Improvement of stability and enzymatic activity by site-directed mutagenesis of E. coli asparaginase II

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1844, Issue 7, 2014, Pages 1219-1230

  Verma, Shikha ^b   Mehta, Ranjit Kumar ^a   Maiti, Prasanta ^c   Röhm, Klaus Heinrich ^b   Sonawane, Avinash ^a  

^a KIIT UNIVERSITY   (India)

^b PHILIPPS UNIVERSITY MARBURG   (Germany)

^c Imgenex India Pvt Ltd   (India)

Author keywords

Activity; Asparaginase; E. coli; Mutagenesis; Stability

Indexed keywords

AMINO ACID; ASPARAGINASE; DIMER; ENZYME VARIANT; ESCHERICHIA COLI ASPARAGINASE II; ESCHERICHIA COLI PROTEIN; MONOMER; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CHEMICAL INTERACTION; CIRCULAR DICHROISM; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DENATURATION; ENZYME MODIFICATION; ENZYME STABILITY; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; WILD TYPE;

ACTIVITY; ASPARAGINASE; E. COLI; MUTAGENESIS; STABILITY;

ASPARAGINASE; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; ENZYME STABILITY; ESCHERICHIA COLI; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION;

EID: 84899673356     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2014.03.013     Document Type: Article

References (43)

