메뉴 건너뛰기




Volumn 393, Issue 10, 2012, Pages 1027-1041

Functional and structural insights into astacin metallopeptidases

Author keywords

Bone morphogenetic protein; Catalytic domain; Meprin; Metzincin; Tolloid; Zinc metallopeptidase

Indexed keywords

ASPARTIC ACID; ASTACIN; ENZYME; ENZYME PRECURSOR; MEPRIN ALPHA; MEPRIN BETA; NEPHROSIN; OVASTACIN; TYROSINE; UNCLASSIFIED DRUG;

EID: 84867043026     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/hsz-2012-0149     Document Type: Review
Times cited : (73)

References (108)
  • 2
    • 70450253102 scopus 로고    scopus 로고
    • A disintegrin-like and metalloprotease (reprolysintype) with thrombospondin type 1 motif (ADAMTS) superfamily: Functions and mechanisms
    • Apte, S.S. (2009). A disintegrin-like and metalloprotease (reprolysintype) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanisms. J. Biol. Chem. 284, 31493-31497.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31493-31497
    • Apte, S.S.1
  • 4
    • 57649123150 scopus 로고    scopus 로고
    • Prointerleukin-18 is activated by meprin β in vitro and in vivo in intestinal infl ammation
    • Banerjee, S. and Bond, J. (2008). Prointerleukin-18 is activated by meprin β in vitro and in vivo in intestinal infl ammation. J. Biol. Chem. 283, 31371-31377.
    • (2008) J. Biol. Chem. , vol.283 , pp. 31371-31377
    • Banerjee, S.1    Bond, J.2
  • 5
    • 84944048911 scopus 로고    scopus 로고
    • 152. Serralysin and related enzymes
    • A.J. Barrett, N.D. Rawlings, and J.F. Woessner Jr., eds. , (London: Elsevier Academic Press)
    • Baumann, U. (2004). 152. Serralysin and related enzymes. In: A.J. Barrett, N.D. Rawlings, and J.F. Woessner Jr., eds. Handbook of Proteolytic Enzymes, Vol. 1 (London: Elsevier Academic Press), pp. 579-581.
    • (2004) Handbook of Proteolytic Enzymes , vol.1 , pp. 579-581
    • Baumann, U.1
  • 9
    • 0027193209 scopus 로고
    • An adhesive domain detected in functionally diverse receptors
    • Beckmann, G. and Bork, P. (1993). An adhesive domain detected in functionally diverse receptors. Trends Biochem. Sci. 18, 40-41.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 40-41
    • Beckmann, G.1    Bork, P.2
  • 10
    • 0017850232 scopus 로고
    • Crystal structure analysis and refi nement of two variants of trigonal trypsinogen: Trigonal trypsin and PEG (polyethylene glycol) trypsinogen and their comparison with orthorhombic trypsin and trigonal trypsinogen
    • Bode, W. and Huber, R. (1978). Crystal structure analysis and refi nement of two variants of trigonal trypsinogen: trigonal trypsin and PEG (polyethylene glycol) trypsinogen and their comparison with orthorhombic trypsin and trigonal trypsinogen. FEBS Lett. 90, 265-269.
    • (1978) Febs Lett. , vol.90 , pp. 265-269
    • Bode, W.1    Huber, R.2
  • 11
    • 0026736225 scopus 로고
    • Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases
    • Bode, W., Gomis-Rüth, F.X., Huber, R., Zwilling, R., and Stöcker, W. (1992). Structure of astacin and implications for activation of astacins and zinc-ligation of collagenases. Nature 358, 164-167.
    • (1992) Nature , vol.358 , pp. 164-167
    • Bode, W.1    Gomis-Ruth, F.X.2    Huber, R.3    Zwilling, R.4    St Cker, Ö.W.5
  • 12
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the' metzincins
    • Bode, W., Gomis-Rüth, F.X., and Stöcker, W. (1993). Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the' metzincins.' FEBS Lett. 331, 134-140.
    • (1993) FEBS Lett. , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    St Cker, Ö.W.3
  • 13
    • 0035447508 scopus 로고    scopus 로고
    • Mutational analysis of the proteolytic domain of pregnancy-associated plasma protein-A (PAPP-A): Classifi cation as a metzincin
    • Boldt, H.B., Overgaard, M.T., Laursen, L.S., Weyer, K., Sottrup-Jensen, L., and Oxvig, C. (2001). Mutational analysis of the proteolytic domain of pregnancy-associated plasma protein-A (PAPP-A): classifi cation as a metzincin. Biochem. J. 358, 359- 367.
    • (2001) Biochem. J. , vol.358 , pp. 359-367
    • Boldt, H.B.1    Overgaard, M.T.2    Laursen, L.S.3    Weyer, K.4    Sottrup-Jensen, L.5    Oxvig, C.6
  • 14
    • 0029016839 scopus 로고
    • The astacin family of metalloendopeptidases
    • Bond, J.S. and Beynon, R.J. (1995). The astacin family of metalloendopeptidases. Protein Sci. 4, 1247-1261.
    • (1995) Protein Sci. , vol.4 , pp. 1247-1261
    • Bond, J.S.1    Beynon, R.J.2
  • 15
    • 33947218270 scopus 로고    scopus 로고
    • Identifi cation and characterization of onchoastacin, an astacin-like metalloproteinase from the fi laria Onchocerca volvulus
    • Borchert, N., Becker-Pauly, C., Wagner, A., Fischer, P., Stöcker, W., and Brattig, N.W. (2007). Identifi cation and characterization of onchoastacin, an astacin-like metalloproteinase from the fi laria Onchocerca volvulus . Microbes Infect. 9, 498-506.
