l-Asparaginase from Erwinia Chrysanthemi 3937: Cloning, expression and characterization

Journal of Biotechnology

Volumn 127, Issue 4, 2007, Pages 657-669

  Kotzia, Georgia A ^a   Labrou, Nikolaos E ^a  

^a AGRICULTURAL UNIVERSITY OF ATHENS   (Greece)

Author keywords

Enzyme immobilization; Hydrolase; l Asparaginase; Leukaemia

Indexed keywords

BIOREACTORS; CLONING; ESCHERICHIA COLI; GENES; ION EXCHANGE; REACTION KINETICS;

HYDROLASE; L-ASPARAGINASE; LEUKAEMIA;

ENZYMES;

AMMONIA; ASPARAGINASE; ASPARAGINE; ASPARTIC ACID; RECOMBINANT ENZYME; SEPHAROSE;

AMINO TERMINAL SEQUENCE; ARTICLE; BIOREACTOR; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME IMMOBILIZATION; ENZYME KINETICS; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; ION EXCHANGE CHROMATOGRAPHY; LEUKEMIA; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PECTOBACTERIUM CHRYSANTHEMI; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE ANALYSIS; THERMOSTABILITY;

AMINO ACID SEQUENCE; ANTINEOPLASTIC AGENTS; ASPARAGINASE; BACTERIAL PROTEINS; CLONING, MOLECULAR; ESCHERICHIA COLI; HEAT; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PECTOBACTERIUM CHRYSANTHEMI; SEQUENCE ALIGNMENT; STEREOISOMERISM;

BACTERIA (MICROORGANISMS); ERWINIA CHRYSANTHEMI STR. 3937; ESCHERICHIA COLI;

EID: 33845649780     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.07.037     Document Type: Article

References (59)

