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Volumn 71, Issue 5-6, 2010, Pages 524-530

Biochemical comparison of two proteolytic enzymes from Carica candamarcensis: Structural motifs underlying resistance to cystatin inhibition

Author keywords

Carica candamarcensis; Caricaceae; Cystatin; Cysteine proteinases; Latex

Indexed keywords

CYSTATIN; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; IODOACETAMIDE; ISOPROTEIN; MITOGENIC AGENT; PEPTIDE HYDROLASE; VEGETABLE PROTEIN;

EID: 77949656532     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2009.12.018     Document Type: Article
Times cited : (10)

References (35)
  • 2
    • 0022552955 scopus 로고
    • Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives
    • Baines B.S., Brocklehurst K., Carey P.R., Jarvis M., Salih E., and Storer A.C. Chymopapain A. Purification and investigation by covalent chromatography and characterization by two-protonic-state reactivity-probe kinetics, steady-state kinetics and resonance Raman spectroscopy of some dithioacyl derivatives. Biochem. J. 233 (1986) 119-129
    • (1986) Biochem. J. , vol.233 , pp. 119-129
    • Baines, B.S.1    Brocklehurst, K.2    Carey, P.R.3    Jarvis, M.4    Salih, E.5    Storer, A.C.6
  • 3
    • 0022083449 scopus 로고
    • Names and numbers of papaya proteinases
    • Barrett A.J., and Buttle D.J. Names and numbers of papaya proteinases. Biochem. J. 228 (1985) 527
    • (1985) Biochem. J. , vol.228 , pp. 527
    • Barrett, A.J.1    Buttle, D.J.2
  • 4
    • 0024066065 scopus 로고
    • The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode W., Engh R., Musil D., Thiele U., Huber R., Karshikov A., Brzin J., Kos J., and Turk V. The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J. 7 (1988) 2593-2599
    • (1988) EMBO J. , vol.7 , pp. 2593-2599
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 5
    • 0028715789 scopus 로고
    • A biochemical comparison between latex from C. candamarcensis and C. papaya
    • Bravo L.M., Hermosilla L., and Salas C.E. A biochemical comparison between latex from C. candamarcensis and C. papaya. Braz. J. Med. Biol. Res. 27 (1994) 2831-2842
    • (1994) Braz. J. Med. Biol. Res. , vol.27 , pp. 2831-2842
    • Bravo, L.M.1    Hermosilla, L.2    Salas, C.E.3
  • 7
    • 77949653137 scopus 로고    scopus 로고
    • DeLano Scientific, Palo Alto, CA, USA
    • DeLano, W.L., 2002. The PyMOL Molecular Graphics System. DeLano Scientific, Palo Alto, CA, USA. .
    • (2002)
    • DeLano, W.L.1
  • 8
    • 0024066667 scopus 로고
    • The thiol proteinases from the latex of Carica papaya L. The primary structure of proteinase Omega
    • Dubois T., Kleinschmidt T., Schnek A.G., Looze Y., and Braunitzer G. The thiol proteinases from the latex of Carica papaya L. The primary structure of proteinase Omega. Biol. Chem. Hoppe-Seyler 369 (1988) 741-754
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 741-754
    • Dubois, T.1    Kleinschmidt, T.2    Schnek, A.G.3    Looze, Y.4    Braunitzer, G.5
  • 9
    • 0023661840 scopus 로고
    • Vein-cutting behavior: insect counterploy to the latex defense of plants
    • Dussourd D.E., and Eisner T. Vein-cutting behavior: insect counterploy to the latex defense of plants. Science 237 (1987) 898-901
    • (1987) Science , vol.237 , pp. 898-901
    • Dussourd, D.E.1    Eisner, T.2
  • 10
    • 0021672206 scopus 로고
    • l-Pyroglutamyl-l-phenylalanyl-l-leucine-p-nitroanilide - a chromogenic substrate for thiol proteinase assay