    • (2007) Microbes Infect. , vol.9 , pp. 498-506
    • Borchert, N.1    Becker-Pauly, C.2    Wagner, A.3    Fischer, P.4    St Cker, Ö.W.5    Brattig, N.W.6
  • 17
    • 2442561604 scopus 로고    scopus 로고
    • The canonical methionine 392 of matrix metalloproteinase 2 (gelatinase A) is not required for catalytic effi ciency or structural integrity: Probing the role of the methionine-turn in the metzincin metalloprotease superfamily
    • Butler, G.S., Tam, E.M., and Overall, C.M. (2004). The canonical methionine 392 of matrix metalloproteinase 2 (gelatinase A) is not required for catalytic effi ciency or structural integrity: probing the role of the methionine-turn in the metzincin metalloprotease superfamily. J. Biol. Chem. 279, 15615-15620.
    • (2004) J. Biol. Chem. , vol.279 , pp. 15615-15620
    • Butler, G.S.1    Tam, E.M.2    Overall, C.M.3
  • 20
    • 27244461848 scopus 로고
    • A new member to the astacin family of metalloendopeptidases: A novel 1,25-dihydroxyvitamin D-3-stimulated mRNA from chorioallantoic membrane of quail
    • Elaroussi, M.A. and DeLuca, H.F. (1994). A new member to the astacin family of metalloendopeptidases: a novel 1,25-dihydroxyvitamin D-3-stimulated mRNA from chorioallantoic membrane of quail. Biochim. Biophys. Acta 1217, 1-8.
    • (1994) Biochim. Biophys. Acta , vol.1217 , pp. 1-8
    • Elaroussi, M.A.1    Deluca, H.F.2
  • 21
    • 0034795758 scopus 로고    scopus 로고
    • Properties of the hatching enzyme from Xenopus laevis
    • Fan, T.J. and Katagiri, C. (2001). Properties of the hatching enzyme from Xenopus laevis . Eur. J. Biochem. 268, 4892-4898.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4892-4898
    • Fan, T.J.1    Katagiri, C.2
  • 22
    • 0017348682 scopus 로고
    • Crystal structure of bovine trypsinogen at 1.8 Å resolution. II. Crystallographic refi nement, refi ned crystal structure and comparison with bovine trypsin
    • Fehlhammer, H., Bode, W., and Huber, R. (1977). Crystal structure of bovine trypsinogen at 1.8 Å resolution. II. Crystallographic refi nement, refi ned crystal structure and comparison with bovine trypsin. J. Mol. Biol. 111, 415-438.
    • (1977) J. Mol. Biol. , vol.111 , pp. 415-438
    • Fehlhammer, H.1    Bode, W.2    Huber, R.3
  • 23
    • 9644291556 scopus 로고    scopus 로고
    • Deletion of epidermal growth factor-like domains converts mammalian tolloid into a chordinase and effective procollagen C-proteinase
    • Garrigue-Antar, L., Francois, V., and Kadler, K.E. (2004). Deletion of epidermal growth factor-like domains converts mammalian tolloid into a chordinase and effective procollagen C-proteinase. J. Biol. Chem. 279, 49835-49841.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49835-49841
    • Garrigue-Antar, L.1    Francois, V.2    Kadler, K.E.3
  • 24
    • 33646567450 scopus 로고    scopus 로고
    • Developmental roles of the BMP1/TLD metalloproteinases
    • Ge, G. and Greenspan, D.S. (2006). Developmental roles of the BMP1/TLD metalloproteinases. Birth Defects Res., Part C 78, 47-68.
    • (2006) Birth Defects Res., Part C , vol.78 , pp. 47-68
    • Ge, G.1    Greenspan, D.S.2
  • 25
    • 0032079907 scopus 로고    scopus 로고
    • Cloning and characterization of a cDNA coding for Astacus embryonic astacin, a member of the astacin family of metalloproteases from the crayfi sh Astacus astacus
    • Geier, G. and Zwilling, R. (1998). Cloning and characterization of a cDNA coding for Astacus embryonic astacin, a member of the astacin family of metalloproteases from the crayfi sh Astacus astacus . Eur. J. Biochem. 253, 796-803.
    • (1998) Eur. J. Biochem. , vol.253 , pp. 796-803
    • Geier, G.1    Zwilling, R.2
  • 26
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Rüth, F.X. (2003). Structural aspects of the metzincin clan of metalloendopeptidases. Mol. Biotechnol. 24, 157-202.
    • (2003) Mol. Biotechnol. , vol.24 , pp. 157-202
    • Gomis-R Th, U.F.X.1
  • 27
    • 54249136672 scopus 로고    scopus 로고
    • Structure and mechanism of metallocarboxypeptidases
    • Gomis-Rüth, F.X. (2008). Structure and mechanism of metallocarboxypeptidases. Crit. Rev. Biochem. Mol. Biol. 43, 319-345.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , pp. 319-345
    • Gomis-R Th, U.F.X.1
  • 28
    • 67650065404 scopus 로고    scopus 로고
    • Catalytic domain architecture of metzincin metalloproteases
    • Gomis-Rüth, F.X. (2009). Catalytic domain architecture of metzincin metalloproteases. J. Biol. Chem. 284, 15353-15357.
