메뉴 건너뛰기




Volumn 259, Issue 3, 1999, Pages 815-820

Studies on the formation and stability of a complex between Streptomyces proteinaceous metalloprotease inhibitor and thermolysin

Author keywords

Electrostatic interactions; Ionic strength; K(i); Streptomyces proteinaceous metalloprotease inhibitor (SMPI); Thermolysin

Indexed keywords

METALLOPROTEINASE INHIBITOR; THERMOLYSIN;

EID: 0033082333     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00103.x     Document Type: Article
Times cited : (4)

References (41)
  • 3
    • 0028641280 scopus 로고
    • Treatment of destructive disorders with MMP inhibitors
    • 3. Greenwald, R.A. (1994) Treatment of destructive disorders with MMP inhibitors. Ann. New York Acad. Sci. 732, 181-198.
    • (1994) Ann. New York Acad. Sci. , vol.732 , pp. 181-198
    • Greenwald, R.A.1
  • 6
    • 0018785906 scopus 로고
    • Purification and properties of a proteinaceous metallo-proteinase inhibitor from Streptomyces nigrescens TK-23
    • 6. Oda, K., Koyama, T. & Murao, S. (1979) Purification and properties of a proteinaceous metallo-proteinase inhibitor from Streptomyces nigrescens TK-23. Biochim. Biophys. Acta 571, 147-156.
    • (1979) Biochim. Biophys. Acta , vol.571 , pp. 147-156
    • Oda, K.1    Koyama, T.2    Murao, S.3
  • 7
    • 0021905124 scopus 로고
    • Amino acid sequence of Streptomyces metallo-proteinase inhibitor from Streptomyces nigrescens TK-23
    • 7. Murai, H., Hara, S., Ikenaka, T., Oda, K. & Murao, S. (1985) Amino acid sequence of Streptomyces metallo-proteinase inhibitor from Streptomyces nigrescens TK-23. J. Biochem. (Tokyo) 97, 173-180.
    • (1985) J. Biochem. (Tokyo) , vol.97 , pp. 173-180
    • Murai, H.1    Hara, S.2    Ikenaka, T.3    Oda, K.4    Murao, S.5
  • 8
    • 0024455802 scopus 로고
    • Characterization of a protein inhibitor of extracellular proteases produced by Erwinia chrysanthmi
    • 8. Letoffe, S., Delepelaire, P. & Wandersman, C. (1989) Characterization of a protein inhibitor of extracellular proteases produced by Erwinia chrysanthmi. Mol. Microbiol. 3, 79-180.
    • (1989) Mol. Microbiol. , vol.3 , pp. 79-180
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 9
    • 0026451216 scopus 로고
    • Families of metalloendopeptidases and their relationships
    • 9. Jiang, W. & Bond, J.S. (1992) Families of metalloendopeptidases and their relationships. FEBS Lett. 312, 110-114.
    • (1992) FEBS Lett. , vol.312 , pp. 110-114
    • Jiang, W.1    Bond, J.S.2
  • 10
    • 0026475721 scopus 로고
    • Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosu: Relationship to other secretory pathways
    • 10. Dugong, F., Lazdunski, A., Cami, B. & Murgier, M. (1992) Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosu: relationship to other secretory pathways. Gene 121, 47-54.
    • (1992) Gene , vol.121 , pp. 47-54
    • Dugong, F.1    Lazdunski, A.2    Cami, B.3    Murgier, M.4
  • 11
    • 0026560394 scopus 로고
    • Production of active Serratia marcescens metalloprotease from Escherichia coli by α-hemolysis HlyB and HlyD
    • 11. Suh, Y. & Benedik, M.J. (1992) Production of active Serratia marcescens metalloprotease from Escherichia coli by α-hemolysis HlyB and HlyD. J. Bacteriol. 174, 2361-2366.
    • (1992) J. Bacteriol. , vol.174 , pp. 2361-2366
    • Suh, Y.1    Benedik, M.J.2
  • 12
    • 0030873066 scopus 로고    scopus 로고
