메뉴 건너뛰기




Volumn 65, Issue 3, 2004, Pages 249-259

Horseradish peroxidase: A modern view of a classic enzyme

Author keywords

Arabidopsis thaliana; Armoracia rusticana; Cruciferae; Heme; Horseradish peroxidase; Hydrogen peroxide; Indole 3 acetic acid; Protein engineering

Indexed keywords

AMINO ACID; HORSERADISH PEROXIDASE; INDOLEACETIC ACID;

EID: 0742324902     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2003.10.022     Document Type: Article
Times cited : (1090)

References (57)
  • 1
    • 84981749918 scopus 로고
    • Untersuchungen über die Rolle der Peroxyde in der Chemie der lebenden Zelle. IV
    • Bach A., Chodat R. Untersuchungen über die Rolle der Peroxyde in der Chemie der lebenden Zelle. IV. Ueber Peroxydase. Ber. Deutsch. Chem. Gesell. 36:1903;600-605.
    • (1903) Ueber Peroxydase. Ber. Deutsch. Chem. Gesell. , vol.36 , pp. 600-605
    • Bach, A.1    Chodat, R.2
  • 2
    • 0033008999 scopus 로고    scopus 로고
    • Production of catalytically active horseradish peroxidase-n in the insect cell-baculovirus expression system
    • Bartonek-Roxå E., Holm C. Production of catalytically active horseradish peroxidase-n in the insect cell-baculovirus expression system. Biotech. Techniques. 13:1999;69-73.
    • (1999) Biotech. Techniques , vol.13 , pp. 69-73
    • Bartonek-Roxå, E.1    Holm, C.2
  • 5
    • 0002154654 scopus 로고
    • Horseradish peroxidase: Structure and kinetic properties
    • J. Everse, K.E. Everse, & M.B. Grisham. Boca Raton, Florida: CRC Press
    • Dunford H.B. Horseradish peroxidase: Structure and kinetic properties. Everse J., Everse K.E., Grisham M.B. Peroxidases in chemistry and biology, Vol. 2. 1991;1-24 CRC Press, Boca Raton, Florida.
    • (1991) Peroxidases in Chemistry and Biology, Vol. 2 , pp. 1-24
    • Dunford, H.B.1
  • 7
    • 0142075823 scopus 로고    scopus 로고
    • The peroxidase gene family in plants: A phylogenetic overview
    • Duroux, L., Welinder, K.G., 2003. The peroxidase gene family in plants: a phylogenetic overview. J. Mol. Evol. 57, 397-407.
    • (2003) J. Mol. Evol. , vol.57 , pp. 397-407
    • Duroux, L.1    Welinder, K.G.2
  • 8
    • 0034639435 scopus 로고    scopus 로고
    • Role of protein environment in horseradish peroxidase compound I formation: Molecular dynamics simulations of horseradish peroxidase-HOOH complex
    • Filizola M., Loew G.H. Role of protein environment in horseradish peroxidase compound I formation: molecular dynamics simulations of horseradish peroxidase-HOOH complex. J. Am. Chem. Soc. 122:2000;18-25.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 18-25
    • Filizola, M.1    Loew, G.H.2
  • 9
    • 0035863281 scopus 로고    scopus 로고
    • Oxidative activation of indole-3-acetic acids to cytotoxic species-a potential new role for plant auxins in cancer therapy
    • Folkes L.K., Wardman P. Oxidative activation of indole-3-acetic acids to cytotoxic species-a potential new role for plant auxins in cancer therapy. Biochem. Pharmacol. 61:2001;129-136.
    • (2001) Biochem. Pharmacol. , vol.61 , pp. 129-136
    • Folkes, L.K.1    Wardman, P.2
  • 10
    • 0037081743 scopus 로고    scopus 로고
    • 5-Fluoroindole-3-acetic acid: A prodrug activated by a peroxidase with potential for use in targeted cancer therapy
    • Folkes L.K., Greco O., Dachs G.U., Stratford M.R.L., Wardman P. 5-Fluoroindole-3-acetic acid: a prodrug activated by a peroxidase with potential for use in targeted cancer therapy. Biochem. Pharmacol. 63:2002;265-272.
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 265-272
    • Folkes, L.K.1    Greco, O.2    Dachs, G.U.3    Stratford, M.R.L.4    Wardman, P.5
  • 12
    • 0025345241 scopus 로고
    • Genomic DNA structure of two new horseradish-peroxidase-encoding genes
    • Fujiyama K., Takemura H., Shinmyo A., Okada H., Takano M. Genomic DNA structure of two new horseradish-peroxidase-encoding genes. Gene. 89:1990;163-169.
    • (1990) Gene , vol.89 , pp. 163-169
    • Fujiyama, K.1    Takemura, H.2    Shinmyo, A.3    Okada, H.4    Takano, M.5