    • (2009) J. Biol. Chem. , vol.284 , pp. 15353-15357
    • Gomis-R Th, U.F.X.1
  • 29
    • 0027418428 scopus 로고
    • Refi ned 1.8 Å X-ray crystal structure of astacin, a zincendopeptidase from the crayfi sh Astacus astacus L. Structure determination, refi nement, molecular structure and comparison with thermolysin
    • Gomis-Rüth, F.X., Stöcker, W., Huber, R., Zwilling, R., and Bode, W. (1993). Refi ned 1.8 Å X-ray crystal structure of astacin, a zincendopeptidase from the crayfi sh Astacus astacus L. Structure determination, refi nement, molecular structure and comparison with thermolysin. J. Mol. Biol. 229, 945-968.
    • (1993) J. Mol. Biol. , vol.229 , pp. 945-968
    • Gomis-R Th, U.F.X.1    St Cker, Ö.W.2    Huber, R.3    Zwilling, R.4    Bode, W.5
  • 32
    • 79952133561 scopus 로고    scopus 로고
    • Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog
    • Goulas, T., Arolas, J.L., and Gomis-Rüth, F.X. (2010). Structure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenolog. Proc. Natl. Acad. Sci. USA 108, 1856-1861.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 1856-1861
    • Goulas, T.1    Arolas, J.L.2    Gomis-Ruth, F.X.3
  • 35
    • 0242384939 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprin β metalloprotease
    • Hahn, D., Pischitzis, A., Roesmann, S., Hansen, M.K., Leuenberger, B., Luginbuehl, U., and Sterchi, E.E. (2003). Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprin β metalloprotease. J. Biol. Chem. 278, 42829-42839.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42829-42839
    • Hahn, D.1    Pischitzis, A.2    Roesmann, S.3    Hansen, M.K.4    Leuenberger, B.5    Luginbuehl, U.6    Sterchi, E.E.7
  • 37
    • 0035941115 scopus 로고    scopus 로고
    • The conserved methionine residue of the metzincins: A site-directed mutagenesis study
    • Hege, T. and Baumann, U. (2001). The conserved methionine residue of the metzincins: a site-directed mutagenesis study. J. Mol. Biol. 314, 181-186.
    • (2001) J. Mol. Biol. , vol.314 , pp. 181-186
    • Hege, T.1    Baumann, U.2
  • 38
    • 23944491189 scopus 로고    scopus 로고
    • Generation of biologically active interleukin-1 β by meprin B
    • Herzog, C., Kaushal, G.P., and Haun, R.S. (2005). Generation of biologically active interleukin-1 β by meprin B. Cytokine 31, 394-403.
    • (2005) Cytokine , vol.31 , pp. 394-403
    • Herzog, C.1    Kaushal, G.P.2    Haun, R.S.3
  • 39
    • 33744753774 scopus 로고    scopus 로고
    • The interaction of recombinant subdomains of the procollagen C-proteinase with procollagen i provides a quantitative explanation for functional differences between the two splice variants, mammalian tolloid and bone morphogenetic protein 1
    • Hintze, V., Höwel, M., Wermter, C., Grosse Berkhoff, E., Becker- Pauly, C., Beermann, B., Yiallouros, I., and Stöcker, W. (2006). The interaction of recombinant subdomains of the procollagen C-proteinase with procollagen I provides a quantitative explanation for functional differences between the two splice variants, mammalian tolloid and bone morphogenetic protein 1. Biochemistry 45, 6741-6748.
    • (2006) Biochemistry , vol.45 , pp. 6741-6748
    • Hintze, V.1    Höwel, M.2    Wermter, C.3    Grosse Berkhoff, E.4    Becker- Pauly, C.5    Beermann, B.6    Yiallouros, I.7    St Cker, Ö.W.8
  • 40
    • 0026489329 scopus 로고
    • Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis
    • Holland, D.R., Tronrud, D.E., Pley, H.W., Flaherty, K.M., Stark, W., Jansonius, J.N., McKay, D.B., and Matthews, B.W. (1992). Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis. Biochemistry 31, 11310-11316.
    • (1992) Biochemistry , vol.31 , pp. 11310-11316
    • Holland, D.R.1    Tronrud, D.E.2    Pley, H.W.3    Flaherty, K.M.4    Stark, W.5    Jansonius, J.N.6    McKay, D.B.7    Matthews, B.W.8
  • 41
    • 0030598871 scopus 로고    scopus 로고
    • The Xenopus dorsalizing factor noggin ventralizes Drosophila embryos by preventing DPP from activating its receptor
    • Holley, S., Neul, J., Attisano, L., Wrana, J., Sasai, Y., O' Connor, M., De Robertis, E., and Ferguson, E. (1996). The Xenopus dorsalizing factor noggin ventralizes Drosophila embryos by preventing DPP from activating its receptor. Cell 86, 607-617.
    • (1996) Cell , vol.86 , pp. 607-617
    • Holley, S.1    Neul, J.2    Attisano, L.3    Wrana, J.4    Sasai, Y.5    O'onnor, M.6    De Robertis, E.7    Ferguson, E.8
  • 42
    • 35348923714 scopus 로고    scopus 로고
    • The bone morphogenetic protein 1/Tolloid-like metalloproteinases
    • Hopkins, D.R., Keles, S., and Greenspan, D.S. (2007). The bone morphogenetic protein 1/Tolloid-like metalloproteinases. Matrix Biol. 26, 508-523.
    • (2007) Matrix Biol. , vol.26 , pp. 508-523
    • Hopkins, D.R.1    Keles, S.2    Greenspan, D.S.3
  • 43
    • 33947092515 scopus 로고
    • Structural basis for the activation and action of trypsin
    • Huber, R. and Bode, W. (1986). Structural basis for the activation and action of trypsin. Acc. Chem. Res. 11, 114-122.
