메뉴 건너뛰기




Volumn 90, Issue 9, 2008, Pages 1414-1421

Effects of mutations in the helix G region of horseradish peroxidase

Author keywords

Horseradish peroxidase; Protein stabilisation; Recombinant; Site specific mutagenesis

Indexed keywords

HORSERADISH PEROXIDASE; REDUCING AGENT; SOLVENT;

EID: 47749085447     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2008.05.008     Document Type: Article
Times cited : (10)

References (58)
  • 1
    • 33745932472 scopus 로고    scopus 로고
    • Horseradish and soybean peroxidases: comparable tools for alternative niches?
    • Ryan B.J., Carolan N., and O'Fágáin C. Horseradish and soybean peroxidases: comparable tools for alternative niches?. Trends in Biotechnology 24 (2006) 355-363
    • (2006) Trends in Biotechnology , vol.24 , pp. 355-363
    • Ryan, B.J.1    Carolan, N.2    O'Fágáin, C.3
  • 2
    • 0030742880 scopus 로고    scopus 로고
    • Catalytic activities and structural properties of horseradish peroxidase distal His42 to Glu or Gln mutant
    • Tanaka M., Ishimori K., Mukai M., Kitagawa T., and Morishima I. Catalytic activities and structural properties of horseradish peroxidase distal His42 to Glu or Gln mutant. Biochemistry 36 (1997) 9889-9898
    • (1997) Biochemistry , vol.36 , pp. 9889-9898
    • Tanaka, M.1    Ishimori, K.2    Mukai, M.3    Kitagawa, T.4    Morishima, I.5
  • 3
    • 0029661445 scopus 로고    scopus 로고
    • Rescue of His-42 to Ala horseradish peroxidase by a Phe-41 to His mutation - engineering of a surrogate catalytic histidine
    • Savenkova M.I., Newmyer S.L., and De Montellano P.R.O. Rescue of His-42 to Ala horseradish peroxidase by a Phe-41 to His mutation - engineering of a surrogate catalytic histidine. Journal of Biological Chemistry 271 (1996) 24598-24603
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 24598-24603
    • Savenkova, M.I.1    Newmyer, S.L.2    De Montellano, P.R.O.3
  • 4
    • 0028833821 scopus 로고
    • Ortiz de Montellano PR, Molecular engineering of horseradish peroxidase. Thioether sulfoxidation and styrene epoxidation by Phe-41 leucine and threonine mutants
    • Ozaki S. Ortiz de Montellano PR, Molecular engineering of horseradish peroxidase. Thioether sulfoxidation and styrene epoxidation by Phe-41 leucine and threonine mutants. Journal of the American Chemical Society 117 (1995) 7056-7064
    • (1995) Journal of the American Chemical Society , vol.117 , pp. 7056-7064
    • Ozaki, S.1
  • 5
    • 0033543221 scopus 로고    scopus 로고
    • Luminol activity of horseradish peroxidase mutants mimicking a proposed binding site for luminol in Arthromyces ramosus peroxidase
    • Tanaka M., Ishimori K., and Morishima I. Luminol activity of horseradish peroxidase mutants mimicking a proposed binding site for luminol in Arthromyces ramosus peroxidase. Biochemistry 38 (1999) 10463-10473
    • (1999) Biochemistry , vol.38 , pp. 10463-10473
    • Tanaka, M.1    Ishimori, K.2    Morishima, I.3
  • 9
    • 0034635116 scopus 로고    scopus 로고
    • Structural and conformational stability of horseradish peroxidase: effect of temperature and pH
    • Chattopadhyay K., and Mazumdar S. Structural and conformational stability of horseradish peroxidase: effect of temperature and pH. Biochemistry 39 (2000) 263-270
    • (2000) Biochemistry , vol.39 , pp. 263-270
    • Chattopadhyay, K.1    Mazumdar, S.2
  • 10
    • 0032705121 scopus 로고    scopus 로고
    • Horseradish peroxidase monitored by infrared spectroscopy: effect of temperature, substrate and calcium
    • Kaposi A.D., Fidy J., Manas E.S., Vanderkooi J.M., and Wright W.W. Horseradish peroxidase monitored by infrared spectroscopy: effect of temperature, substrate and calcium. Biochimica et Biophysica Acta 1435 (1999) 41-50
    • (1999) Biochimica et Biophysica Acta , vol.1435 , pp. 41-50
    • Kaposi, A.D.1    Fidy, J.2    Manas, E.S.3    Vanderkooi, J.M.4    Wright, W.W.5
  • 11
    • 0032536139 scopus 로고    scopus 로고
    • Glycosylation and thermodynamic versus kinetic stability of horseradish peroxidase
