메뉴 건너뛰기




Volumn 390, Issue 1, 2009, Pages 11-18

Biochemical characterization of the catalytic domains of three different clostridial collagenases

Author keywords

Clostridium histolyticum; Clostridium tetani; Enzymatic mechanism; FALGPA; Inhibition; Zinc metalloprotease

Indexed keywords

1,10 PHENANTHROLINE; AMINO TERMINAL TELOPEPTIDE; COLLAGENASE; COLLAGENASE G; COLLAGENASE H; COLLAGENASE T; UNCLASSIFIED DRUG;

EID: 58249106774     PISSN: 14316730     EISSN: 14374315     Source Type: Journal    
DOI: 10.1515/BC.2009.004     Document Type: Article
Times cited : (41)

References (40)
  • 2
    • 0024293209 scopus 로고
    • Preparation and reconstitution with divalent metal ions of class I and class II Clostridium histolyticum apocollagenases
    • Angleton, E.L. and Van Wart, H.E. (1988). Preparation and reconstitution with divalent metal ions of class I and class II Clostridium histolyticum apocollagenases. Biochemistry 27, 7406-7412.
    • (1988) Biochemistry , vol.27 , pp. 7406-7412
    • Angleton, E.L.1    Van Wart, H.E.2
  • 4
    • 0021766908 scopus 로고
    • Purification and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatography
    • Bond, M.D. and Van Wart, H.E. (1984a). Purification and separation of individual collagenases of Clostridium histolyticum using red dye ligand chromatography. Biochemistry 23, 3077-3085.
    • (1984) Biochemistry , vol.23 , pp. 3077-3085
    • Bond, M.D.1    Van Wart, H.E.2
  • 5
    • 0021766906 scopus 로고
    • Characterization of the individual collagenases from Clostridium histolyticum
    • Bond, M.D. and Van Wart, H.E. (1984b). Characterization of the individual collagenases from Clostridium histolyticum. Biochemistry 23, 3085-3091.
    • (1984) Biochemistry , vol.23 , pp. 3085-3091
    • Bond, M.D.1    Van Wart, H.E.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0035907237 scopus 로고    scopus 로고
    • The 1.8-Å crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition
    • Brandstetter, H., Grams, F., Glitz, D., Lang, A., Huber, R., Bode, W., Krell, H.W., and Engh, R.A. (2001). The 1.8-Å crystal structure of a matrix metalloproteinase 8-barbiturate inhibitor complex reveals a previously unobserved mechanism for collagenase substrate recognition. J. Biol. Chem. 276, 17405-17412.
    • (2001) J. Biol. Chem , vol.276 , pp. 17405-17412
    • Brandstetter, H.1    Grams, F.2    Glitz, D.3    Lang, A.4    Huber, R.5    Bode, W.6    Krell, H.W.7    Engh, R.A.8
  • 10
    • 0000860810 scopus 로고
    • Genus Clostridium. Prazmowski, 1880, 23AL
    • P.H.A. Sneath, N.S. Mair, M.E. Sharpe and J.G. Holt, eds, Baltimore, MD, USA: The Williams & Wilkins Co, pp
    • Cato, E.P., George, W.L., and Finegold, S.M. (1986). Genus Clostridium. Prazmowski, 1880, 23AL. In: Bergey's Manual of Systematic Bacteriology, Vol. 2, P.H.A. Sneath, N.S. Mair, M.E. Sharpe and J.G. Holt, eds. (Baltimore, MD, USA: The Williams & Wilkins Co.), pp. 1141-1200.
    • (1986) Bergey's Manual of Systematic Bacteriology , vol.2 , pp. 1141-1200
    • Cato, E.P.1    George, W.L.2    Finegold, S.M.3
  • 11
    • 43049136620 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum
    • Eckhard, U., Nüss, D., Ducka, P., Schönauer, E., and Brandstetter, H. (2008). Crystallization and preliminary X-ray characterization of the catalytic domain of collagenase G from Clostridium histolyticum. Acta Crystallogr. F Struct. Biol. Cryst. Commun. 64, 419-421.
    • (2008) Acta Crystallogr. F Struct. Biol. Cryst. Commun , vol.64 , pp. 419-421
    • Eckhard, U.1    Nüss, D.2    Ducka, P.3    Schönauer, E.4    Brandstetter, H.5
  • 12