    • (1986) Acc. Chem. Res. , vol.11 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 44
    • 0030985950 scopus 로고    scopus 로고
    • Purifi cation and cloning of carp nephrosin, a secreted zinc endopeptidase of the astacin family
    • Hung, C.H., Huang, H.R., Huang, C.J., Huang, F.L., and Chang, G.D. (1997). Purifi cation and cloning of carp nephrosin, a secreted zinc endopeptidase of the astacin family. J. Biol. Chem. 272, 13772-13778.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13772-13778
    • Hung, C.H.1    Huang, H.R.2    Huang, C.J.3    Huang, F.L.4    Chang, G.D.5
  • 46
    • 0030593032 scopus 로고    scopus 로고
    • Bone morphogenetic protein-1: The type i procollagen C-proteinase
    • Kessler, E., Takahara, K., Biniaminov, L., Brusel, M., and Greenspan, D.S. (1996). Bone morphogenetic protein-1: the type I procollagen C-proteinase. Science 271, 360-362.
    • (1996) Science , vol.271 , pp. 360-362
    • Kessler, E.1    Takahara, K.2    Biniaminov, L.3    Brusel, M.4    Greenspan, D.S.5
  • 47
    • 0031956497 scopus 로고    scopus 로고
    • Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
    • Khan, A.R. and James, M.N. (1998). Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. Protein Sci. 7, 815-836.
    • (1998) Protein Sci. , vol.7 , pp. 815-836
    • Khan, A.R.1    James, M.N.2
  • 49
    • 0026536983 scopus 로고
    • Spatial and temporal expression pattern during sea urchin embryogenesis of a gene coding for a protease homologous to the human protein BMP-1 and to the product of the Drosophila dorsal-ventral patterning gene tolloid
    • Lepage, T., Ghiglione, C., and Gache, C. (1992). Spatial and temporal expression pattern during sea urchin embryogenesis of a gene coding for a protease homologous to the human protein BMP-1 and to the product of the Drosophila dorsal-ventral patterning gene tolloid. Development 114, 147-163.
    • (1992) Development , vol.114 , pp. 147-163
    • Lepage, T.1    Ghiglione, C.2    Gache, C.3
  • 50
    • 0029906315 scopus 로고    scopus 로고
    • The C-proteinase that processes procollagens to fi brillar collagens is identical to the protein previously identifi ed as bone morphogenic protein-1
    • Li, S.W., Sieron, A.L., Fertala, A., Hojima, Y., Arnold, W.V., and Prockop, D.J. (1996). The C-proteinase that processes procollagens to fi brillar collagens is identical to the protein previously identifi ed as bone morphogenic protein-1. Proc. Natl. Acad. Sci. USA 93, 5127-5130.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5127-5130
    • Li, S.W.1    Sieron, A.L.2    Fertala, A.3    Hojima, Y.4    Arnold, W.V.5    Prockop, D.J.6
  • 51
    • 0037954614 scopus 로고    scopus 로고
    • Characterization and cloning of metallo-proteinase in the excretory/secretory products of the infective-stage larva of Trichinella spiralis
    • Lun, H.M., Mak, C.H., and Ko, R.C. (2003). Characterization and cloning of metallo-proteinase in the excretory/secretory products of the infective-stage larva of Trichinella spiralis . Parasitol. Res. 90, 27-37.
    • (2003) Parasitol. Res. , vol.90 , pp. 27-37
    • Lun, H.M.1    Mak, C.H.2    Ko, R.C.3
  • 54
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • Matthews, B.W. (1988). Structural basis of the action of thermolysin and related zinc peptidases. Acc. Chem. Res. 21, 333-340.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.W.1
  • 56
    • 0034055985 scopus 로고    scopus 로고
    • Function and mechanism of zinc metalloenzymes
    • McCall, K.A., Huang, C., and Fierke, C.A. (2000). Function and mechanism of zinc metalloenzymes. J. Nutr. 130, 1437S - 1446S.
    • (2000) J. Nutr. , vol.130
    • McCall, K.A.1    Huang, C.2    Fierke, C.A.3
  • 57
    • 0028020026 scopus 로고
    • The cleavage of the bait region of α2 -macroglobulin by human immunodefi ciency virus proteinases and by astacin
    • Meier, U.C., Boetzel, J., Kellermann, J., Mann, K., Billich, A., Stöcker, W., and Schramm, H.J. (1994). The cleavage of the bait region of α2 -macroglobulin by human immunodefi ciency virus proteinases and by astacin. Ann. NY Acad. Sci. 737, 431-433.
    • (1994) Ann. NY Acad. Sci. , vol.737 , pp. 431-433
    • Meier, U.C.1    Boetzel, J.2    Kellermann, J.3    Mann, K.4    Billich, A.5    St Cker, Ö.W.6    Schramm, H.J.7
  • 58
    • 17444450739 scopus 로고    scopus 로고
    • The astacin protein family in Caenorhabditis elegans
    • Möhrlen, F., Hutter, H., and Zwilling, R. (2003). The astacin protein family in Caenorhabditis elegans . Eur. J. Biochem. 270, 4909-4920.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4909-4920
    • Mohrlen, F.1    Hutter, H.2    Zwilling, R.3
  • 59
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase, H. (1997). Activation mechanisms of matrix metalloproteinases. Biol. Chem. 378, 151-160.
