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Volumn 52, Issue 2, 2007, Pages 265-272

The dodecameric vanadium-dependent haloperoxidase from the marine algae Corallina officinalis: Cloning, expression, and refolding of the recombinant enzyme

Author keywords

Biotransformation; Corallina officinalis; Dodecamer; Protein refolding; Vanadium dependent bromoperoxidase

Indexed keywords

IODIDE PEROXIDASE; OIL; P & S LIQUID; PHENOL DERIVATIVE; POLYMER; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VANADIUM IODOPEROXIDASE;

EID: 33846468923     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.08.010     Document Type: Article
Times cited : (31)

References (26)
  • 1
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg A.P.J. Preparative protein refolding. Trends Biotechnol. 20 (2002) 437-443
    • (2002) Trends Biotechnol. , vol.20 , pp. 437-443
    • Middelberg, A.P.J.1
  • 5
    • 0032039627 scopus 로고    scopus 로고
    • Vanadium haloperoxidases
    • Butler A. Vanadium haloperoxidases. Curr. Opin. Chem. Biol. 2 (1998) 279-285
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 279-285
    • Butler, A.1
  • 6
    • 0035371814 scopus 로고    scopus 로고
    • Enzymatic halogenation of flavanones and flavones
    • Yaipakdee P., and Robertson L.W. Enzymatic halogenation of flavanones and flavones. Phytochemistry 57 (2001) 341-347
    • (2001) Phytochemistry , vol.57 , pp. 341-347
    • Yaipakdee, P.1    Robertson, L.W.2
  • 8
    • 0027368552 scopus 로고
    • Biotransformation of alkenes by haloperoxidases: regiospecific bromohydrin formation from cinnamyl substrates
    • Coughlin P., Roberts S., Rush C., and Willetts A. Biotransformation of alkenes by haloperoxidases: regiospecific bromohydrin formation from cinnamyl substrates. Biotechnol. Lett. 15 (1993) 907-912
    • (1993) Biotechnol. Lett. , vol.15 , pp. 907-912
    • Coughlin, P.1    Roberts, S.2    Rush, C.3    Willetts, A.4
  • 9
    • 0035940872 scopus 로고    scopus 로고
    • Biocatalytic chlorination of aromatic hydrocarbons by chloroperoxidase of Caldariomyces fumago
    • Vazquez-Duhalt R., Ayala M., and Marquez-Rocha F.J. Biocatalytic chlorination of aromatic hydrocarbons by chloroperoxidase of Caldariomyces fumago. Phytochemistry 6 (2001) 929-933
    • (2001) Phytochemistry , vol.6 , pp. 929-933
    • Vazquez-Duhalt, R.1    Ayala, M.2    Marquez-Rocha, F.J.3
  • 12
    • 25144486262 scopus 로고
    • Purification and characterisation of the vanadium bromoperoxidase from the macroalga Corallina officinalis
    • Sheffield D.J., Harry T., Smith A.J., and Roger L.J. Purification and characterisation of the vanadium bromoperoxidase from the macroalga Corallina officinalis. Phytochemistry 32 (1993) 21-26
    • (1993) Phytochemistry , vol.32 , pp. 21-26
    • Sheffield, D.J.1    Harry, T.2    Smith, A.J.3    Roger, L.J.4
  • 13
    • 0034674155 scopus 로고    scopus 로고
    • Crystal structure of dodecameric Vanadium dependent bromoperoxidase from the red algae Corallina officinalis
    • Isupov M., Dalby A., Brindley A., Izumi Y., Tanabe T., Murshudov G., and Littlechild J.A. Crystal structure of dodecameric Vanadium dependent bromoperoxidase from the red algae Corallina officinalis. J. Mol. Biol. 299 (2000) 1035-1049
    • (2000) J. Mol. Biol. , vol.299 , pp. 1035-1049
    • Isupov, M.1    Dalby, A.2    Brindley, A.3    Izumi, Y.4    Tanabe, T.5    Murshudov, G.6    Littlechild, J.A.7
  • 14
    • 0028883681 scopus 로고
    • Inhibition and inactivation of vanadium bromoperoxidase by the substrate hydrogen peroxide and further mechanistic studies
    • Soedjak H.S., Walker J.V., and Butler A. Inhibition and inactivation of vanadium bromoperoxidase by the substrate hydrogen peroxide and further mechanistic studies. Biochemistry 34 (1995) 12689-12696
    • (1995) Biochemistry , vol.34 , pp. 12689-12696
    • Soedjak, H.S.1    Walker, J.V.2    Butler, A.3
  • 15
    • 0028895691 scopus 로고
    • Purification, crystallisation and preliminary X-ray analysis of the vanadium dependent haloperoxidase from Corallina officinalis