    • Tams J.W., and Welinder K.G. Glycosylation and thermodynamic versus kinetic stability of horseradish peroxidase. FEBS Letters 421 (1998) 234-236
    • (1998) FEBS Letters , vol.421 , pp. 234-236
    • Tams, J.W.1    Welinder, K.G.2
  • 12
    • 0036220998 scopus 로고    scopus 로고
    • The enzyme horseradish peroxidase is less compressible at higher pressures
    • Smeller L., and Fidy J. The enzyme horseradish peroxidase is less compressible at higher pressures. Biophysical Journal 82 (2002) 426-436
    • (2002) Biophysical Journal , vol.82 , pp. 426-436
    • Smeller, L.1    Fidy, J.2
  • 16
    • 0033556088 scopus 로고    scopus 로고
    • Structural changes of horseradish peroxidase in presence of low concentrations of urea
    • Haque M.E., Debnath D., Basak S., and Chakrabarti A. Structural changes of horseradish peroxidase in presence of low concentrations of urea. European Journal of Biochemistry 259 (1999) 269-274
    • (1999) European Journal of Biochemistry , vol.259 , pp. 269-274
    • Haque, M.E.1    Debnath, D.2    Basak, S.3    Chakrabarti, A.4
  • 17
    • 0029858291 scopus 로고    scopus 로고
    • Structural alterations of horseradish peroxidase in the presence of low concentrations of guanidinium chloride
    • Chakrabarti A., and Basak S. Structural alterations of horseradish peroxidase in the presence of low concentrations of guanidinium chloride. European Journal of Biochemistry 241 (1996) 462-467
    • (1996) European Journal of Biochemistry , vol.241 , pp. 462-467
    • Chakrabarti, A.1    Basak, S.2
  • 18
    • 0037193185 scopus 로고    scopus 로고
    • Effect of dimethyl sulfoxide on the structure of the functional properties of horseradish peroxidase as observed by spectroscopy and cyclic voltammetry
    • Santucci R., Laurenti E., Sinibaldi F., and Ferrari R.P. Effect of dimethyl sulfoxide on the structure of the functional properties of horseradish peroxidase as observed by spectroscopy and cyclic voltammetry. Biochimica et Biophysica Acta 1596 (2002) 225-233
    • (2002) Biochimica et Biophysica Acta , vol.1596 , pp. 225-233
    • Santucci, R.1    Laurenti, E.2    Sinibaldi, F.3    Ferrari, R.P.4
  • 19
    • 24744435515 scopus 로고    scopus 로고
    • Thermal stability and activity regain of horseradish peroxidase in aqueous mixtures of imidazolium-based ionic liquids
    • Machado M.F., and Saraiva J.M. Thermal stability and activity regain of horseradish peroxidase in aqueous mixtures of imidazolium-based ionic liquids. Biotechnology Letters 27 (2005) 1233-1239
    • (2005) Biotechnology Letters , vol.27 , pp. 1233-1239
    • Machado, M.F.1    Saraiva, J.M.2
  • 20
    • 0034842869 scopus 로고    scopus 로고
    • Functional expression and stabilization of horseradish peroxidase by directed evolution in Saccharomyces cerevisiae
    • Morawski B., Quan S., and Arnold F.H. Functional expression and stabilization of horseradish peroxidase by directed evolution in Saccharomyces cerevisiae. Biotechnology and Bioengineering 76 (2001) 99-107
    • (2001) Biotechnology and Bioengineering , vol.76 , pp. 99-107
    • Morawski, B.1    Quan, S.2    Arnold, F.H.3
  • 21
    • 33644891075 scopus 로고    scopus 로고
    • Increased thermal and organic solvent tolerance of modified horseradish peroxidase, Protein Engineering
    • Liu J.Z., Wang T.L., Huang M.T., Song H.Y., Weng L.P., and Ji L.N. Increased thermal and organic solvent tolerance of modified horseradish peroxidase, Protein Engineering. Design & Selection 19 (2006) 169-173
    • (2006) Design & Selection , vol.19 , pp. 169-173
    • Liu, J.Z.1    Wang, T.L.2    Huang, M.T.3    Song, H.Y.4    Weng, L.P.5    Ji, L.N.6
  • 22
    • 0442307778 scopus 로고    scopus 로고
    • The application of O-aminopropyl amylose for the stabilisation of horseradish peroxidase via addition and crosslinking
    • Gonera A., Mischnick P., and Ukeda H. The application of O-aminopropyl amylose for the stabilisation of horseradish peroxidase via addition and crosslinking. Enzyme and Microbial Technology 34 (2004) 248-254