    • (1997) Biol. Chem. , vol.378 , pp. 151-160
    • Nagase, H.1
  • 60
    • 70349456579 scopus 로고    scopus 로고
    • Metzincin' s canonical methionine is responsible for the structural integrity of the zinc-binding site
    • Oberholzer, A.E., Bumann, M., Hege, T., Russo, S., and Baumann, U. (2009). Metzincin' s canonical methionine is responsible for the structural integrity of the zinc-binding site. Biol. Chem. 390, 875-881.
    • (2009) Biol. Chem. , vol.390 , pp. 875-881
    • Oberholzer, A.E.1    Bumann, M.2    Hege, T.3    Russo, S.4    Baumann, U.5
  • 61
    • 77951479269 scopus 로고    scopus 로고
    • Analyzing the protease web in skin: Meprin metalloproteases are activated specifi cally by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation
    • Ohler, A., Debela, M., Wagner, S., Magdolen, V., and Becker-Pauly, C. (2010). Analyzing the protease web in skin: meprin metalloproteases are activated specifi cally by KLK4, 5 and 8 vice versa leading to processing of proKLK7 thereby triggering its activation. Biol. Chem. 391, 455-460.
    • (2010) Biol. Chem. , vol.391 , pp. 455-460
    • Ohler, A.1    Debela, M.2    Wagner, S.3    Magdolen, V.4    Becker-Pauly, C.5
  • 63
    • 0024278094 scopus 로고
    • Crystal structure of neutral protease from Bacillus cereus refi ned at 3.0 Å resolution and comparison with the homologous but more thermostable enzyme thermolysin
    • Pauptit, R.A., Karlsson, R., Picot, D., Jenkins, J.A., Niklaus-Reimer, A.S., and Jansonius, J.N. (1988). Crystal structure of neutral protease from Bacillus cereus refi ned at 3.0 Å resolution and comparison with the homologous but more thermostable enzyme thermolysin. J. Mol. Biol. 199, 525-537.
    • (1988) J. Mol. Biol. , vol.199 , pp. 525-537
    • Pauptit, R.A.1    Karlsson, R.2    Picot, D.3    Jenkins, J.A.4    Niklaus-Reimer, A.S.5    Jansonius, J.N.6
  • 64
    • 34249935565 scopus 로고    scopus 로고
    • Substitution of methionine 435 with leucine, isoleucine, and serine in tumor necrosis factor α converting enzyme inactivates ectodomain shedding activity
    • P é rez, L., Kerrigan, J.E., Li, X., and Fan, H. (2007). Substitution of methionine 435 with leucine, isoleucine, and serine in tumor necrosis factor α converting enzyme inactivates ectodomain shedding activity. Biochem. Cell Biol. 85, 141-149.
    • (2007) Biochem. Cell Biol. , vol.85 , pp. 141-149
    • Perez, L.1    Kerrigan, J.E.2    Li, X.3    Fan, H.4
  • 65
    • 0030852784 scopus 로고    scopus 로고
    • Expression, purifi cation, characterization, and X-ray analysis of selenomethionine 215 variant of leukocyte collagenase
    • Pieper, M., Betz, M., Budisa, N., Gomis-Rüth, F.X., Bode, W., and Tschesche, H. (1997). Expression, purifi cation, characterization, and X-ray analysis of selenomethionine 215 variant of leukocyte collagenase. J. Protein Chem. 16, 637-650.
    • (1997) J. Protein Chem. , vol.16 , pp. 637-650
    • Pieper, M.1    Betz, M.2    Budisa, N.3    Gomis-Ruth, F.X.4    Bode, W.5    Tschesche, H.6
  • 66
    • 2942754000 scopus 로고    scopus 로고
    • Identifi cation and characterization of human and mouse ovastacin: A novel metalloproteinase similar to hatching enzymes from arthropods, birds, amphibians, and fi sh
    • Quesada, V., S á nchez, L.M., Alvarez, J., and L ó pez-Ot í n, C. (2004). Identifi cation and characterization of human and mouse ovastacin: a novel metalloproteinase similar to hatching enzymes from arthropods, birds, amphibians, and fi sh. J. Biol. Chem. 279, 26627-26634.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26627-26634
    • Quesada, V.1    Sanchez, L.M.2    Alvarez, J.3    Lopez-Otin, C.4
  • 69
    • 0033572635 scopus 로고    scopus 로고
    • CDNA cloning, bacterial expression, in vitro renaturation and affi nity purifi cation of the zinc endopeptidase astacin
    • Reyda, S., Jacob, E., Zwilling, R., and Stöcker, W. (1999). cDNA cloning, bacterial expression, in vitro renaturation and affi nity purifi cation of the zinc endopeptidase astacin. Biochem. J. 344, 851-857.
    • (1999) Biochem. J. , vol.344 , pp. 851-857
    • Reyda, S.1    Jacob, E.2    Zwilling, R.3    St Cker, Ö.W.4
  • 70
    • 0026603920 scopus 로고
    • Early mRNAs, spatially restricted along the animalvegetal axis of sea urchin embryos, include one encoding a protein related to tolloid and BMP-1
    • Reynolds, S.D., Angerer, L.M., Palis, J., Nasir, A., and Angerer, R.C. (1992). Early mRNAs, spatially restricted along the animalvegetal axis of sea urchin embryos, include one encoding a protein related to tolloid and BMP-1. Development 114, 769-786.
