New approaches for functional expression of recombinant horseradish peroxidase C in Escherichia coli

Biocatalysis and Biotransformation

Volumn 17, Issue 5, 1999, Pages 359-379

  Grigorenko, Vitaly ^a   Chubar, Tatiana ^a   Kapeliuch, Yury ^a   Börchers, Torsten ^b   Spener, Friedrich ^c   Egorov, Alexey ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b ICB Institut fur Chemo und Biosensorik GmbH   (Germany)

^c UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

E. coli; Horseradish peroxidase; Periplasm; Recombinant holoprotein; Refolding

Indexed keywords

BIOLOGICAL MATERIALS; CATALYSIS; CHEMICAL ANALYSIS; ESCHERICHIA COLI; FILTRATION; IMMUNOLOGY;

CULTURE MEDIUM; HORSERADISH PEROXIDASE; IMMUNOCHEMICAL ANALYSIS;

ENZYMES;

HISTIDINE; HORSERADISH PEROXIDASE; IMIDAZOLE; PLANT EXTRACT; RECOMBINANT ENZYME; SULFONIC ACID DERIVATIVE;

ARTICLE; CATALYSIS; CELL INCLUSION; CULTURE MEDIUM; CYTOPLASM; ENZYME CONFORMATION; ENZYME SUBSTRATE; ENZYME SYNTHESIS; ESCHERICHIA COLI; GEL FILTRATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PROCESSING; SPECTROSCOPY;

ARMORACIA RUSTICANA; ESCHERICHIA COLI;

EID: 0033375087     PISSN: 10242422     EISSN: None     Source Type: Journal    
DOI: 10.3109/10242429909015236     Document Type: Article

References (38)