    • 0033151775 scopus 로고    scopus 로고
    • The N-terminus of collagenase MMP-8 determines superactivity and inhibition: A relation of structure and function analyzed by biomolecular interaction analysis
    • Farr, M., Pieper, M., Calvete, J., and Tschesche, H. (1999). The N-terminus of collagenase MMP-8 determines superactivity and inhibition: a relation of structure and function analyzed by biomolecular interaction analysis. Biochemistry 38, 7332-7338.
    • (1999) Biochemistry , vol.38 , pp. 7332-7338
    • Farr, M.1    Pieper, M.2    Calvete, J.3    Tschesche, H.4
  • 13
    • 0031868477 scopus 로고    scopus 로고
    • The potential of collagenase as a new therapy for separation of human retained placenta: Hydrolytic potency on human, equine and bovine placentae
    • Fecteau, K.A., Haffner, J.C., and Eiler, H. (1998). The potential of collagenase as a new therapy for separation of human retained placenta: hydrolytic potency on human, equine and bovine placentae. Placenta 19, 379-383.
    • (1998) Placenta , vol.19 , pp. 379-383
    • Fecteau, K.A.1    Haffner, J.C.2    Eiler, H.3
  • 14
    • 0000771267 scopus 로고    scopus 로고
    • Equine retained placenta: Technique for and tolerance to umbilical artery injections of collagenase
    • Haffner, J.C., Fecteau, K.A., Held, J.P., and Eiler, H. (1998). Equine retained placenta: technique for and tolerance to umbilical artery injections of collagenase. Theriogenology 49, 711-716.
    • (1998) Theriogenology , vol.49 , pp. 711-716
    • Haffner, J.C.1    Fecteau, K.A.2    Held, J.P.3    Eiler, H.4
  • 16
    • 0031856715 scopus 로고    scopus 로고
    • An EXCEL template for calculation of enzyme kinetic parameters by non-linear regression
    • Hernandez, A. and Ruiz, M.T. (1998). An EXCEL template for calculation of enzyme kinetic parameters by non-linear regression. Bioinformatics 14, 227-228.
    • (1998) Bioinformatics , vol.14 , pp. 227-228
    • Hernandez, A.1    Ruiz, M.T.2
  • 17
    • 0029557952 scopus 로고
    • Recombinant enzymes for islet isolation: Purification of a collagenase from Clostridium histolyticum and cloning/expression of the gene
    • Hesse, F., Burtscher, H., Popp, F., and Ambrosius, D. (1995). Recombinant enzymes for islet isolation: purification of a collagenase from Clostridium histolyticum and cloning/expression of the gene. Transplant. Proc. 27, 3287-3289.
    • (1995) Transplant. Proc , vol.27 , pp. 3287-3289
    • Hesse, F.1    Burtscher, H.2    Popp, F.3    Ambrosius, D.4
  • 18
    • 0037041031 scopus 로고    scopus 로고
    • Rapid determination of substrate specificity of Clostridium histolyticum β-collagenase using an immobilized peptide library
    • Hu, Y., Webb, E., Singh, J., Morgan, B.A., Gainor, J.A., Gordon, T.D., and Siahaan, T.J. (2002). Rapid determination of substrate specificity of Clostridium histolyticum β-collagenase using an immobilized peptide library. J. Biol. Chem. 277, 8366-8371.
    • (2002) J. Biol. Chem , vol.277 , pp. 8366-8371
    • Hu, Y.1    Webb, E.2    Singh, J.3    Morgan, B.A.4    Gainor, J.A.5    Gordon, T.D.6    Siahaan, T.J.7
  • 19
    • 0032947997 scopus 로고    scopus 로고
    • Identification of metal ligands in the Clostridium histolyticum ColH collagenase
    • Jung, C.M., Matsushita, O., Katayama, S., Minami, J., Sakurai, J., and Okabe, A. (1999). Identification of metal ligands in the Clostridium histolyticum ColH collagenase. J. Bacteriol. 181, 2816-2822.
    • (1999) J. Bacteriol , vol.181 , pp. 2816-2822
    • Jung, C.M.1    Matsushita, O.2    Katayama, S.3    Minami, J.4    Sakurai, J.5    Okabe, A.6
  • 20