    • (1992) Development , vol.114 , pp. 769-786
    • Reynolds, S.D.1    Angerer, L.M.2    Palis, J.3    Nasir, A.4    Angerer, R.C.5
  • 71
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe, M., Wong, S.C., Henzel, W.J., and Goeddel, D.V. (1994). A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell 78, 681-692.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.C.2    Henzel, W.J.3    Goeddel, D.V.4
  • 73
    • 0025096627 scopus 로고
    • Molecular approach to dorsoanterior development in Xenopus laevis
    • Sato, S.M. and Sargent, T.D. (1990). Molecular approach to dorsoanterior development in Xenopus laevis . Dev. Biol. 137, 135-141.
    • (1990) Dev. Biol. , vol.137 , pp. 135-141
    • Sato, S.M.1    Sargent, T.D.2
  • 74
    • 77952485887 scopus 로고    scopus 로고
    • Let it fl ow: Morpholino knockdown in zebrafi sh embryos reveals a pro-angiogenic effect of the metalloprotease meprin α2
    • Schütte, A., Hedrich, J., Stöcker, W., and Becker-Pauly, C. (2010). Let it fl ow: Morpholino knockdown in zebrafi sh embryos reveals a pro-angiogenic effect of the metalloprotease meprin α2. PLoS ONE 5, e8835.
    • (2010) PLoS ONE , vol.5
    • Sch Tte, Ü.A.1    Hedrich, J.2    St Cker, Ö.W.3    Becker-Pauly, C.4
  • 75
    • 0034708629 scopus 로고    scopus 로고
    • Identifi cation and cDNA cloning of alveolin, an extracellular metalloproteinase, which induces chorion hardening of medaka (Oryzias latipes) eggs upon fertilization
    • Shibata, Y., Iwamatsu, T., Oba, Y., Kobayashi, D., Tanaka, M., Nagahama, Y., Suzuki, N., and Yoshikuni, M. (2000). Identifi cation and cDNA cloning of alveolin, an extracellular metalloproteinase, which induces chorion hardening of medaka (Oryzias latipes) eggs upon fertilization. J. Biol. Chem. 275, 8349-8354.
    • (2000) J. Biol. Chem. , vol.275 , pp. 8349-8354
    • Shibata, Y.1    Iwamatsu, T.2    Oba, Y.3    Kobayashi, D.4    Tanaka, M.5    Nagahama, Y.6    Suzuki, N.7    Yoshikuni, M.8
  • 76
    • 0025986820 scopus 로고
    • The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1
    • Shimell, M.J., Ferguson, E.L., Childs, S.R., and O' Connor, M.B. (1991). The Drosophila dorsal-ventral patterning gene tolloid is related to human bone morphogenetic protein 1. Cell 67, 469-481.
    • (1991) Cell , vol.67 , pp. 469-481
    • Shimell, M.J.1    Ferguson, E.L.2    Childs, S.R.3    O'Connor, M.B.4
  • 77
    • 0034724260 scopus 로고    scopus 로고
    • Structure and function of procollagen C-proteinase (mTolloid) domains determined by protease digestion, circular dichroism, binding to procollagen type I, and computer modeling
    • Sieron, A.L., Tretiakova, A., Jameson, B.A., Segall, M.L., Lund- Katz, S., Khan, M.T., Li, S.W., and Stöcker, W. (2000). Structure and function of procollagen C-proteinase (mTolloid) domains determined by protease digestion, circular dichroism, binding to procollagen type I, and computer modeling. Biochemistry 39, 3231-3239.
    • (2000) Biochemistry , vol.39 , pp. 3231-3239
    • Sieron, A.L.1    Tretiakova, A.2    Jameson, B.A.3    Segall, M.L.4    Lund- Katz, S.5    Khan, M.T.6    Li, S.W.7    St Cker, Ö.W.8
  • 79
    • 52949132216 scopus 로고    scopus 로고
    • Meprins, membrane- bound and secreted astacin metalloproteinases
    • Sterchi, E.E., Stöcker, W., and Bond, J.S. (2008). Meprins, membrane- bound and secreted astacin metalloproteinases. Mol. Aspects Med. 29, 309-328.
    • (2008) Mol. Aspects Med. , vol.29 , pp. 309-328
    • Sterchi, E.E.1    St Cker, Ö.W.2    Bond, J.S.3
  • 80
    • 0029095760 scopus 로고
    • Structural features of a superfamily of zinc-endopeptidases: The metzincins
    • Stöcker, W. and Bode, W. (1995). Structural features of a superfamily of zinc-endopeptidases: the metzincins. Curr. Opin. Struct. Biol. 5, 383-390.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 383-390
    • St Cker, Ö.W.1    Bode, W.2
  • 82
    • 0024996696 scopus 로고
    • Fluorescent oligopeptide substrates for kinetic characterization of the specifi city of Astacus protease
    • Stöcker, W., Ng, M., and Auld, D.S. (1990). Fluorescent oligopeptide substrates for kinetic characterization of the specifi city of Astacus protease. Biochemistry 29, 10418-10425.
    • (1990) Biochemistry , vol.29 , pp. 10418-10425
    • St Cker, Ö.W.1    Ng, M.2    Auld, D.S.3
  • 83
    • 0026041499 scopus 로고
    • α2-Macroglobulin from hemolymph of the freshwater crayfi sh Astacus astacus. Comp. Biochem. Physiol
    • Stöcker, W., Breit, S., Sottrup-Jensen, L., and Zwilling, R. (1991a). α2 -Macroglobulin from hemolymph of the freshwater crayfi sh Astacus astacus . Comp. Biochem. Physiol., Part B: Biochem. Mol. Biol. 98, 501-509.