    • (2004) Enzyme and Microbial Technology , vol.34 , pp. 248-254
    • Gonera, A.1    Mischnick, P.2    Ukeda, H.3
  • 23
    • 0035829832 scopus 로고    scopus 로고
    • Location of crosslinks in chemically stabilised horseradish peroxidase. Implications for design of crosslinks
    • O'Brien A.M., O'Fágáin C., Nielsen P.F., and Welinder K.G. Location of crosslinks in chemically stabilised horseradish peroxidase. Implications for design of crosslinks. Biotechnology and Bioengineering 76 (2001) 277-284
    • (2001) Biotechnology and Bioengineering , vol.76 , pp. 277-284
    • O'Brien, A.M.1    O'Fágáin, C.2    Nielsen, P.F.3    Welinder, K.G.4
  • 24
    • 0030248390 scopus 로고    scopus 로고
    • Modification of horseradish peroxidase with bifunctional N-hydroxysuccinimide esters: effects on molecular stability
    • Miland E., Smyth M.R., and O'Fágáin C. Modification of horseradish peroxidase with bifunctional N-hydroxysuccinimide esters: effects on molecular stability. Enzyme and Microbial Technology 19 (1996) 242-249
    • (1996) Enzyme and Microbial Technology , vol.19 , pp. 242-249
    • Miland, E.1    Smyth, M.R.2    O'Fágáin, C.3
  • 25
    • 0028363563 scopus 로고
    • Thermostabilised chemical derivatives of horseradish peroxidase
    • Ryan O., Smyth M.R., and O'Fágáin C. Thermostabilised chemical derivatives of horseradish peroxidase. Enzyme and Microbial Technology 16 (1994) 501-505
    • (1994) Enzyme and Microbial Technology , vol.16 , pp. 501-505
    • Ryan, O.1    Smyth, M.R.2    O'Fágáin, C.3
  • 27
    • 0347297131 scopus 로고    scopus 로고
    • Effects of phthalic anhydride modification on horseradish peroxidase stability and activity
    • O'Brien A.M., Smith A.T., and O'Fágáin C. Effects of phthalic anhydride modification on horseradish peroxidase stability and activity. Biotechnology and Bioengineering 81 (2003) 233-240
    • (2003) Biotechnology and Bioengineering , vol.81 , pp. 233-240
    • O'Brien, A.M.1    Smith, A.T.2    O'Fágáin, C.3
  • 28
    • 0037164183 scopus 로고    scopus 로고
    • Increased thermostability and phenol removal efficiency by chemical modified horseradish peroxidase
    • Liu J.Z., Song H.Y., Weng L.P., and Ji L.N. Increased thermostability and phenol removal efficiency by chemical modified horseradish peroxidase. Journal of Molecular Catalysis B 18 (2002) 225-232
    • (2002) Journal of Molecular Catalysis B 18 , pp. 225-232
    • Liu, J.Z.1    Song, H.Y.2    Weng, L.P.3    Ji, L.N.4
  • 29
    • 0030200465 scopus 로고    scopus 로고
    • Increased thermal and solvent tolerance of acetylated horseradish peroxidase
    • Miland E., Smyth M.R., and O'Fágáin C. Increased thermal and solvent tolerance of acetylated horseradish peroxidase. Enzyme and Microbial Technology 19 (1996) 63-67
    • (1996) Enzyme and Microbial Technology , vol.19 , pp. 63-67
    • Miland, E.1    Smyth, M.R.2    O'Fágáin, C.3
  • 30
    • 0033136115 scopus 로고    scopus 로고
    • Functional expression of horseradish peroxidase in E. coli by directed evolution
    • Lin Z., Thorsen T., and Arnold F.H. Functional expression of horseradish peroxidase in E. coli by directed evolution. Biotechnology Progress 15 (1999) 457-471
    • (1999) Biotechnology Progress , vol.15 , pp. 457-471
    • Lin, Z.1    Thorsen, T.2    Arnold, F.H.3
  • 32
    • 0023410604 scopus 로고
    • Characterisation of the Erwinia carotovora pelB gene and its product pectate lyase
    • Lei S.P., Lin H.C., Wang S.S., Callaway J., and Wilcox G. Characterisation of the Erwinia carotovora pelB gene and its product pectate lyase. Journal of Bacteriology 169 (1987) 4379-4383
    • (1987) Journal of Bacteriology , vol.169 , pp. 4379-4383
    • Lei, S.P.1    Lin, H.C.2    Wang, S.S.3    Callaway, J.4    Wilcox, G.5
  • 34
    • 0032957639 scopus 로고    scopus 로고
    • Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuickChange™ site-directed mutagenesis
    • Wang W., and Malcom B.A. Two-stage PCR protocol allowing introduction of multiple mutations, deletions and insertions using QuickChange™ site-directed mutagenesis. BioTechniques 26 (1999) 680-682