    • Identification of reactive site of a proteinaceous metalloproteinase inhibitor from Streptomyces nigrescens TK-23
    • 12. Seeram, S.S., Hiraga, K., Saji, A., Tashiro, M. & Oda, K. (1997) Identification of reactive site of a proteinaceous metalloproteinase inhibitor from Streptomyces nigrescens TK-23. J. Biochem. (Tokyo) 121, 1088-1095.
    • (1997) J. Biochem. (Tokyo) , vol.121 , pp. 1088-1095
    • Seeram, S.S.1    Hiraga, K.2    Saji, A.3    Tashiro, M.4    Oda, K.5
  • 13
    • 0030699083 scopus 로고    scopus 로고
    • Resynthesis of reactive site peptide bond and temporary inhibition of Streptomyces metalloproteinase inhibitor
    • 13. Seeram, S.S., Hiraga, K. & Oda, K. (1997) Resynthesis of reactive site peptide bond and temporary inhibition of Streptomyces metalloproteinase inhibitor. J. Biochem. (Tokyo) 122, 788-794.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 788-794
    • Seeram, S.S.1    Hiraga, K.2    Oda, K.3
  • 15
    • 0032544292 scopus 로고    scopus 로고
    • NMR structure of streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23 -another example of ancestral βγ-crystallin precursor structure
    • 15. Ohno, A., Tate, S., Seeram, S.S., Hiraga, K., Swindells, M.B., Oda, K. & Kainosho, M. (1998) NMR structure of Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23 -another example of ancestral βγ-crystallin precursor structure. J. Mol. Biol. 282, 421-433.
    • (1998) J. Mol. Biol. , vol.282 , pp. 421-433
    • Ohno, A.1    Tate, S.2    Seeram, S.S.3    Hiraga, K.4    Swindells, M.B.5    Oda, K.6    Kainosho, M.7
  • 16
    • 0032544663 scopus 로고    scopus 로고
    • Elucidation of the mode of interaction of a proteinaceous metalloproteinase inhibitor, SMPI, with thermolysin by computer modeling with the NMR derived inhibitor structure
    • 16. Tate, S., Ohno, A., Seeram, S.S., Hiraga, K., Oda, K. & Kainosho, M. (1998) Elucidation of the mode of interaction of a proteinaceous metalloproteinase inhibitor, SMPI, with thermolysin by computer modeling with the NMR derived inhibitor structure. J. Mol. Biol. 282, 435-446.
    • (1998) J. Mol. Biol. , vol.282 , pp. 435-446
    • Tate, S.1    Ohno, A.2    Seeram, S.S.3    Hiraga, K.4    Oda, K.5    Kainosho, M.6
  • 17
    • 0020130996 scopus 로고
    • pH and temperature dependences of thermolysin catalysis: Catalytic role of zinc-coordinated water
    • 17. Kunugi, S., Hirohara, H. & Ise, N. (1982) pH and temperature dependences of thermolysin catalysis: catalytic role of zinc-coordinated water. Eur. J. Biochem. 124, 157-163.
    • (1982) Eur. J. Biochem. , vol.124 , pp. 157-163
    • Kunugi, S.1    Hirohara, H.2    Ise, N.3
  • 19
    • 0001308793 scopus 로고
    • Kinetics of the peptide formation catalyzed by thermolysin in a homogeneous aqueous-organic system
    • 19. Kunugi, S., Suzuki, N., Sakamoto, A. & Yoshida, M. (1995a) Kinetics of the peptide formation catalyzed by thermolysin in a homogeneous aqueous-organic system. Bull. Chem. Soc. Jpn. 68, 1019-1023.
    • (1995) Bull. Chem. Soc. Jpn. , vol.68 , pp. 1019-1023
    • Kunugi, S.1    Suzuki, N.2    Sakamoto, A.3    Yoshida, M.4
  • 20
    • 0028938857 scopus 로고
    • Observation of the pre-steady state process in thermolysin catalysis with a fluorescent displacement probe at low pH
    • 20. Kunugi, S., Yokoyama, M. & Sakamoto, A. (1995b) Observation of the pre-steady state process in thermolysin catalysis with a fluorescent displacement probe at low pH. FEBS Lett. 362, 189-191.