    • (1991) Biochem. Mol. Biol. , vol.98 , pp. 501-509
    • St Cker, Ö.W.1    Breit, S.2    Sottrup-Jensen, L.3    Zwilling, R.4
  • 85
    • 0027287308 scopus 로고
    • Implications of the three-dimensional structure of astacin for the structure and function of the astacin-family of zinc-endopeptidases
    • Stöcker, W., Gomis-Rüth, F.X., Bode, W., and Zwilling, R. (1993). Implications of the three-dimensional structure of astacin for the structure and function of the astacin-family of zinc-endopeptidases. Eur. J. Biochem. 214, 215-231.
    • (1993) Eur. J. Biochem. , vol.214 , pp. 215-231
    • St Cker, Ö.W.1    Gomis-Ruth, F.X.2    Bode, W.3    Zwilling, R.4
  • 86
    • 0028969678 scopus 로고
    • The metzincins - Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) defi ne a superfamily of zinc-peptidases
    • Stöcker, W., Grams, F., Baumann, U., Reinemer, P., Gomis-Rüth, F.X., McKay, D.B., and Bode, W. (1995). The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) defi ne a superfamily of zinc-peptidases. Protein Sci. 4, 823-840.
    • (1995) Protein Sci. , vol.4 , pp. 823-840
    • St Cker, Ö.W.1    Grams, F.2    Baumann, U.3    Reinemer, P.4    Gomis-Ruth, F.X.5    McKay, D.B.6    Bode, W.7
  • 87
    • 63649149047 scopus 로고    scopus 로고
    • Three-dimensional domain architecture of the ADAM family proteinases
    • Takeda, S. (2009). Three-dimensional domain architecture of the ADAM family proteinases. Semin. Cell Dev. Biol. 20, 146-152.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 146-152
    • Takeda, S.1
  • 88
    • 82755161763 scopus 로고    scopus 로고
    • Snake venom metalloproteinases: Structure, function and relevance to the mammalian ADAM/ADAMTS family proteins
    • Takeda, S., Takeya, H., and Iwanaga, S. (2012). Snake venom metalloproteinases: structure, function and relevance to the mammalian ADAM/ADAMTS family proteins. Biochim. Biophys. Acta 1824, 164-176.
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 164-176
    • Takeda, S.1    Takeya, H.2    Iwanaga, S.3
  • 89
    • 33745837768 scopus 로고    scopus 로고
    • Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases
    • Tallant, C., Garc í a-Castellanos, R., Seco, J., Baumann, U., and Gomis-Rüth, F.X. (2006). Molecular analysis of ulilysin, the structural prototype of a new family of metzincin metalloproteases. J. Biol. Chem. 281, 17920-17928.
    • (2006) J. Biol. Chem. , vol.281 , pp. 17920-17928
    • Tallant, C.1    Garcia-Castellanos, R.2    Seco, J.3    Baumann, U.4    Gomis-Ruth, F.X.5
  • 91
    • 77149154385 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Fold and function of their catalytic domains. Biochim. Biophys. Acta
    • Tallant, C., Marrero, A., and Gomis-Rüth, F.X. (2010b). Matrix metalloproteinases: fold and function of their catalytic domains. Biochim. Biophys. Acta, Mol. Cell Res. 1803, 20-28.
    • (2010) Mol. Cell Res. , vol.1803 , pp. 20-28
    • Tallant, C.1    Marrero, A.2    Gomis-Ruth, F.X.3
  • 92
    • 0025906404 scopus 로고
    • Threedimensional structure of the elastase of Pseudomonas aeruginosa at 1.5- Å resolution
    • Thayer, M.M., Flaherty, K.M., and McKay, D.B. (1991). Threedimensional structure of the elastase of Pseudomonas aeruginosa at 1.5- Å resolution. J. Biol. Chem. 266, 2864-2871.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2864-2871
    • Thayer, M.M.1    Flaherty, K.M.2    McKay, D.B.3
  • 94
    • 1642483564 scopus 로고    scopus 로고
    • Purifi cation and cloning of an endogenous protein inhibitor of carp nephrosin, an astacin metalloproteinase
    • Tsai, P.L., Chen, C.H., Huang, C.J., Chou, C.M., and Chang, G.D. (2004). Purifi cation and cloning of an endogenous protein inhibitor of carp nephrosin, an astacin metalloproteinase. J. Biol. Chem. 279, 11146-11155.
    • (2004) J. Biol. Chem. , vol.279 , pp. 11146-11155
    • Tsai, P.L.1    Chen, C.H.2    Huang, C.J.3    Chou, C.M.4    Chang, G.D.5
  • 96
    • 27644534995 scopus 로고    scopus 로고
    • Nonnatural amino acid incorporation into the methionine 214 position of the metzincin Pseudomonas aeruginosa alkaline protease
    • Walasek, P. and Honek, J.F. (2005). Nonnatural amino acid incorporation into the methionine 214 position of the metzincin Pseudomonas aeruginosa alkaline protease. BMC Biochem. 6, 21.
    • (2005) BMC Biochem. , vol.6 , pp. 21
    • Walasek, P.1    Honek, J.F.2
  • 97
    • 77955832351 scopus 로고    scopus 로고
    • Crystal structure of archaemetzincin AmzA from Methanopyrus kandleri at 1.5 Å resolution
    • Waltersperger, S., Widmer, C., Wang, M., and Baumann, U. (2010). Crystal structure of archaemetzincin AmzA from Methanopyrus kandleri at 1.5 Å resolution. Proteins 78, 2720-2723.