1. Bradford, M M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
2. Chiswell, D.J. and Ortlepp, S.A. (1989) DNA sequence coding for HRP enzyme. European patent No EP0299682.
3. Dalton, D.A., Diaz del Castillo, L., Kahn, M.L., Joyner, S.L. and Chatfield, J.M. (1996) Heterologous expression and characterization of soybean cytosolic ascorbate peroxidase. Archives of Biochemistry and Biophysics, 328, 1-8.
4. Dunford, H.B. and Stillman, J.S. (1976) On the function and mechanism of action of peroxidases, Coordination Chemistry Reviews, 19, 187-251.
5. Egorov, A.M., Gazaryan, I.G., Kim, B.B., Doseeva, V.V., Kapeliuch, J.L., Veryovkin, A.N. and Fechina, V.A. (1994) Horseradish peroxidase isozyme C. A comparative study of native and recombinant enzyme produced by E. coli transformants. Annals New York Academy of Sciences, 721, 73-82.
6. Freedman, R.B. (1995) The formation of protein disulphide bonds. Current Opinion in Structural Biology, 5, 85-91.
7. Fuhrhop, J.-H. and Smith, K.M. (1975) Laboratory Methods. In Porphyrins and Metalloproteins (Ed. K.M. Smith). Elsevier, Amsterdam, pp. 757-869.
8. Gajhede, M., Schuller, D.J., Henriksen, A., Smith, A.T. and Poulos, T.L. (1997) Crystal structure of horseradish peroxidase C at 2.15 Å resolution. Nature Structural Biology, 4, 1032-1038.
9. Gazaryan, I.G., Doseeva, V.V., Galkin, A.G. and Tishkov, V.I. (1994) Effect of single-point mutations Phe41 → His and Phe143 → Glu on folding and catalytic properties of recombinant horseradish peroxidase expressed in E. coli. FEBS Letters, 354, 248-250.
10. George, P. (1953) The chemical nature of the second hydrogen peroxide compound formed by cytochrome c peroxidase and horseradish peroxidase. Biochemical Journal, 54, 267-271.
11. Gillet, D., Ducancel, F., Pradel, E., Leonetti, M., Menez, A. and Boulain, J.C. (1992) Insertion of a disulfide-containing neurotoxin into E. coli alkaline phosphatase: the hybrid retains both biological activities. Protein Engineering, 5, 273-278.
12. Hargrove, M.S., Krzywda, S., Wilkinson, A.J., Dou, Y., Ikeda-Saito, M. and Olson, J.S. (1994) Stability of myoglobin: a model for the folding of heme proteins. Biochemistry, 33, 11769-11775.
13. Hartmann, C. and Ortiz de Montellano, P.R. (1992) Baculovirus expression and characterization of catalytically active horseradish peroxidase. Archives of Biochemistry and Biophysics, 297, 61-72.
14. Howes, B.D., Rodriguez-Lopez, J.N., Smith, A.T. and Smulevich, G. (1997) Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity properties. Biochemistry, 36, 1532-1543.
15. Johnson, M.L. and Frasier, S.G. (1985) Nonlinear least-squares analysis. Methods in Enzymology, 117, 301-342.
16. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
17. Le, H.V. and Trotta, P.P. (1991) Purification of secreted recombinant proteins from Escherichia coli. Bioprocess Technology, 12, 163-181.
18. Machamer, C.E. and Rose, L.K. (1988) Vesicular stomatitis virus G proteins with altered glycosylation sites display temperature-sensitive intracellular transport and are subject to aberrant intermolecular disulfide bonding. Journal of Biological Chemistry, 263, 5955-5960.
19. Mazza, G. and Welinder, K.G. (1980) Covalent structure of turnip peroxidase 7. Cyanogen bromide fragments, complete structure and comparison to horseradish peroxidase C. European Journal of Biochemistry, 108, 481-489.
20. Meunier, B., Rodriguez-Lopez, J.N., Smith, A.T., Thorneley, R.N.F. and Rich, P.R. (1995) Laser photolysis behavior of ferrous horseradish peroxidase with carbon monoxide and cyanide: effects of mutations in the distal heme pocket. Biochemistry, 34, 14687-14692.
21. Miller, V.P., Goodin, D.B., Friedman, A.E., Hartmann, C. and Ortiz de Montellano, P.R. (1995) Horseradish peroxidase Phe172 → Tyr mutant. Sequential formation of compound I with a porphyrin radical cation and a protein radical. Journal of Biological Chemistry, 270, 18413-18419.
22. Newmyer, S.L. and Ortiz de Montellano, P.R. (1996) Rescue of the catalytic activity of an H42A mutant of horseradish peroxidase by exogenous imidazoles. Journal of Biological Chemistry, 271, 14891-14896.
23. Newmyer, S.L., Sun, J., Loehr, T.M. and Ortiz de Montellano, P.R. (1996) Rescue of the horseradish peroxidase His-170 → Ala mutant activity by imidazole: importance of proximal ligand tethering. Biochemistry, 35, 12788-12795.
24. Ouzzine, M., Boyd, A. and Hulmes, D.J. (1996) Expression of active, human lysyl oxidase in Escherichia coli. FEBS Letters, 399, 215-219.
25. Phelps, C., Antonini, E. (1969) The combination of carbon monoxide-haem with apoperoxidase. Biochemical Journal, 114, 719-724.
26. Rubtsova, M.Y., Kovba, G.V. and Egorov, A.M. (1998) Chemiluminescent biosensors based on porous supports with immobilized peroxidase. Biosensors & Bioelectronics, 13, 75-85.
27. Ruzgas, T., Gorton, L., Emneus, J. and Marko-Varga, G. (1995) Kinetic models of horseradish peroxidase action on a graphite electrode. Journal of Electroanalytical Chemistry, 391, 41-49.
28. Savenkova, M.I., Newmyer, S.L. and Ortez de Montellano, P.R. (1996) Rescue of His-42 → Ala horseradish peroxidase by a Phe-41 → His mutation. Engineering of a surrogate catalytic histidine. Journal of Biological Chemistry, 271, 24598-24603.
29. Skerra, A. and Plückthun, A. (1988) Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science, 240, 1038-1041.
30. 2+ and heme. Journal of Biological Chemistry, 265, 13335-13343.
31. Smith, A.T., Sanders, S.A., Thorneley, R.N.F., Burke, J.F. and Bray, R.R.C. (1992) Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41-Va1, with altered reactivity towards hydrogen peroxide and reducing substrates. European Journal of Biochemistry, 201, 501-519.
32. Studier, F.W., Rosenberg, A.H., Dunn, J.J. and Dubendorf, J.W. (1990) Use of T7 RNA polymerase to direct expression of cloned genes. Methods in Enzymology, 185, 60-89.
33. Tams, J.W. and Welinder, K.G. (1995) Mild chemical deglycosylation of horseradish peroxidase yields a fully active, homogeneous enzyme. Analytical Biochemistry, 228, 48-55.
34. Tien, M. and Tu, C-P. (1987) Cloning and sequencing of a cDNA for a ligninase from Phanerochaete chrysosporium. Nature, 326, 520-523.
35. Verezin, I.C., Ugarova, N.N., Kershchengolbts, B.M. and Brovko, L.I.U. (1975) Effect of prosthetic group of horseradish peroxidase on enzyme stability (in Russian) Biokhimiia, 40, 297-301.
36. Vlamis-Gardikas, A., Smith, A.T., Clements, J.M. and Burke, J.F. (1992) Expression of active horseradish peroxidase in Saccharomyces cerevisiae. Biochemical Society Transactions, 20, 111S.
37. Welinder, K.G. (1979) Amino acid sequence studies of horseradish peroxidase. Amino and carboxyl termini, cyanogen bromide and tryptic fragments, the complete sequence, and some structural characteristics of horseradish peroxidase C. European Journal of Biochemistry, 96, 483-502.
38. Wulfing, C. and Plückthun, A. (1994) An Escherichia coli protein consisting of a domain homologous to FK506-binding proteins (FKBP) and a new metal binding motif. Journal Molecular Biology, 242, 655-669.