    • Rush C., Willetts A., Davies C., Dauter S., Littlechild J., and Watson H.C. Purification, crystallisation and preliminary X-ray analysis of the vanadium dependent haloperoxidase from Corallina officinalis. FEBS Lett. 359 (1995) 244-246
    • (1995) FEBS Lett. , vol.359 , pp. 244-246
    • Rush, C.1    Willetts, A.2    Davies, C.3    Dauter, S.4    Littlechild, J.5    Watson, H.C.6
  • 16
    • 0032557641 scopus 로고    scopus 로고
    • Cloning and expression of the gene for a vanadium dependent bromoperoxidase from a marine macroalga Corallina pilulifera
    • Shimonishi M., Kuwamoto S., Inoue H., Wever R., Onishiro T., Izumi Y., and Tanabe T. Cloning and expression of the gene for a vanadium dependent bromoperoxidase from a marine macroalga Corallina pilulifera. FEBS Lett. 42 (1998) 105-110
    • (1998) FEBS Lett. , vol.42 , pp. 105-110
    • Shimonishi, M.1    Kuwamoto, S.2    Inoue, H.3    Wever, R.4    Onishiro, T.5    Izumi, Y.6    Tanabe, T.7
  • 17
    • 0035983823 scopus 로고    scopus 로고
    • Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the recombinant enzyme
    • Ohshiro T., Hemrika W., Aibara T., Wever R., and Izumi Y. Expression of the vanadium-dependent bromoperoxidase gene from a marine macro-alga Corallina pilulifera in Saccharomyces cerevisiae and characterization of the recombinant enzyme. Phytochemistry 60 (2002) 595-601
    • (2002) Phytochemistry , vol.60 , pp. 595-601
    • Ohshiro, T.1    Hemrika, W.2    Aibara, T.3    Wever, R.4    Izumi, Y.5
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 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. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalities 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, positions-specific gap penalities and weight matrix choice. Nucleic Acids Res. 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 21
    • 84943464186 scopus 로고    scopus 로고
    • H. Vilter, Peroxidases from Phaeophycae. IV. Fractionation and location of peroxidases isoenzymes. in: Ascophyllum nodosum. Botanica Marina, vol. 26, 1983, pp. 451-455.
  • 22
    • 0029442216 scopus 로고    scopus 로고
    • H. Vilter, Vanadium-dependent haloperoxidases, in: M. Bekker (Ed.), Metal Ions in Biological Systems-Vanadium and its Role in Life, New York USA, vol. 31, 1995, pp. 325-362.
  • 23
    • 0024971771 scopus 로고
    • The brown alga Ascophyllum nodosum contains two different vanadium bromoperoxidase
    • Krenn B.E., Tromp M.G.M., and Wever R. The brown alga Ascophyllum nodosum contains two different vanadium bromoperoxidase. J. Biol. Chem. 264 (1989) 19287-19292
    • (1989) J. Biol. Chem. , vol.264 , pp. 19287-19292
    • Krenn, B.E.1    Tromp, M.G.M.2    Wever, R.3
  • 24
    • 0037173579 scopus 로고    scopus 로고
    • Reactivity of recombinant and mutant vanadium bromoperoxidase from the red alga Corallina officinalis
    • Carter J.N., Beatty K.E., Simpson M.T., and Butler A. Reactivity of recombinant and mutant vanadium bromoperoxidase from the red alga Corallina officinalis. J. Inorg. Biochem. 91 (2002) 59-69
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 59-69
    • Carter, J.N.1    Beatty, K.E.2    Simpson, M.T.3    Butler, A.4
  • 25
    • 0034113189 scopus 로고    scopus 로고
    • Purification and characterisation of vanadium haloperoxidases from the brown alga Pelvetia canaliculata
    • Almedia M.G., Humanes M., Melo R., Silva R.A., Frausto da Silva J.J.R., and Wever R. Purification and characterisation of vanadium haloperoxidases from the brown alga Pelvetia canaliculata. Phytochemistry 54 (2000) 5-11
    • (2000) Phytochemistry , vol.54 , pp. 5-11
    • Almedia, M.G.1    Humanes, M.2    Melo, R.3    Silva, R.A.4    Frausto da Silva, J.J.R.5    Wever, R.6
  • 26
    • 0030938579 scopus 로고    scopus 로고
    • From phosphatases to vanadium peroxidases: a similar architecture of the active site
    • Hemrika W., Renirie R., Dekker H., Barnett P., and Wever R. From phosphatases to vanadium peroxidases: a similar architecture of the active site. Proc. Natl. Acad. Sci. USA 94 (1997) 2145-2149
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2145-2149
    • Hemrika, W.1    Renirie, R.2    Dekker, H.3    Barnett, P.4    Wever, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.