  • 18
    • 0033521007 scopus 로고    scopus 로고
    • The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates
    • Henriksen A., Smith A.T., Gajhede M. The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates. J. Biol. Chem. 274:1999;35005-35011.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35005-35011
    • Henriksen, A.1    Smith, A.T.2    Gajhede, M.3
  • 19
    • 0035798657 scopus 로고    scopus 로고
    • The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase
    • Howes B.D., Feis A., Raimondi L., Indiani C., Smulevich G. The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase. J. Biol. Chem. 276:2001;40704-40711.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40704-40711
    • Howes, B.D.1    Feis, A.2    Raimondi, L.3    Indiani, C.4    Smulevich, G.5
  • 20
    • 0034085246 scopus 로고    scopus 로고
    • A cis-element containing PAL-box functions in the expression of the wound-inducible peroxidase gene of horseradish
    • Kaothien P., Shimokawatoko Y., Kawaoka A., Yoshida K., Shinmyo A. A cis-element containing PAL-box functions in the expression of the wound-inducible peroxidase gene of horseradish. Plant Cell Rep. 19:2000;558-562.
    • (2000) Plant Cell Rep. , vol.19 , pp. 558-562
    • Kaothien, P.1    Shimokawatoko, Y.2    Kawaoka, A.3    Yoshida, K.4    Shinmyo, A.5
  • 23
    • 0742317882 scopus 로고
    • Isolation and characterization of α-guaiaconic acid and the nature of guaiacum blue
    • Kratochvil J.F., Burris R.H., Seikel M.K., Harkin J.M. Isolation and characterization of α-guaiaconic acid and the nature of guaiacum blue. Phytochemistry. 10:1971;2529-2531.
    • (1971) Phytochemistry , vol.10 , pp. 2529-2531
    • Kratochvil, J.F.1    Burris, R.H.2    Seikel, M.K.3    Harkin, J.M.4
  • 24
    • 0742300322 scopus 로고    scopus 로고
    • Recent advances in catalytic peroxidase histochemistry
    • Krieg R., Halbhuber K.-J. Recent advances in catalytic peroxidase histochemistry. Cellular Mol. Biol. 49:2003;547-563.
    • (2003) Cellular Mol. Biol. , vol.49 , pp. 547-563
    • Krieg, R.1    Halbhuber, K.-J.2
  • 25
    • 0002533061 scopus 로고    scopus 로고
    • The role of the tobacco anionic peroxidase in growth and development
    • C. Obinger, U. Burner, R. Ebermann, C. Penel, & H. Greppin. Geneva: University of Geneva
    • Lagrimini L.M. The role of the tobacco anionic peroxidase in growth and development. Obinger C., Burner U., Ebermann R., Penel C., Greppin H. Plant Peroxidases, Biochemistry and Physiology. 1996;235-242 University of Geneva, Geneva.
    • (1996) Plant Peroxidases, Biochemistry and Physiology , pp. 235-242
    • Lagrimini, L.M.1
  • 26
    • 0036728244 scopus 로고    scopus 로고
    • Oxidative stress, antioxidants and stress tolerance
    • Mittler R. Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci. 7:2002;405-410.
    • (2002) Trends Plant Sci. , vol.7 , pp. 405-410
    • Mittler, R.1
  • 27
    • 0034088553 scopus 로고    scopus 로고
    • Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris
    • Morawski B., Lin Z., Cirino P., Joo H., Bandara G., Arnold F.H. Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris. Protein Eng. 13:2000;377-384.
    • (2000) Protein Eng. , vol.13 , pp. 377-384
    • Morawski, B.1    Lin, Z.2    Cirino, P.3    Joo, H.4    Bandara, G.5    Arnold, F.H.6
  • 28
    • 0034842869 scopus 로고    scopus 로고
    • Functional expression and stabilization of horseradish peroxidase by directed evolution in Saccharomyces cerevisiae
    • Morawski B., Quan S., Arnold F.H. Functional expression and stabilization of horseradish peroxidase by directed evolution in Saccharomyces cerevisiae. Biotechnol. Bioeng. 76:2001;99-107.
    • (2001) Biotechnol. Bioeng. , vol.76 , pp. 99-107
    • Morawski, B.1    Quan, S.2    Arnold, F.H.3
  • 29
    • 0029151614 scopus 로고
    • Horseradish peroxidase His-42→Ala, His-42→Val, and Phe-41→Ala mutants. Histidine catalysis and control of substrate access to the heme iron