    • (1995) FEBS Lett. , vol.362 , pp. 189-191
    • Kunugi, S.1    Yokoyama, M.2    Sakamoto, A.3
  • 21
    • 0013622002 scopus 로고    scopus 로고
    • Intermediate formation process in thermolysin catalysis observed using a fluorescent displacement probe in the stopped-flow method
    • 21. Kunugi, S., Yokoyama, M., Kuroda, Y., Yoshida, M., Koyasu, A., Yamada, T. & Sakamoto, A. (1996a) Intermediate formation process in thermolysin catalysis observed using a fluorescent displacement probe in the stopped-flow method. Bull. Chem. Soc. Jpn. 69, 1747-1753.
    • (1996) Bull. Chem. Soc. Jpn. , vol.69 , pp. 1747-1753
    • Kunugi, S.1    Yokoyama, M.2    Kuroda, Y.3    Yoshida, M.4    Koyasu, A.5    Yamada, T.6    Sakamoto, A.7
  • 22
    • 0029858288 scopus 로고    scopus 로고
    • Kinetic characterization of the neutral protease vimelysin from Vibrio sp. T1800
    • 22. Kunugi, S., Koyasu, A., Kitayaki, M., Takahashi, S. & Oda, K. (1996b) Kinetic characterization of the neutral protease vimelysin from Vibrio sp. T1800. Eur. J. Biochem. 241, 368-373.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 368-373
    • Kunugi, S.1    Koyasu, A.2    Kitayaki, M.3    Takahashi, S.4    Oda, K.5
  • 24
    • 0000518309 scopus 로고    scopus 로고
    • Kinetics of a thermolysin-catalyzed peptide formation reaction in acetonitrile-water
    • 24. Kunugi, S. & Yoshida, M. (1996) Kinetics of a thermolysin-catalyzed peptide formation reaction in acetonitrile-water. Bull. Chem. Soc. Jpn. 69, 805-809.
    • (1996) Bull. Chem. Soc. Jpn. , vol.69 , pp. 805-809
    • Kunugi, S.1    Yoshida, M.2
  • 25
    • 0000372387 scopus 로고
    • Pressure dependence of carboxypeptidase A action
    • 25. Fukuda, M., Kunugi, S. & Ise, N. (1983) Pressure dependence of carboxypeptidase A action. Bull. Chem. Soc. Jpn. 56, 3308-3313.
    • (1983) Bull. Chem. Soc. Jpn. , vol.56 , pp. 3308-3313
    • Fukuda, M.1    Kunugi, S.2    Ise, N.3
  • 26
    • 0001618238 scopus 로고
    • Pressure dependence of L-leucine-p-nitroanilide hydrolysis by leucine aminopeptidase
    • 26. Fukuda, M., Shima, H. & Kunugi, S. (1985) Pressure dependence of L-leucine-p-nitroanilide hydrolysis by leucine aminopeptidase. Bull. Chem. Soc Jpn. 58, 1349-1350.
    • (1985) Bull. Chem. Soc Jpn. , vol.58 , pp. 1349-1350
    • Fukuda, M.1    Shima, H.2    Kunugi, S.3
  • 27
    • 0021473029 scopus 로고
    • Pressure dependence of thermolysin catalysis
    • 27. Fukuda, M. & Kunugi, S. (1984a) Pressure dependence of thermolysin catalysis. Eur. J. Biochem. 142, 565-570.
    • (1984) Eur. J. Biochem. , vol.142 , pp. 565-570
    • Fukuda, M.1    Kunugi, S.2
  • 28
    • 0013598966 scopus 로고
    • Mechanism of dipeptidyl carboxypeptidase activity of thermolysin
    • 28. Fukuda, M. & Kunugi, S. (1984b) Mechanism of dipeptidyl carboxypeptidase activity of thermolysin. Bull. Chem. Soc. Jpn. 57, 2965-2970.
    • (1984) Bull. Chem. Soc. Jpn. , vol.57 , pp. 2965-2970
    • Fukuda, M.1    Kunugi, S.2
  • 29
    • 0000260537 scopus 로고
    • Modification of biopolymer functions by high pressure
    • 29. Kunugi, S. (1993) Modification of biopolymer functions by high pressure. Prog. Polymer Sci. 18, 805-838.
    • (1993) Prog. Polymer Sci. , vol.18 , pp. 805-838
    • Kunugi, S.1
  • 30
    • 0026505650 scopus 로고
    • A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases
    • 30. Knight, C.G., Willenbrock, F. & Murphy, G. (1992) A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases. FEBS Lett. 296, 263-266.
    • (1992) FEBS Lett. , vol.296 , pp. 263-266
    • Knight, C.G.1    Willenbrock, F.2    Murphy, G.3
  • 32
    • 0016619961 scopus 로고
    • Studies on inhibitory effect of phosphoramidon and its analogs on thermolysin
    • 32. Komiyama, T., Suda, H., Aoyagi, T., Takeuchi, T. & Umezawa, H. (1975) Studies on inhibitory effect of phosphoramidon and its analogs on thermolysin. Arch. Biochem. Biophys. 171, 727-731.
    • (1975) Arch. Biochem. Biophys. , vol.171 , pp. 727-731
    • Komiyama, T.1    Suda, H.2    Aoyagi, T.3    Takeuchi, T.4    Umezawa, H.5
  • 35
    • 0015506348 scopus 로고
    • The structure of thermolysin: An electron density map at 2.3 Å resolution
    • 35. Colman, P.M., Jansonius, J.N. & Matthews, B.W. (1972) The structure of thermolysin: an electron density map at 2.3 Å resolution. J. Mol. Biol. 70, 701-724.
    • (1972) J. Mol. Biol , vol.70 , pp. 701-724
    • Colman, P.M.1    Jansonius, J.N.2    Matthews, B.W.3
  • 36
    • 0023839658 scopus 로고
    • The binding of L-valyl-L-tryptophan to the crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis
    • 36. Holden, H.M. & Matthews, B.W. (1988) The binding of L-valyl-L-tryptophan to the crystalline thermolysin illustrates the mode of interaction of a product of peptide hydrolysis. J. Biol. Chem. 263, 3256-3260.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3256-3260
    • Holden, H.M.1    Matthews, B.W.2
  • 37
    • 0020017199 scopus 로고
    • High pressure effects on proteins and other biomolecules
    • 37. Heremans, K. (1982) High pressure effects on proteins and other biomolecules. Annu. Rev. Biophys. Bioeng. 11, 1-21.
    • (1982) Annu. Rev. Biophys. Bioeng. , vol.11 , pp. 1-21
    • Heremans, K.1
  • 38
    • 0001094555 scopus 로고
    • Studies on protease produced by thermophilic bacteria
    • 38. Endo, S. (1962) Studies on protease produced by thermophilic bacteria. J. Ferment. Technol. 40, 346-353.
    • (1962) J. Ferment. Technol. , vol.40 , pp. 346-353
    • Endo, S.1
  • 39
    • 0017400132 scopus 로고
    • A crystallographic study on the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substrates
    • 39. Weaver, L.H., Kester, W.R. & Matthews, B.W. (1977) A crystallographic study on the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substrates. J. Mol. Biol. 114, 119-132.
    • (1977) J. Mol. Biol. , vol.114 , pp. 119-132
    • Weaver, L.H.1    Kester, W.R.2    Matthews, B.W.3
  • 40
    • 0023667724 scopus 로고
    • Slow-and fast-binding inhibitors of thermolysin display different modes of binding: Crystallographic analysis of extended phosphonamidate transition-state analogues
    • 40. Holden, H.M., Tronrud, D.E., Monzing, A.F., Weaver, L.H. & Matthews, B.W. (1987) Slow-and fast-binding inhibitors of thermolysin display different modes of binding: crystallographic analysis of extended phosphonamidate transition-state analogues. Biochemistry 26, 8542-8553.
    • (1987) Biochemistry , vol.26 , pp. 8542-8553
    • Holden, H.M.1    Tronrud, D.E.2    Monzing, A.F.3    Weaver, L.H.M.B.W.4
  • 41
    • 0026489329 scopus 로고
    • Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis
    • 41. Holland, D.R., Tronrud, D.E., Pley, H.W., Flaherty, K.M., Stark, W., Jansonius, J.N., McKay, D.B. & 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.