    • Filippova I.Y., Lysogorskaya E.N., Oksenoit E.S., Rudenskaya G.N., and Stepanov V.M. l-Pyroglutamyl-l-phenylalanyl-l-leucine-p-nitroanilide - a chromogenic substrate for thiol proteinase assay. Anal. Biochem. 143 (1984) 293-297
    • (1984) Anal. Biochem. , vol.143 , pp. 293-297
    • Filippova, I.Y.1    Lysogorskaya, E.N.2    Oksenoit, E.S.3    Rudenskaya, G.N.4    Stepanov, V.M.5
  • 11
    • 0028341649 scopus 로고
    • Hevein, a lectin-like protein from Hevea brasiliensis (rubber tree) is involved in the coagulation of latex
    • Gidrol X., Chrestin H., Tan H.L., and Kush A. Hevein, a lectin-like protein from Hevea brasiliensis (rubber tree) is involved in the coagulation of latex. J. Biol. Chem. 269 (1994) 9278-9283
    • (1994) J. Biol. Chem. , vol.269 , pp. 9278-9283
    • Gidrol, X.1    Chrestin, H.2    Tan, H.L.3    Kush, A.4
  • 12
  • 13
    • 34547536616 scopus 로고    scopus 로고
    • The structure of CMS2MS2, a mitogenic protein isolated from latex of Carica candamarcensis
    • Gomes M.T.R., Bemquerer M.P., Lopes M.T.P., Richardson M., Oyama S., and Salas C.E. The structure of CMS2MS2, a mitogenic protein isolated from latex of Carica candamarcensis. Biol. Chem. 388 (2007) 819-822
    • (2007) Biol. Chem. , vol.388 , pp. 819-822
    • Gomes, M.T.R.1    Bemquerer, M.P.2    Lopes, M.T.P.3    Richardson, M.4    Oyama, S.5    Salas, C.E.6
  • 15
    • 0028155056 scopus 로고
    • Biochemical characterization of a new cysteine endopeptidase from Carica candamarcensis L.
    • Gravina de Moraes M., Termignoni C., and Salas C.E. Biochemical characterization of a new cysteine endopeptidase from Carica candamarcensis L. Plant Sci. 102 (1994) 11-18
    • (1994) Plant Sci. , vol.102 , pp. 11-18
    • Gravina de Moraes, M.1    Termignoni, C.2    Salas, C.E.3
  • 17
    • 0028446499 scopus 로고
    • Primary structure of CC-III, the glycosylated cysteine proteinase from the latex of Carica candamarcensis Hook
    • Jaziri M., Kleinschmidt T., Walraevens V., Schnek A.G., and Looze Y. Primary structure of CC-III, the glycosylated cysteine proteinase from the latex of Carica candamarcensis Hook. Biol. Chem. Hoppe-Seyler 375 (1994) 379-385
    • (1994) Biol. Chem. Hoppe-Seyler , vol.375 , pp. 379-385
    • Jaziri, M.1    Kleinschmidt, T.2    Walraevens, V.3    Schnek, A.G.4    Looze, Y.5
  • 18
    • 77956980664 scopus 로고    scopus 로고
    • Resin ducts in the mango fruit: a defense system
    • Joel D.M. Resin ducts in the mango fruit: a defense system. J. Exp. Bot. 31 (2001) 1707-1718
    • (2001) J. Exp. Bot. , vol.31 , pp. 1707-1718
    • Joel, D.M.1
  • 20
  • 21
    • 0033614254 scopus 로고    scopus 로고
    • Spontaneous processing of peptides during coagulation of latex from Carica papaya
    • Moutim V., Silva L.G., Lopes M.T.P., Fernandes G.W., and Salas C.E. Spontaneous processing of peptides during coagulation of latex from Carica papaya. Plant Sci. 142 (1999) 115-121
    • (1999) Plant Sci. , vol.142 , pp. 115-121
    • Moutim, V.1    Silva, L.G.2    Lopes, M.T.P.3    Fernandes, G.W.4    Salas, C.E.5
  • 22
    • 0034962673 scopus 로고    scopus 로고
    • Purification of a cysteine proteinase from Carica candamarcensis L. and cloning of a genomic putative fragment coding for this enzyme
    • Pereira M.T., Lopes M.T., Meira W.O., and Salas C.E. Purification of a cysteine proteinase from Carica candamarcensis L. and cloning of a genomic putative fragment coding for this enzyme. Protein Expr. Purif. 22 (2001) 249-257
    • (2001) Protein Expr. Purif. , vol.22 , pp. 249-257
    • Pereira, M.T.1    Lopes, M.T.2    Meira, W.O.3    Salas, C.E.4