    • (1999) BioTechniques , vol.26 , pp. 680-682
    • Wang, W.1    Malcom, B.A.2
  • 35
    • 0030269967 scopus 로고    scopus 로고
    • Development of a simple method for the recovery of recombinant proteins from the E. coli periplasm
    • French C., Keshavarz-Moore E., and Ward J.M. Development of a simple method for the recovery of recombinant proteins from the E. coli periplasm. Enzyme and Microbial Technology 19 (1996) 332-338
    • (1996) Enzyme and Microbial Technology , vol.19 , pp. 332-338
    • French, C.1    Keshavarz-Moore, E.2    Ward, J.M.3
  • 36
    • 0026695468 scopus 로고
    • Characterisation of a heme active-site mutant of horseradish peroxidase, 41-Phe-Val, with altered reactivity towards hydrogen peroxide and reducing substrates
    • Smith A.T., Sanders S.A., Thorneley R.N.F., Burke J.F., and Bray R.R.C. Characterisation of a heme active-site mutant of horseradish peroxidase, 41-Phe-Val, with altered reactivity towards hydrogen peroxide and reducing substrates. European Journal of Biochemistry 207 (1992) 507-519
    • (1992) European Journal of Biochemistry , vol.207 , pp. 507-519
    • Smith, A.T.1    Sanders, S.A.2    Thorneley, R.N.F.3    Burke, J.F.4    Bray, R.R.C.5
  • 37
    • 84987261038 scopus 로고
    • Thermal inactivation kinetics of horseradish peroxidase
    • Chang B.S., Park K.H., and Lund D.B. Thermal inactivation kinetics of horseradish peroxidase. Journal of Food Science 53 (1988) 920-923
    • (1988) Journal of Food Science , vol.53 , pp. 920-923
    • Chang, B.S.1    Park, K.H.2    Lund, D.B.3
  • 38
    • 0025882622 scopus 로고
    • Denaturation capacity: a new quantitative criterion for selection of organic solvents as reaction media in biocatalysis
    • Khmelnitsky Y.L., Mozhaev V.V., Belova A.B., Sergeeva M.V., and Martinek K. Denaturation capacity: a new quantitative criterion for selection of organic solvents as reaction media in biocatalysis. European Journal of Biochemistry 198 (1991) 31-41
    • (1991) European Journal of Biochemistry , vol.198 , pp. 31-41
    • Khmelnitsky, Y.L.1    Mozhaev, V.V.2    Belova, A.B.3    Sergeeva, M.V.4    Martinek, K.5
  • 40
    • 0003514551 scopus 로고    scopus 로고
    • John Wiley and Sons, New York 1-23, 92-111
    • Dunford H.B. Heme Peroxidases (1999), John Wiley and Sons, New York 1-23, 92-111
    • (1999) Heme Peroxidases
    • Dunford, H.B.1
  • 41
    • 0018788891 scopus 로고
    • Chemical modification of the ε-amino groups of lysine residues in horseradish peroxidase and its effect on the catalytic properties and thermostability of the enzyme
    • Ugarova N.N., Rozhkova G.D., and Berezin I.V. Chemical modification of the ε-amino groups of lysine residues in horseradish peroxidase and its effect on the catalytic properties and thermostability of the enzyme. Biochimica et Biophysica Acta 570 (1979) 31-42
    • (1979) Biochimica et Biophysica Acta , vol.570 , pp. 31-42
    • Ugarova, N.N.1    Rozhkova, G.D.2    Berezin, I.V.3
  • 42
    • 0026078438 scopus 로고
    • Use of pyrocarbonate for chemical modification of histidine residues of horseradish peroxidase
    • Urrutigoity M., Baboulene M., and Lattes A. Use of pyrocarbonate for chemical modification of histidine residues of horseradish peroxidase. Bioorganic Chemistry 19 (1991) 66-76
    • (1991) Bioorganic Chemistry , vol.19 , pp. 66-76
    • Urrutigoity, M.1    Baboulene, M.2    Lattes, A.3
  • 43
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modelling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-Pdb Viewer: an environment for comparative protein modelling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 45
    • 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., and Smulevich G. The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase. Journal of Biological Chemistry 276 (2001) 40704-40711
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 40704-40711
    • Howes, B.D.1    Feis, A.2    Raimondi, L.3    Indiani, C.4    Smulevich, G.5
  • 47