    • 36448991500 scopus 로고    scopus 로고
    • Larkin, M.A, Blackshields, G, Brown, N.P, Chenna, R, McGettigan, P.A, McWilliam, H, Valentin, F, Wallace, I.M, Wilm, A, Lopez, R, et al, 2007, Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947-2948
    • Larkin, M.A., Blackshields, G., Brown, N.P., Chenna, R., McGettigan, P.A., McWilliam, H., Valentin, F., Wallace, I.M., Wilm, A., Lopez, R., et al. (2007). Clustal W and Clustal X version 2.0. Bioinformatics 23, 2947-2948.
  • 21
    • 2442499624 scopus 로고    scopus 로고
    • CHOP proteins into structural domain-like fragments
    • Liu, J. and Rost, B. (2004). CHOP proteins into structural domain-like fragments. Proteins 55, 678-688.
    • (2004) Proteins , vol.55 , pp. 678-688
    • Liu, J.1    Rost, B.2
  • 22
    • 0034862658 scopus 로고    scopus 로고
    • Clostridial hydrolytic enzymes degrading extracellular components
    • Matsushita, O. and Okabe, A. (2001). Clostridial hydrolytic enzymes degrading extracellular components. Toxicon 39, 1769-1780.
    • (2001) Toxicon , vol.39 , pp. 1769-1780
    • Matsushita, O.1    Okabe, A.2
  • 23
    • 0028084886 scopus 로고
    • Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene
    • Matsushita, O., Yoshihara, K., Katayama, S., Minami, J., and Okabe, A. (1994). Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene. J. Bacteriol. 176, 149-156.
    • (1994) J. Bacteriol , vol.176 , pp. 149-156
    • Matsushita, O.1    Yoshihara, K.2    Katayama, S.3    Minami, J.4    Okabe, A.5
  • 24
    • 0032891451 scopus 로고    scopus 로고
    • Gene duplication and multiplicity of collagenases in Clostridium histolyticum
    • Matsushita, O., Jung, C.M., Katayama, S., Minami, J., Takahashi, Y., and Okabe, A. (1999). Gene duplication and multiplicity of collagenases in Clostridium histolyticum. J. Bacteriol. 181, 923-933.
    • (1999) J. Bacteriol , vol.181 , pp. 923-933
    • Matsushita, O.1    Jung, C.M.2    Katayama, S.3    Minami, J.4    Takahashi, Y.5    Okabe, A.6
  • 25
    • 0035937822 scopus 로고    scopus 로고
    • Substrate recognition by the collagen-binding domain of Clostridium histolyticum class I collagenase
    • Matsushita, O., Koide, T., Kobayashi, R., Nagata, K., and Okabe, A. (2001). Substrate recognition by the collagen-binding domain of Clostridium histolyticum class I collagenase. J. Biol. Chem. 276, 8761-8770.
    • (2001) J. Biol. Chem , vol.276 , pp. 8761-8770
    • Matsushita, O.1    Koide, T.2    Kobayashi, R.3    Nagata, K.4    Okabe, A.5
  • 26
    • 15544372997 scopus 로고    scopus 로고
    • Alternative treatments for Clostridium difficile disease: What really works?
    • McFarland, L.V. (2005). Alternative treatments for Clostridium difficile disease: what really works? J. Med. Microbiol. 54, 101-111.
    • (2005) J. Med. Microbiol , vol.54 , pp. 101-111
    • McFarland, L.V.1
  • 27
    • 0034810522 scopus 로고    scopus 로고
    • Evidence for antibiotic induced Clostridium perfringens diarrhoea
    • Modi, N. and Wilcox, M.H. (2001). Evidence for antibiotic induced Clostridium perfringens diarrhoea. J. Clin. Pathol. 54, 748-751.
    • (2001) J. Clin. Pathol , vol.54 , pp. 748-751
    • Modi, N.1    Wilcox, M.H.2
  • 28
    • 0034297101 scopus 로고    scopus 로고
    • Matrix metalloproteinases in wound repair
    • Ravanti, L. and Kahari, V.M. (2000). Matrix metalloproteinases in wound repair. Int. J. Mol. Med. 6, 391-407.
    • (2000) Int. J. Mol. Med , vol.6 , pp. 391-407
    • Ravanti, L.1    Kahari, V.M.2
  • 30
    • 0028040070 scopus 로고
    • Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study