  • 24
    • 0024551586 scopus 로고
    • Stem bromelain: amino acid sequence and implications for weak binding of cystatin
    • Ritonja A., Rowan A.D., Buttle D.J., Rawlings N.D., Turk V., and Barrett A.J. Stem bromelain: amino acid sequence and implications for weak binding of cystatin. FEBS Lett. 247 (1989) 419-424
    • (1989) FEBS Lett. , vol.247 , pp. 419-424
    • Ritonja, A.1    Rowan, A.D.2    Buttle, D.J.3    Rawlings, N.D.4    Turk, V.5    Barrett, A.J.6
  • 25
    • 0024289238 scopus 로고
    • Ananain: a novel cysteine proteinase found in pineapple stem
    • Rowan A.D., Buttle D.J., and Barrett A.J. Ananain: a novel cysteine proteinase found in pineapple stem. Arch. Biothem. Biophys. 267 (1988) 262-270
    • (1988) Arch. Biothem. Biophys. , vol.267 , pp. 262-270
    • Rowan, A.D.1    Buttle, D.J.2    Barrett, A.J.3
  • 26
    • 0025268799 scopus 로고
    • The cysteine proteinases of the pineapple plant
    • Rowan A.D., Buttle D.J., and Barrett A.J. The cysteine proteinases of the pineapple plant. Biochem. J. 266 (1990) 869-875
    • (1990) Biochem. J. , vol.266 , pp. 869-875
    • Rowan, A.D.1    Buttle, D.J.2    Barrett, A.J.3
  • 27
    • 0031134925 scopus 로고    scopus 로고
    • Changes in protein profile during coagulation of latex from Carica papaya
    • Silva L.G., Garcia O., Lopes M.T.P., and Salas C.E. Changes in protein profile during coagulation of latex from Carica papaya. Braz. J. Med. Biol. Res. 30 (1997) 615-619
    • (1997) Braz. J. Med. Biol. Res. , vol.30 , pp. 615-619
    • Silva, L.G.1    Garcia, O.2    Lopes, M.T.P.3    Salas, C.E.4
  • 30
    • 0028860244 scopus 로고
    • The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin
    • Thomas M.P., Verma C., Boyd S.M., and Brocklehurst K. The structural origins of the unusual specificities observed in the isolation of chymopapain M and actinidin by covalent chromatography and the lack of inhibition of chymopapain M by cystatin. Biochem. J. 306 (1995) 39-46
    • (1995) Biochem. J. , vol.306 , pp. 39-46
    • Thomas, M.P.1    Verma, C.2    Boyd, S.M.3    Brocklehurst, K.4
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 32
    • 0345310073 scopus 로고    scopus 로고
    • Revised definition of substrate binding sites of papain-like cysteine proteases
    • Turk D., Guncar G., Podobnik M., and Turk B. Revised definition of substrate binding sites of papain-like cysteine proteases. Biol. Chem. 379 (1998) 137-147
    • (1998) Biol. Chem. , vol.379 , pp. 137-147
    • Turk, D.1    Guncar, G.2    Podobnik, M.3    Turk, B.4
  • 34
    • 0032934842 scopus 로고    scopus 로고
    • Isolation and primary structure of the CCI papain-like cysteine proteinases from the latex of Carica candamarcensis Hook
    • Walraevens V., Vandermeers-Piret M., Vandermeers A., Gourlet P., and Robberecht P. Isolation and primary structure of the CCI papain-like cysteine proteinases from the latex of Carica candamarcensis Hook. Biol. Chem. Hoppe-Seyler 380 (1999) 485-488
    • (1999) Biol. Chem. Hoppe-Seyler , vol.380 , pp. 485-488
    • Walraevens, V.1    Vandermeers-Piret, M.2    Vandermeers, A.3    Gourlet, P.4    Robberecht, P.5
  • 35
    • 0025008745 scopus 로고
    • The aminoacid sequence of chymopapain from Carica papaya
    • Watson C., Yaguchi M., and Lynn K.R. The aminoacid sequence of chymopapain from Carica papaya. Biochem. J. 266 (1990) 75-81
    • (1990) Biochem. J. , vol.266 , pp. 75-81
    • Watson, C.1    Yaguchi, M.2    Lynn, K.R.3


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