1. Aghaiypour K., Wlodawer A., and Lubkowski J. Do bacterial l-asparaginases utilize a catalytic triad Thr-Tyr-Glu?. Biochim. Biophys. Acta 1550 (2001) 117-128
2. Aghaiypour K., Wlodawer A., and Lubkowski J. Structural basis for the activity and substrate specificity of Er. chrysanthemi l-asparaginase. Biochemistry 40 (2001) 5655-5664
3. Altschul S.F., Gish W., Miller W., Myers E.W., and Lipman D.J. Basic local alignment search tool. J. Mol. Biol. 215 (1990) 403-410
4. Aung H.P., Bocola M., Schleper S., and Rohm K.H. Dynamics of a mobile loop at the active site of Escherichia coli asparaginase. Biochim. Biophys. Acta 1481 (2000) 349-359
5. Avramis V.I., and Panosyan E.H. Pharmacokinetic/pharmacodynamic relationships of asparaginase formulations: the past, the present and recommendations for the future. Clin. Pharmacokinet. 44 (2005) 367-393
6. Axarli I., Prigipaki A., and Labrou N.E. Engineering cytochrome P450 CYP102A2 substrate specificity by directed evolution: production of an efficient enzyme for bioconversion of fine chemicals. Biomol. Eng. 22 (2005) 81-88
7. 6-ethanoadenosine 2′,5′-biphosphate. Biochemistry 35 (1985) 2658-2667
8. Balcao V.M., Mateo C., Fernandez-Lafuente R., Malcata F.X., and Guisan J.M. Structural and functional stabilization of l-asparaginase via multisubunit Immobilization onto highly activated supports. Biotechnol. Prog. 17 (2001) 537-542
9. Boyse E.A., Old L.J., Campbell H.A., and Mashburn L.T. Suppression of murine leukemias by l-asparaginase. Incidence of sensitivity among leukemias of various types: comparative inhibitory activities of guinea pig serum l-asparaginase and Escherichia coli l-asparaginase. J. Exp. Med. 125 (1967) 17-31
10. Bradford M.A. 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
11. Cammack K.A., Marlborough D.I., and Miller D.S. Physical properties and subunit structure of l-asparaginase isolated from Erwinia carotovora. Biochem. J. 126 (1972) 361-379
12. Chang T.M. Artificial cells in medicine and biotechnology. Appl. Biochem. Biotechnol. 10 (1984) 5-24
13. DeLano W.L. The PyMOL Molecular Graphics System (2002), DeLano Scientific, San Carlos, USA
14. DeLoach J.R., Andrews K., Satterfield W., and Keeling M. Intraperitoneal administration of carrier erythrocytes in dogs: an improved method for delivery of l-asparaginase. Biotechnol. Appl. Biochem. 12 (1990) 331-335
15. Derst C., Henseling J., and Rohm K.H. Engineering the substrate specificity of Escherichia coli asparaginase II. Selective reduction of glutaminase activity by amino acid replacements at position 248. Protein Sci. 9 (2000) 2009-2017
16. Duval M., Suciu S., Ferster A., Rialland X., Nelken B., Lutz P., Benoit Y., Robert A., Manel A.M., Vilmer E., Otten J., and Philippe N. Comparison of Escherichia coli-asparaginase with Erwinia-asparaginase in the treatment of childhood lymphoid malignancies: results of a randomized European Organization for Research and Treatment of Cancer-Children's Leukemia Group phase 3 trial. Blood 99 (2002) 2734-2739
17. Ehrman M., Cedar H., and Schwartz J.H. l-Asparaginase II of Escherichia coli. Studies on the enzymatic mechanism of action. J. Biol. Chem. 246 (1971) 88-94
18. Eijsink V.G., Gaseidnes S., Borchert T.V., and van den Burg B. Directed evolution of enzyme stability. Biomol. Eng. 22 (2005) 21-30
19. Fan Y.X., McPhie P., and Miles E.W. Regulation of tryptophan synthase by temperature, monovalent cations, and an allosteric ligand. Evidence from Arrhenius plots, absorption spectra, and primary kinetic isotope effects. Biochemistry 39 (2000) 4692-4703
20. Fernandes A.I., and Gregoriadis G. Polysialylated asparaginase: preparation, activity and pharmacokinetics. Biochim. Biophys. Acta 1341 (1997) 26-34
21. Filpula D., Nagle J.W., Pulford S., and Anderson D.M. Sequence of l-asparaginase gene from Erwinia chrysanthemi NCPPB 1125. Nucleic Acids Res. 16 (1988) 10385
22. Freire E., van Osdol W.W., Mayorga O.L., and Sanchez-Ruiz J.M. Calorimetrically determined dynamics of complex unfolding transitions in proteins. Annu. Rev. Biophys. Biophys. Chem. 19 (1990) 159-188
23. Goward C.R., Stevens G.B., Tattersall R., and Atkinson T. Rapid large-scale preparation of recombinant Erwinia chrysanthemi l-asparaginase. Bioseparation 2 (1992) 335-341
24. Hawkins D.S., Park J.R., Thomson B.G., Felgenhauer J.L., Holcenberg J.S., Panosyan E.H., and Avramis V.I. Asparaginase pharmacokinetics after intensive polyethylene glycol-conjugated l-asparaginase therapy for children with relapsed acute lymphoblastic leukemia. Clin. Cancer Res. 10 (2004) 5335-5341
25. Hibbert E.G., Baganz F., Hailes H.C., Ward J.M., Lye G.J., Woodley J.M., and Dalby P.A. Directed evolution of biocatalytic processes. Biomol. Eng. 22 (2005) 11-19
26. Howard J.B., and Carpenter F.H. l-Asparaginase from Erwinia carotovora. Substrate specificity and enzymatic properties. J. Biol. Chem. 247 (1972) 1020-1030
27. Jean-Francëois J., D'Urso E.M., and Fortier G. Immobilization of l-asparaginase into a biocompatible poly(ethylene glycol)-albumin hydrogel: evaluation of performance in vivo. Biotechnol. Appl. Biochem. 26 (1997) 203-212
28. Jorge J.C., Perez-Soler R., Morais J.G., and Cruz M.E. Liposomal palmitoyl-l-asparaginase: characterization and biological activity. Cancer Chemother. Pharmacol. 34 (1994) 230-234
