • 0028889668 scopus 로고
    • Molecular analysis of a metalloprotease from Proetus mirabilis
    • C. Wasiff, D. Cheek, and R. Belas Molecular analysis of a metalloprotease from Proetus mirabilis J. Bacteriol. 177 1995 5790 5798
    • (1995) J. Bacteriol. , vol.177 , pp. 5790-5798
    • Wasiff, C.1    Cheek, D.2    Belas, R.3
  • 18
    • 34247108241 scopus 로고    scopus 로고
    • Cleavage site analysis of a serralysin-like protease, PrtA, from an insect pathogen Photorhabdus luminescens and development of a highly sensitive and specific substrate
    • DOI 10.1111/j.1742-4658.2007.05739.x
    • J. Marokházi, N. Mihala, F. Hudecz, A. Fodor, L. Gráf, and I. Venekei Cleavage site analysis of a serralysin-like protease, PrtA, from an insect pathogen Photorhabdus luminescens and development of a highly sensitive and specific substrate FEBS J. 274 2007 1946 1956 (Pubitemid 46587995)
    • (2007) FEBS Journal , vol.274 , Issue.8 , pp. 1946-1956
    • Marokhazi, J.1    Mihala, N.2    Hudecz, F.3    Fodor, A.4    Graf, L.5    Venekei, I.6
  • 19
    • 0027463205 scopus 로고
    • DNA relatedness between Xenorhabdus spp. (Enterobacteriaceae), symbiotic bacteria of entomopathogenic nematodes, and a proposal to transfer Xenorhabdus luminescens to a new genus, Photorhabdus gen. nov.
    • N.E. Boemare, R.J. Akhurst, and R.G. Mourant DNA Relatedness between Xenorhabdus spp. (Enterobacteriaceae), Symbiotic Bacteria of Entomopathogenic Nematodes, and a Proposal To Transfer Xenorhabdus luminescens to a New Genus, Photorhabdus gen. nov. Int. J. Syst. Bacteriol. 43 1993 249 255 (Pubitemid 23118463)
    • (1993) International Journal of Systematic Bacteriology , vol.43 , Issue.2 , pp. 249-255
    • Boemare, N.E.1    Akhurst, R.J.2    Mourant, R.G.3
  • 20
  • 21
    • 0003086394 scopus 로고    scopus 로고
    • Bacteria-nematode symbiosis
    • R. Gaugler, CABI Publishing Wallingford
    • S. Forst, and D. Clarke Bacteria-nematode symbiosis R. Gaugler, Entomopathogenic Nematology 2002 CABI Publishing Wallingford 57 77
    • (2002) Entomopathogenic Nematology , pp. 57-77
    • Forst, S.1    Clarke, D.2
  • 22
    • 10444263849 scopus 로고    scopus 로고
    • Comparison of proteolytic activities produced by entomopathogenic Photorhabdus bacteria: Strain- and phase-dependent heterogeneity in composition and activity of four enzymes
    • DOI 10.1128/AEM.70.12.7311-7320.2004
    • J. Marokházi, and K. Lengyel Sz. Pekár, G. Felföldi, A. Patthy, L. Gráf, A. Fodor and I. Venekei, Comparison of proteolytic activities produced by entomopathogenic Photorhabdus bacteria: Strain- and phase-dependent heterogeneity in composition and activity of four enzymes Appl. Environ. Microbiol. 70 2004 7311 7320 (Pubitemid 39643796)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.12 , pp. 7311-7320
    • Marokhazi, J.1    Lengyel, K.2    Pekar, S.3    Felfoldi, G.4    Patthy, A.5    Graf, L.6    Fodor, A.7    Venekei, I.8
  • 23
    • 77958529585 scopus 로고    scopus 로고
    • Proteolytic enzyme production of insect pathogen Xenorhabdus bacterium strains and characterization of an early secreted protease as a potential virulence factor
    • M.K. Massaoud, J. Marokházi, A. Fodor, and I. Venekei Proteolytic enzyme production of insect pathogen Xenorhabdus bacterium strains and characterization of an early secreted protease as a potential virulence factor Appl. Environ. Microbiol. 76 2010 6901 6909
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 6901-6909
    • Massaoud, M.K.1    Marokházi, J.2    Fodor, A.3    Venekei, I.4
  • 24
    • 2542577762 scopus 로고    scopus 로고
    • Enzymic characterization with progress curve analysis of a collagen peptidase from an enthomopathogenic bacterium, Photorhabdus luminescens
    • DOI 10.1042/BJ20031116
    • J. Marokházi, Gy. Kóczán, F. Hudecz, L. Gráf, A. Fodor, and I. Venekei Enzymatic characterization with progress curve analysis of a collagen peptidase from an enthomopathogenic bacterium, Photorhabdus luminescens Biochem. J. 379 2004 633 640 (Pubitemid 38703647)
    • (2004) Biochemical Journal , vol.379 , Issue.3 , pp. 633-640
    • Marokhazi, J.1    Koczan, G.2    Hudecz, F.3    Graf, L.4    Fodor, A.5    Venekei, I.6
  • 25
    • 0036195622 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular protease from Xenorhabdus nematophila involved in insect immunosuppression
    • DOI 10.1128/AEM.68.3.1297-1304.2002
    • C. Caldas, A. Cherqui, A. Pereira, and N. Simoes Purification and characterization of an extracellular protease from Xenorhabdus nematophila involved in insect immunosuppression Appl. Environ. Microbiol. 68 2002 1297 1304 (Pubitemid 34205369)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.3 , pp. 1297-1304
    • Caldas, C.1    Cherqui, A.2    Pereira, A.3    Simoes, N.4
  • 27