    • Reinemer, P., Grams, F., Huber, R., Kleine, T., Schnierer, S., Piper, M., Tschesche, H., and Bode, W. (1994). Structural implications for the role of the N terminus in the 'superactivation' of collagenases. A crystallographic study. FEBS Lett. 338, 227-233.
    • (1994) FEBS Lett , vol.338 , pp. 227-233
    • Reinemer, P.1    Grams, F.2    Huber, R.3    Kleine, T.4    Schnierer, S.5    Piper, M.6    Tschesche, H.7    Bode, W.8
  • 31
    • 0024306575 scopus 로고
    • Increased calcium levels alter cellular and molecular events in wound healing
    • discussion 1147-1148
    • Sank, A., Chi, M., Shima, T., Reich, R., and Martin, G.R. (1989). Increased calcium levels alter cellular and molecular events in wound healing. Surgery 106, 1141-1147; discussion 1147-1148.
    • (1989) Surgery , vol.106 , pp. 1141-1147
    • Sank, A.1    Chi, M.2    Shima, T.3    Reich, R.4    Martin, G.R.5
  • 32
    • 47749093130 scopus 로고    scopus 로고
    • The bacteria fight back
    • Taubes, G. (2008a). The bacteria fight back. Science 321, 356-361.
    • (2008) Science , vol.321 , pp. 356-361
    • Taubes, G.1
  • 33
    • 47749107559 scopus 로고    scopus 로고
    • Collateral damage. The rise of resistant C. difficile
    • Taubes, G. (2008b). Collateral damage. The rise of resistant C. difficile. Science 321, 360.
    • (2008) Science , vol.321 , pp. 360
    • Taubes, G.1
  • 34
    • 0019880981 scopus 로고
    • A continuous spectrophotometric assay for Clostridium histolyticum collagenase
    • Van Wart, H.E. and Steinbrink, D.R. (1981). A continuous spectrophotometric assay for Clostridium histolyticum collagenase. Anal. Biochem. 113, 356-365.
    • (1981) Anal. Biochem , vol.113 , pp. 356-365
    • Van Wart, H.E.1    Steinbrink, D.R.2
  • 35
    • 0022411969 scopus 로고
    • Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum
    • Van Wart, H.E. and Steinbrink, D.R. (1985). Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum. Biochemistry 24, 6520-6526.
    • (1985) Biochemistry , vol.24 , pp. 6520-6526
    • Van Wart, H.E.1    Steinbrink, D.R.2
  • 36
    • 1242292972 scopus 로고    scopus 로고
    • Collagenolytic proteases from bacteria
    • Watanabe, K. (2004). Collagenolytic proteases from bacteria. Appl. Microbiol. Biotechnol. 63, 520-526.
    • (2004) Appl. Microbiol. Biotechnol , vol.63 , pp. 520-526
    • Watanabe, K.1
  • 38
    • 0344942600 scopus 로고    scopus 로고
    • A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation
    • Wilson, J.J., Matsushita, O., Okabe, A., and Sakon, J. (2003). A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation. EMBO J. 22, 1743-1752.
    • (2003) EMBO J , vol.22 , pp. 1743-1752
    • Wilson, J.J.1    Matsushita, O.2    Okabe, A.3    Sakon, J.4
  • 39
    • 0037048734 scopus 로고    scopus 로고
    • Application potency of engineered G159 mutants on P1 substrate pocket of subtilisin YaB as improved meat tenderizers
    • Yeh, C.M., Yang, M.C., and Tsai, Y.C. (2002). Application potency of engineered G159 mutants on P1 substrate pocket of subtilisin YaB as improved meat tenderizers. J. Agric. Food. Chem. 50, 6199-6204.
    • (2002) J. Agric. Food. Chem , vol.50 , pp. 6199-6204
    • Yeh, C.M.1    Yang, M.C.2    Tsai, Y.C.3
  • 40
    • 0028075721 scopus 로고
    • Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase
    • Yoshihara, K., Matsushita, O., Minami, J., and Okabe, A. (1994). Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase. J. Bacteriol. 176, 6489-6496.
    • (1994) J. Bacteriol , vol.176 , pp. 6489-6496
    • Yoshihara, K.1    Matsushita, O.2    Minami, J.3    Okabe, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.