    • 33846833785 scopus 로고    scopus 로고
    • Structural stabilisation and functional improvement of horseradish peroxidase upon modification of accessible lysines: experiments and simulation
    • Mogharrab N., Ghourchian H., and Amininasab M. Structural stabilisation and functional improvement of horseradish peroxidase upon modification of accessible lysines: experiments and simulation. Biophysical Journal 92 (2007) 1192-1203
    • (2007) Biophysical Journal , vol.92 , pp. 1192-1203
    • Mogharrab, N.1    Ghourchian, H.2    Amininasab, M.3
  • 48
    • 0031432888 scopus 로고    scopus 로고
    • Influence of immobilization on enzyme activity in aqueous-organic cosolvent mixtures
    • Batra R., Tyagi R., and Gupta M.N. Influence of immobilization on enzyme activity in aqueous-organic cosolvent mixtures. Biocatalysis and Biotransformation 15 (1997) 101-119
    • (1997) Biocatalysis and Biotransformation , vol.15 , pp. 101-119
    • Batra, R.1    Tyagi, R.2    Gupta, M.N.3
  • 50
    • 0031984007 scopus 로고    scopus 로고
    • Kinetics of inactivation of horseradish peroxidase: stabilizing effect of methoxypoly(ethylene glycol)
    • Garcia D., Ortega F., and Marty J.L. Kinetics of inactivation of horseradish peroxidase: stabilizing effect of methoxypoly(ethylene glycol). Biotechnology and Applied Biochemistry 27 (1998) 49-54
    • (1998) Biotechnology and Applied Biochemistry , vol.27 , pp. 49-54
    • Garcia, D.1    Ortega, F.2    Marty, J.L.3
  • 52
    • 0035830685 scopus 로고    scopus 로고
    • Thermostabilisation of a chimeric enzyme by residue substitutions: four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase
    • Numata K., Hayashi-Iwasaki Y., Kawaguchi J., Sakurai M., Moriyama H., Tanaka N., and Oshima T. Thermostabilisation of a chimeric enzyme by residue substitutions: four amino acid residues in loop regions are responsible for the thermostability of Thermus thermophilus isopropylmalate dehydrogenase. Biochimica et Biophysica Acta 1545 (2001) 174-183
    • (2001) Biochimica et Biophysica Acta , vol.1545 , pp. 174-183
    • Numata, K.1    Hayashi-Iwasaki, Y.2    Kawaguchi, J.3    Sakurai, M.4    Moriyama, H.5    Tanaka, N.6    Oshima, T.7
  • 53
    • 0035078662 scopus 로고    scopus 로고
    • 1 site of bovine pancreatic trypsin inhibitor affect its stability
    • 1 site of bovine pancreatic trypsin inhibitor affect its stability. Protein Science 10 (2001) 715-724
    • (2001) Protein Science , vol.10 , pp. 715-724
    • Krowarsch, D.1    Otlewski, J.2
  • 54
    • 0035808971 scopus 로고    scopus 로고
    • Identification of thermostabilising residues in a Bacillus alkaline cellulase by construction of chimeras from mesophilic and thermostable enzymes and site directed mutagenesis
    • Hakamada Y., Hatada Y., Ozawa T., Ozaki K., Kobayashi T., and Ito S. Identification of thermostabilising residues in a Bacillus alkaline cellulase by construction of chimeras from mesophilic and thermostable enzymes and site directed mutagenesis. FEMS Microbiology Letters 195 (2001) 67-72
    • (2001) FEMS Microbiology Letters , vol.195 , pp. 67-72
    • Hakamada, Y.1    Hatada, Y.2    Ozawa, T.3    Ozaki, K.4    Kobayashi, T.5    Ito, S.6
  • 55
    • 34447094807 scopus 로고    scopus 로고
    • Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide
    • Ryan B.J., and Ó'Fágáin C. Effects of single mutations on the stability of horseradish peroxidase to hydrogen peroxide. Biochimie 89 (2007) 1029-1032
    • (2007) Biochimie , vol.89 , pp. 1029-1032
    • Ryan, B.J.1    Ó'Fágáin, C.2
  • 58
    • 33847614353 scopus 로고    scopus 로고
    • Hybrid penicillin acylases with improved properties for synthesis of β-lactam antibiotics
    • Jager S.A.W., Jekel P.A., and Janssen D.B. Hybrid penicillin acylases with improved properties for synthesis of β-lactam antibiotics. Enzyme and Microbial Technology 40 (2007) 1335-1344
    • (2007) Enzyme and Microbial Technology , vol.40 , pp. 1335-1344
    • Jager, S.A.W.1    Jekel, P.A.2    Janssen, D.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.