1. G.J. Palm, J. Lubkowski, C. Derst, S. Schleper, K.H. Röhm, and A. Wlodawer A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant FEBS Lett. 390 1996 211 216 (Pubitemid 26281204)
2. A.L. Swain, M. Jaskolski, D. Housset, J.K. Rao, and A. Wlodawer Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy Proc. Natl. Acad. Sci. U. S. A. 90 1993 1474 1478 (Pubitemid 23058195)
3. J. Lubkowski, A. Wlodawer, H.L. Ammon, T.D. Copeland, and A.L. Swain Structural characterization of Pseudomonas 7A glutaminase-asparaginase Biochemistry 33 1994 10257 10265 (Pubitemid 24281790)
4. K. Aghaiypour, A. Wlodawer, and J. Lubkowski Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase Biochemistry 40 2001 5655 5664 (Pubitemid 32440869)
5. J. Lubkowski, G.J. Palm, G.L. Gilliland, C. Derst, K.H. Röhm, and A. Wlodawer Crystal structure and amino acid sequence of Wolinella succinogenes L-asparaginase Eur. J. Biochem. 241 1996 201 207 (Pubitemid 26342990)
6. N.E. Labrou, A.C. Papageorgiou, and V.I. Avramis Structure-function relationships and clinical applications of L-asparaginases Curr. Med. Chem. 17 2010 2183 2195
7. R. Pieters, S.P. Hunger, J. Boos, C. Rizzari, L. Silverman, A. Baruchel, N. Goekbuget, M. Schrappe, and C.H. Pui L-asparaginase treatment in acute lymphoblastic leukemia: a focus on Erwinia asparaginase Cancer 117 2011 238 249
8. U.K. Narta, S.S. Kanwar, and W. Azmi Pharmacological and clinical evaluation of L-asparaginase in the treatment of leukemia Crit. Rev. Oncol. Hematol. 61 2007 208 221 (Pubitemid 46329425)
9. H.J. Müller, and J. Boos Use of L-asparaginase in childhood ALL Crit. Rev. Oncol. Hematol. 28 1998 97 113 (Pubitemid 28390409)
10. B.M. Fine, G.J. Kaspers, M. Ho, A.H. Loonen, and L.M. Boxer A genome-wide view of the in vitro response to l-asparaginase in acute lymphoblastic leukemia Cancer Res. 65 2005 291 299 (Pubitemid 40070821)
11. Y. Iiboshi, P.J. Papst, S.P. Hunger, and N. Terada L-Asparaginase inhibits the rapamycin-targeted signaling pathway Biochem. Biophys. Res. Commun. 260 1999 534 539 (Pubitemid 29352097)
12. H. Suto, H. Yasuda, Y. Isobe, M. Sasaki, H. Imai, M. Tsutsui, K. Oshimi, N. Komatsu, and K. Sugimoto Suppression of eIF4E expression by L-asparaginase Acta Haematol. (Basel) 123 2010 215 219
13. M.H. Woo, L.J. Hak, M.C. Storm, W.E. Evans, J.T. Sandlund, G.K. Rivera, B. Wang, C.H. Pui, and M.V. Relling Anti-asparaginase antibodies following E. coli asparaginase therapy in pediatric acute lymphoblastic leukemia Leukemia 12 1998 1527 1533 (Pubitemid 28470435)
14. N. Patel, S. Krishnan, M.N. Offman, M. Krol, C.X. Moss, C. Leighton, F.W. van Delft, M. Holland, J. Liu, S. Alexander, C. Dempsey, H. Ariffin, M. Essink, T.O. Eden, C. Watts, P.A. Bates, and V. Saha A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug L-asparaginase J. Clin. Invest. 119 2009 1964 1973
15. C. Derst, J. Henseling, and K.H. Röhm 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. G.A. Kotzia, and N.E. Labrou Engineering thermal stability of L-asparaginase by in vitro directed evolution FEBS J. 276 2009 1750 1761
17. G.A. Kotzia, K. Lappa, and N.E. Labrou Tailoring structure-function properties of L-asparaginase: engineering resistance to trypsin cleavage Biochem. J. 404 2007 337 343 (Pubitemid 46849605)
18. R.K. Mehta, S. Verma, R. Pati, M. Sengupta, B. Khatua, R.K. Jena, S. Sethy, S.K. Kar, C. Mandal, K.H. Röhm, and A. Sonawane Mutations in subunit interface and B-cell epitopes improve antileukemic activities of Escherichia coli asparaginase-II: evaluation of immunogenicity in mice J. Biol. Chem. 289 2014 3555 3570
19. C. Derst, J. Henseling, and K.H. Röhm Probing the role of threonine and serine residues of E. coli asparaginase II by site-specific mutagenesis Protein Eng. 5 1992 785 789 (Pubitemid 23036549)
20. C. Derst, A. Wehner, V. Spech, and K.H. Röhm States and functions of tyrosine residues in Escherichia coli asparaginase II Eur. J. Biochem. 224 1994 533 540 (Pubitemid 24282837)
21. E. Harms, A. Wehner, M.P. Jennings, K.J. Pugh, I.R. Beacham, and K.H. Röhm Construction of expression systems for Escherichia coli asparaginase II and two-step purification of the recombinant enzyme from periplasmic extracts Protein Expr. Purif. 2 1991 144 150
22. H.P. Aung, M. Bocola, S. Schleper, and K.H. Röhm Dynamics of a mobile loop at the active site of Escherichia coli asparaginase Biochim. Biophys. Acta 1481 2000 349 359
23. A. Wehner, E. Harms, M.P. Jennings, I.R. Beacham, C. Derst, P. Bast, and K.H. Röhm Site-specific mutagenesis of Escherichia coli asparaginase II. None of the three histidine residues is required for catalysis Eur. J. Biochem. 208 1992 475 480
24. P.K. Smith, R.I. Krohn, G.T. Hermanson, A.K. Mallia, F.H. Gartner, M.D. Provenzano, E.K. Fujimoto, N.M. Goeke, B.J. Olson, and D.C. Klenk Measurement of protein using bicinchoninic acid Anal. Biochem. 150 1985 76 85 (Pubitemid 16258399)
25. C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280 (Pubitemid 16002205)
26. Y. Nozaki The preparation of guanidine hydrochloride Methods Enzymol. 26 1972 43 50
27. L.M. Siegel, and K.J. Monty Determination of molecular weights and frictional ratios of proteins in impure systems by use of gel filtration and density gradient centrifugation. Application to crude preparations of sulfite and hydroxylamine reductases Biochim. Biophys. Acta 112 1966 346 362
28. M.A. Bothwell, G.J. Howlett, and H.K. Schachman A sedimentation equilibrium method for determining molecular weights of proteins with a tabletop high speed air turbine centrifuge J. Biol. Chem. 253 1978 2073 2077 (Pubitemid 8328184)
29. S. Benjwal, S. Verma, K.H. Röhm, and O. Gursky Monitoring protein aggregation during thermal unfolding in circular dichroism experiments Protein Sci. 15 2006 635 639
30. M.R. Eftink The use of fluorescence methods to monitor unfolding transitions in proteins Biochemistry 63 1998 276 284 (Pubitemid 128588265)
31. J. Backmann, G. Schäfer, L. Wyns, and H. Bönisch Thermodynamics and kinetics of unfolding of the thermostable trimeric adenylate kinase from the archaeon Sulfolobus acidocaldarius J. Mol. Biol. 284 1998 817 833 (Pubitemid 28550025)
32. M.M. Santoro, and D.W. Bolen Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants Biochemistry 27 1988 8063 8068
33. J. Backmann, and G. Schäfer Thermodynamic analysis of hyperthermostable oligomeric proteins Methods Enzymol. 334 2001 328 342 (Pubitemid 32507285)
34. D.K. Wilkins, S.B. Grimshaw, V. Receveur, C.M. Dobson, J.A. Jones, and L.J. Smith Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques Biochemistry 38 1999 16424 16431
35. C. Duy, and J. Fitter How aggregation and conformational scrambling of unfolded states govern fluorescence emission spectra Biophys. J. 90 2006 3704 3711
36. C.R. Johnson, P.E. Morin, C.H. Arrowsmith, and E. Freire Thermodynamic analysis of the structural stability of the tetrameric oligomerization domain of p53 tumor suppressor Biochemistry 34 1995 5309 5316
37. A. Cooper Thermodynamics of protein folding and stability G. Allen, Protein: a Comprehensive Treatise Vol. 2 1999 JAI Press Stamford 217 270
38. A.I. Cooper, and C.M. Johnson Differential scanning calorimetry Methods Mol. Biol. 22 1994 125 136
39. M.G. Mateu, M.M. Sanchez Del Pino, and A.R. Fersht Mechanism of folding and assembly of a small tetrameric protein domain from tumor suppressor p53 Nat. Struct. Biol. 6 1999 191 198 (Pubitemid 29069783)
40. C.N. Pace, S. Trevino, E. Prabhakaran, and J.M. Scholtz Protein structure, stability and solubility in water and other solvents Philos. Trans. R. Soc. B 359 2004 1225 1234
41. M.G. Mateu, and A.R. Fersht Nine hydrophobic side chains are key determinants of the thermodynamic stability and oligomerization status of tumour suppressor p53 tetramerization domain EMBO J. 17 1998 2748 2758
42. Y.C. Park, and H. Bedouelle Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions J. Biol. Chem. 273 1998 18052 18059 (Pubitemid 28334720)
43. E. Krissinel, and K. Henrick Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372 2007 774 797 (Pubitemid 47321791)