    • Newmyer S.L., Ortiz de Montellano P.R. Horseradish peroxidase His-42→Ala, His-42→Val, and Phe-41→Ala mutants. Histidine catalysis and control of substrate access to the heme iron. J. Biol. Chem. 270:1995;19430-19438.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19430-19438
    • Newmyer, S.L.1    Ortiz De Montellano, P.R.2
  • 30
    • 0035909072 scopus 로고    scopus 로고
    • Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2
    • Nielsen K.L., Indiani C., Henriksen A., Feis A., Becucci M., Gajhede M., Smulevich G., Welinder K.G. Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2. Biochemistry. 40:2001;11013-11021.
    • (2001) Biochemistry , vol.40 , pp. 11013-11021
    • Nielsen, K.L.1    Indiani, C.2    Henriksen, A.3    Feis, A.4    Becucci, M.5    Gajhede, M.6    Smulevich, G.7    Welinder, K.G.8
  • 31
    • 1642489328 scopus 로고    scopus 로고
    • Enzyme stabilization - Recent experimental progress
    • Ó'Fágáin C. Enzyme stabilization - recent experimental progress. Enzyme Microb. Technol. 33:2003;137-149.
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 137-149
    • Ó'Fágáin, C.1
  • 34
    • 0028833821 scopus 로고
    • Molecular engineering of horseradish peroxidase; Thioether sulfoxidation and styrene epoxidation by Phe-41 leucine and threonine mutants
    • Ozaki S., Ortiz de Montellano P.R. Molecular engineering of horseradish peroxidase; thioether sulfoxidation and styrene epoxidation by Phe-41 leucine and threonine mutants. J. Am. Chem. Soc. 117:1995;7056-7064.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7056-7064
    • Ozaki, S.1    Ortiz De Montellano, P.R.2
  • 35
    • 0011998433 scopus 로고
    • Peroxidases: Historical background
    • H. Greppin, C. Penel, & T. Gaspar. Geneva: University of Geneva
    • Paul K.G. Peroxidases: historical background. Greppin H., Penel C., Gaspar T. Molecular and Physiological Aspects of Plant Peroxidases. 1986;1-14 University of Geneva, Geneva.
    • (1986) Molecular and Physiological Aspects of Plant Peroxidases , pp. 1-14
    • Paul, K.G.1
  • 36
    • 0009193408 scopus 로고
    • Note sur la sophistication de la résine de jalap et sur les moyens de la reconnaître, etc
    • Planche L.A. Note sur la sophistication de la résine de jalap et sur les moyens de la reconnaître, etc. Bull. Pharmacie. 2:1810;578-580.
    • (1810) Bull. Pharmacie , vol.2 , pp. 578-580
    • Planche, L.A.1
  • 37
    • 0038372484 scopus 로고    scopus 로고
    • Growth suppression, altered stomatal responses, and augmented induction of heat shock proteins in cytosolic ascorbate peroxidase (Apx1)-deficient Arabidopsis plants
    • Pnueli L., Liang H., Rozenberg M., Mittler R. Growth suppression, altered stomatal responses, and augmented induction of heat shock proteins in cytosolic ascorbate peroxidase (Apx1)-deficient Arabidopsis plants. Plant J. 34:2003;187-203.
    • (2003) Plant J. , vol.34 , pp. 187-203
    • Pnueli, L.1    Liang, H.2    Rozenberg, M.3    Mittler, R.4
  • 39
    • 0037119677 scopus 로고    scopus 로고
    • Halogenated indole-3-acetic acids as oxidatively activated prodrugs with potential for targeted cancer therapy
    • Rossiter S., Folkes L.K., Wardman P. Halogenated indole-3-acetic acids as oxidatively activated prodrugs with potential for targeted cancer therapy. Bioorg. Med. Chem. Lett. 12:2002;2523-2526.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 2523-2526
    • Rossiter, S.1    Folkes, L.K.2    Wardman, P.3
  • 40
    • 0028249225 scopus 로고
    • Horseradish peroxidase: The analyst's friend
    • D.K. Ballou. London: Portland Press
    • Ryan O., Smyth M.R., Ó'Fágáin C. Horseradish peroxidase: the analyst's friend. Ballou D.K. Essays in Biochemistry, Vol. 28. 1994;129-146 Portland Press, London.
    • (1994) Essays in Biochemistry, Vol. 28 , pp. 129-146
    • Ryan, O.1    Smyth, M.R.2    Ó'Fágáin, C.3
  • 41
    • 0242518089 scopus 로고    scopus 로고
    • A novel type of spiro compound formed by oxidative cross coupling of methyl sinapate with a syringyl lignin model compound. A model system for the β-1 pathway in lignin biosynthesis