29. Kamisaki Y., Wada H., Yagura T., Nishimura H., Matsushima A., and Inada Y. Increased antitumor activity of Escherichia coli l-asparaginase by modification with monomethoxypolyethylene glycol. Gann 73 (1982) 470-474
30. Katchalski-Katzir E., Kraemer D., and Eupergit M. A carrier for immobilization of enzymes of industrial potential. J. Mol. Catal. B: Enzym. 10 (2000) 157-176
31. Keating M.J., Holmes R., Lerner S., and Ho D.H. l-Asparaginase and PEG asparaginase-past, present, and future. Leuk. Lymphoma 10 (1993) 153-157
32. Kelo E., Noronkoski T., Stoineva I.B., Petkov D.D., and Mononen I. Beta-aspartylpeptides as substrates of l-asparaginases from Escherichia coli and Erwinia chrysanthemi. FEBS Lett. 528 (2002) 130-132
33. Khushoo A., Pal Y., Singh B.N., and Mukherjee K.J. Extracellular expression and single step purification of recombinant Escherichia coli l-asparaginase II. Protein Expr. Purif. 38 (2004) 29-36
34. Kotzia G.A., and Labrou N.E. S-(2,3-Dichlorotriazinyl)glutathione. A new affinity label for probing the structure and function of glutathione transferases. Eur. J. Biochem. 271 (2004) 3503-3511
35. Kotzia G.A., and Labrou N.E. Cloning, expression and characterisation of Erwinia carotovora l-asparaginase. J. Biotechnol. 119 (2005) 309-323
36. Kozak M., Borek D., Janowski R., and Jaskolski M. Crystallization and preliminary crystallographic studies of five crystal forms of Escherichia coli l-asparaginase II (Asp90Glu mutant). Acta Crystallogr. D: Biol. Crystallogr. 58 (2002) 130-132
37. Krasotkina J., Borisova A.A., Gervaziev Y.V., and Sokolov N.N. One-step purification and kinetic properties of the recombinant l-asparaginase from Erwinia carotovora. Biotechnol. Appl. Biochem. 39 (2004) 215-221
38. Kravtzoff R., Colombat P.H., Desbois I., Linassier C., Muh J.P., Philip T., Blay J.Y., Gardenbas M., Poumier-Gaschard P., Lamagnere J.P., Chassaigne M., and Ropars C. Tolerance evaluation of l-asparaginase loaded in red blood cells. Eur. J. Clin. Pharmacol. 51 (1996) 221-225
39. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
40. Leatherbarrow R.J. GraFit, Version 3 (1998), Erythacus Software, Ltd., Staines, United Kingdom
41. Luthy R., Bowie J.U., and Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature 356 (1992) 83-85
42. Moola Z.B., Scawen M.D., Atkinson T., and Nicholls D.J. Erwinia chrysanthemi l-asparaginase: epitope mapping and production of antigenically modified enzymes. Biochem J. 302 (1994) 921-927
43. Muller H.J., Beier R., Loning L., Blutters-Sawatzki R., Dorffel W., Maass E., Muller-Weihrich S., Scheel-Walter H.G., Scherer F., Stahnke K., Schrappe M., Horn A., Lumkemann K., and Boos J. Pharmacokinetics of native Escherichia coli asparaginase (Asparaginase medac) and hypersensitivity reactions in ALL-BFM 95 reinduction treatment. Br. J. Haematol. 114 (2001) 794-799
44. Neerunjun E.D., and Gregoriadis G. Tumour regression with liposome-entrapped asparaginase: some immunological advantages. Biochem. Soc. Trans. 4 (1976) 133-134
45. Peng G., Fritzsch G., Zickermann V., Schagger H., Mentele R., Lottspeich F., Bostina M., Radermacher M., Huber R., Stetter K.O., and Michel H. Isolation, characterization and electron microscopic single particle analysis of the NADH:ubiquinone oxidoreductase (complex I) from the hyperthermophilic eubacterium Aquifex aeolicus. Biochemistry 42 (2003) 3032-3039
46. Perlman D., and Halvorson H.O. A putative signal peptidase recognition site and sequence in eukaryotic and prokaryotic signal peptides. J. Mol. Biol. 167 (1983) 391-409
47. Poznansky M.J., Shandling M., Salkie M.A., Elliott J.F., and Lau E. Advantages in the use of l-asparaginase-albumin polymer as an antitumor agent. Cancer Res. 42 (1982) 1020-1025
48. Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
49. Sambrook J., Fritsch E.F., and Maniatis T. Molecular Cloning: A Laboratory Manual vol. 1-3 (1989), Cold Spring Harbor Laboratory Press, New York
50. Sheng S., Kraft J.J., and Schuster S.M. A specific quantitative colorimetric assay for l-asparagine. Anal. Biochem. 211 (1993) 242-249
51. Sippl M.J. Recognition of errors in three-dimensional structures of proteins. Proteins 17 (1993) 355-362
52. Stecher A.L., de Deus P.M., Polikarpov I., and Abrahao-Neto J. Stability of l-asparaginase: an enzyme used in leukemia treatment. Pharm. Acta Helv. 74 (1999) 1-9
53. Sturtevant J.M. Biochemical applications of differential scanning calorimetry. Annu. Rev. Phys. Chem. 38 (1987) 463-488
54. Swain A.L., Jaskolski M., Housset D., Rao J.K., and Wlodawer A. Crystal structure of Escherichia coli l-asparaginase, an enzyme used in cancer therapy. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 1474-1478
55. 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. Nucleic Acids Res. 22 (1994) 4673-4680
56. Wileman T.E., Foster R.L., and Elliott P.N. Soluble asparaginase-dextran conjugates show increased circulatory persistence and lowered antigen reactivity. J. Pharm. Pharmacol. 38 (1986) 264-271
57. Wriston Jr. J.C., and Yellin T.O. l-Asparaginase: a review. Adv. Enzymol. Relat. Areas Mol. Biol. 39 (1973) 185-248
58. Wriston Jr. J.C. l-Asparaginase. Meth. Enzymol. 113 (1985) 608-618
59. Zhang J.F., Shi L.Y., and Wei D.Z. Chemical modification of l-asparaginase from Escherichia coli with a modified polyethyleneglycol under substrate protection conditions. Biotechnol. Lett. 26 (2004) 753-756