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • I. Schechter, and A. Berger 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
  • 29
    • 0023031993 scopus 로고
    • 1-proteinase inhibitor by proteinases from Staphylococcus aureus
    • J. Potempa, W. Watorek, and J. Travis The inactivation of human plasma alpha 1-proteinase inhibitor by proteinases from Staphylococcus aureus J. Biol. Chem. 261 1986 14330 14334 (Pubitemid 17196344)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.30 , pp. 14330-14334
    • Potempa, J.1    Watorek, W.2    Travis, J.3
  • 30
    • 0030995095 scopus 로고    scopus 로고
    • Kinetic characterization of the serralysins: A divergent catalytic mechanism pertaining to astacin-type metalloproteases
    • DOI 10.1021/bi963149p
    • W.L. Mock, and J. Yao Kinetic characterization of the serralysins: A divergent catalytic mechanism pertaining to astacin-type metalloprpteases Biochemistry 36 1997 4949 4958 (Pubitemid 27180977)
    • (1997) Biochemistry , vol.36 , Issue.16 , pp. 4949-4958
    • Mock, W.L.1    Yao, J.2
  • 31
    • 0024817526 scopus 로고
    • Carboxypeptidase A: Mechanism of zinc inhibition
    • DOI 10.1021/bi00451a012
    • K.S. Larsen, and D.S. Auld Carboxypeptidase A: Mechanism of zinc inhibition Biochemistry 28 1989 9620 9625 (Pubitemid 20022301)
    • (1989) Biochemistry , vol.28 , Issue.25 , pp. 9620-9625
    • Larsen, K.S.1    Auld, D.S.2
  • 32
    • 0036936933 scopus 로고    scopus 로고
    • Mechanistic studies of the astacin-like Serratia metalloendopeptidase serralysin: Highly active (>2000%) Co(II) and Cu(II) derivatives for further corroboration of a "metallotriad" mechanism
    • DOI 10.1007/s00775-002-0338-2
    • H.I. Park, and L.-J. Ming Mechanistic studies of the astacin-like Serratia metallopepetidase serralysin: highly active (> 2000%) Co(II) and Cu(II) derivatives for further corroboration of a "metallotriad" mechanism J. Biol. Inorg. Chem. 7 2002 600 610 (Pubitemid 36061675)
    • (2002) Journal of Biological Inorganic Chemistry , vol.7 , Issue.6 , pp. 600-610
    • Park, H.I.1    Ming, L.-J.2
  • 33
    • 0037864165 scopus 로고    scopus 로고
    • PH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15)
    • DOI 10.1016/S0014-5793(03)00548-9
    • J.A. Sigman, S.R. Edwards, A. Pabon, M.J. Glucksman, and A.J. Wolfson pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase EC 3.4.24.15 FEBS Lett. 545 2003 224 228 (Pubitemid 36694706)
    • (2003) FEBS Letters , vol.545 , Issue.2-3 , pp. 224-228
    • Sigman, J.A.1    Edwards, S.R.2    Pabon, A.3    Glucksman, M.J.4    Wolfson, A.J.5
  • 36
    • 0025909433 scopus 로고
    • Characterization of an inhibitory metal binding site in carboxypeptidase A
    • K.S. Larsen, and D.S. Auld Characterization of an inhibitory metal binding site in carboxypeptidase A Biochemistry 30 1991 2613 2618
    • (1991) Biochemistry , vol.30 , pp. 2613-2618
    • Larsen, K.S.1    Auld, D.S.2
  • 37
    • 0033603510 scopus 로고    scopus 로고
    • Molecular characterization of a protease secreted by Erwinia amylovora
    • DOI 10.1006/jmbi.1999.2846
    • Y. Zhang, D.D. Bak, H. Heid, and K. Geider Molecular characterization of a protease secreted by Erwinia amylovora J. Mol. Biol. 289 1999 1239 1251 (Pubitemid 29296703)
    • (1999) Journal of Molecular Biology , vol.289 , Issue.5 , pp. 1239-1251
    • Zhang, Y.1    Bak, D.D.2    Heid, H.3    Geider, K.4
  • 38
    • 0029042476 scopus 로고
    • Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi
    • U. Baumann, M. Bauer, S. Letoffe, P. Delepelaire, and C. Wandersmann Crystal structure of a complex between Serratia marcescens metallo-protease and an inhibitor from Erwinia chrysanthemi J. Mol. Biol. 248 1995 653 661
    • (1995) J. Mol. Biol. , vol.248 , pp. 653-661
    • Baumann, U.1    Bauer, M.2    Letoffe, S.3    Delepelaire, P.4    Wandersmann, C.5
  • 39
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: A two-domain protein with a calcium binding parallel beta roll motif
    • U. Baumann, S. Wu, K.M. Flaherty, and D.B. McKay Three dimensional structure of the alkaline proteinase of Pseudomonas aeruginosa: a two domain protein with a calcium binding parallel beta roll motif EMBO J. 12 1993 3357 3364 (Pubitemid 23256422)
    • (1993) EMBO Journal , vol.12 , Issue.9 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 40
    • 0035941112 scopus 로고    scopus 로고
    • Protease C of Erwinia chrysanthemi: The crystal structure and role of amino acids Y228 and E189
    • DOI 10.1006/jmbi.2001.5124
    • T. Hege, and U. Baumann Protease C of Erwinia chrysanthemi: the structure and role of amino acids Y228 and E189 J. Mol. Biol. 314 2001 187 193 (Pubitemid 33105085)
    • (2001) Journal of Molecular Biology , vol.314 , Issue.2 , pp. 187-193
    • Hege, T.1    Baumann, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.