    • (2010) Proteins , vol.78 , pp. 2720-2723
    • Waltersperger, S.1    Widmer, C.2    Wang, M.3    Baumann, U.4
  • 98
    • 34249022942 scopus 로고    scopus 로고
    • The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains
    • Wermter, C., Höwel, M., Hintze, V., Bombosch, B., Aufenvenne, K., Yiallouros, I., and Stöcker, W. (2007). The protease domain of procollagen C-proteinase (BMP1) lacks substrate selectivity, which is conferred by non-proteolytic domains. Biol. Chem. 388, 513-521.
    • (2007) Biol. Chem. , vol.388 , pp. 513-521
    • Wermter, C.1    Howel, M.2    Hintze, V.3    Bombosch, B.4    Aufenvenne, K.5    Yiallouros, I.6    Stocker, W.7
  • 99
    • 0027431501 scopus 로고
    • The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: Structural, functional, and evolutionary implications
    • Wolfsberg, T., Bazan, J., Blobel, C., Myles, D., Primakoff, P., and White, J. (1993). The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications. Proc. Natl. Acad. Sci. USA 90, 10783-10787.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10783-10787
    • Wolfsberg, T.1    Bazan, J.2    Blobel, C.3    Myles, D.4    Primakoff, P.5    White, J.6
  • 101
    • 0033959339 scopus 로고    scopus 로고
    • Identifi cation and characterization of hydra metalloproteinase 2 (HMP2): A meprin-like astacin metalloproteinase that functions in foot morphogenesis
    • Yan, L., Fei, K., Zhang, J., Dexter, S., and Sarras, M.P. Jr. (2000a). Identifi cation and characterization of hydra metalloproteinase 2 (HMP2): a meprin-like astacin metalloproteinase that functions in foot morphogenesis. Development 127, 129-141.
    • (2000) Development , vol.127 , pp. 129-141
    • Yan, L.1    Fei, K.2    Zhang, J.3    Dexter, S.4    Sarras Jr., M.P.5
  • 102
    • 0034163284 scopus 로고    scopus 로고
    • Hydra metalloproteinase 1: A secreted astacin metalloproteinase whose apical axis expression is differentially regulated during head regeneration
    • Yan, L., Leontovich, A., Fei, K., and Sarras, M.P. Jr. (2000b). Hydra metalloproteinase 1: a secreted astacin metalloproteinase whose apical axis expression is differentially regulated during head regeneration. Dev. Biol. 219, 115-128.
    • (2000) Dev. Biol. , vol.219 , pp. 115-128
    • Yan, L.1    Leontovich, A.2    Fei, K.3    Sarras Jr., M.P.4
  • 103
    • 0026697681 scopus 로고
    • Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development
    • Yasumasu, S., Yamada, K., Akasaka, K., Mitsunaga, K., Iuchi, I., Shimada, H., and Yamagami, K. (1992). Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development. Dev. Biol. 153, 250-258.
    • (1992) Dev. Biol. , vol.153 , pp. 250-258
    • Yasumasu, S.1    Yamada, K.2    Akasaka, K.3    Mitsunaga, K.4    Iuchi, I.5    Shimada, H.6    Yamagami, K.7
  • 104
    • 0030012873 scopus 로고    scopus 로고
    • Different exon-intron organizations of the genes for two astacin-like proteases, high choriolytic enzyme (choriolysin H) and low choriolytic enzyme (choriolysin L), the constituents of the fi sh hatching enzyme
    • Yasumasu, S., Shimada, H., Inohaya, K., Yamazaki, K., Iuchi, I., Yasumasu, I., and Yamagami, K. (1996). Different exon-intron organizations of the genes for two astacin-like proteases, high choriolytic enzyme (choriolysin H) and low choriolytic enzyme (choriolysin L), the constituents of the fi sh hatching enzyme. Eur. J. Biochem. 237, 752-758.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 752-758
    • Yasumasu, S.1    Shimada, H.2    Inohaya, K.3    Yamazaki, K.4    Iuchi, I.5    Yasumasu, I.6    Yamagami, K.7
  • 105
    • 0034634473 scopus 로고    scopus 로고
    • The roles of Glu93 and Tyr149 in astacin-like zinc peptidases
    • Yiallouros, I., Grosse-Berkhoff, E., and Stöcker, W. (2000). The roles of Glu93 and Tyr149 in astacin-like zinc peptidases. FEBS Lett. 484, 224-228.
    • (2000) Febs Lett. , vol.484 , pp. 224-228
    • Yiallouros, I.1    Grosse-Berkhoff, E.2    St Cker, Ö.W.3
  • 106
  • 107
    • 0035968303 scopus 로고    scopus 로고
    • A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains
    • Zapata, J.M., Pawlowski, K., Haas, E., Ware, C.F., Godzik, A., and Reed, J.C. (2001). A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains. J. Biol. Chem. 276, 24242-24252.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24242-24252
    • Zapata, J.M.1    Pawlowski, K.2    Haas, E.3    Ware, C.F.4    Godzik, A.5    Reed, J.C.6
  • 108
    • 33845967114 scopus 로고    scopus 로고
    • Inhibition of bone morphogenetic protein 1 by native and altered forms of α2 - Macroglobulin
    • Zhang, Y., Ge, G., and Greenspan, D.S. (2006). Inhibition of bone morphogenetic protein 1 by native and altered forms of α2 - macroglobulin. J. Biol. Chem. 281, 39096-39104.
    • (2006) J. Biol. Chem. , vol.281 , pp. 39096-39104
    • Zhang, Y.1    Ge, G.2    Greenspan, D.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.