    • Setälä H., Pajunen A., Rummakko P., Sipilä J., Brunow G. A novel type of spiro compound formed by oxidative cross coupling of methyl sinapate with a syringyl lignin model compound. A model system for the β-1 pathway in lignin biosynthesis. J. Chem. Soc. Perkin Trans. 1:1999;461-464.
    • (1999) J. Chem. Soc. Perkin Trans. , vol.1 , pp. 461-464
    • Setälä, H.1    Pajunen, A.2    Rummakko, P.3    Sipilä, J.4    Brunow, G.5
  • 44
    • 0032042908 scopus 로고    scopus 로고
    • Substrate binding and catalysis in heme peroxidases
    • Smith A.T., Veitch N.C. Substrate binding and catalysis in heme peroxidases. Curr. Opin. Chem. Biol. 2:1998;269-278.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 269-278
    • Smith, A.T.1    Veitch, N.C.2
  • 46
    • 0343554668 scopus 로고    scopus 로고
    • On the fate of catharanthine and vindoline during the peroxidase-mediated enzymatic synthesis of α-3′,4′- anhydrovinblastine
    • Sottomayor M., DiCosmo F., Ros Barceló A.R. On the fate of catharanthine and vindoline during the peroxidase-mediated enzymatic synthesis of α-3′,4′-anhydrovinblastine. Enzyme Microb. Technol. 21:1997;543-549.
    • (1997) Enzyme Microb. Technol. , vol.21 , pp. 543-549
    • Sottomayor, M.1    Dicosmo, F.2    Ros Barceló, A.R.3
  • 47
    • 0344972955 scopus 로고    scopus 로고
    • Purification and characterization of α-3′,4′- anhydrovinblastine synthase (peroxidase-like) from Catharanthus roseus (L.)
    • Sottomayor M., López-Serrano M., DiCosmo F., Ros Barceló A.R. Purification and characterization of α-3′,4′- anhydrovinblastine synthase (peroxidase-like) from Catharanthus roseus (L.). G. Don. FEBS Lett. 428:1998;299-303.
    • (1998) G. Don. FEBS Lett. , vol.428 , pp. 299-303
    • Sottomayor, M.1    López-Serrano, M.2    Dicosmo, F.3    Ros Barceló, A.R.4
  • 48
    • 0037123359 scopus 로고    scopus 로고
    • Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana
    • Tognolli M., Penel C., Greppin H., Simon P. Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana. Gene. 288:2002;129-138.
    • (2002) Gene , vol.288 , pp. 129-138
    • Tognolli, M.1    Penel, C.2    Greppin, H.3    Simon, P.4
  • 49
    • 0035253633 scopus 로고    scopus 로고
    • Improving the catalytic performance of peroxidases in organic synthesis
    • Van de Velde F., Van Rantwijk F., Sheldon R.A. Improving the catalytic performance of peroxidases in organic synthesis. Trends Biotechnol. 19:2001;73-80.
    • (2001) Trends Biotechnol. , vol.19 , pp. 73-80
    • Van De Velde, F.1    Van Rantwijk, F.2    Sheldon, R.A.3
  • 51
    • 0036015564 scopus 로고    scopus 로고
    • Indole-3-acetic acids and horseradish peroxidase: A new prodrug/enzyme combination for targeted cancer therapy
    • Wardman P. Indole-3-acetic acids and horseradish peroxidase: A new prodrug/enzyme combination for targeted cancer therapy. Current Pharmaceutical Design. 8:2002;1363-1374.
    • (2002) Current Pharmaceutical Design , vol.8 , pp. 1363-1374
    • Wardman, P.1
  • 52
    • 0017041348 scopus 로고
    • Covalent structure of the glycoprotein horseradish peroxidase
    • Welinder K.G. Covalent structure of the glycoprotein horseradish peroxidase. FEBS Lett. 72:1976;19-23.
    • (1976) FEBS Lett. , vol.72 , pp. 19-23
    • Welinder, K.G.1
  • 53
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • Welinder K.G. Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 2:1992;388-393.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 55
    • 0002037932 scopus 로고
    • Structure and evolution of peroxidases
    • K.G. Welinder, S.K. Rasmussen, C. Penel, & H. Greppin. Geneva: University of Geneva
    • Welinder K.G., Gajhede M. Structure and evolution of peroxidases. Welinder K.G., Rasmussen S.K., Penel C., Greppin H. Plant Peroxidases: Biochemistry and Physiology. 1993;35-42 University of Geneva, Geneva.
    • (1993) Plant Peroxidases: Biochemistry and Physiology , pp. 35-42
    • Welinder, K.G.1    Gajhede, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.