Disulfide bonds of phospholipase A2 from bee venom yield discrete contributions to its conformational stability

Biochimie

Volumn 93, Issue 2, 2011, Pages 195-201

  Welker, Sylvia ^a,b   Markert, Yvonne ^a,c   Köditz, Jens ^a,d   Mansfeld, Johanna ^a   Ulbrich Hofmann, Renate ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^c ROCHE DIAGNOSTICS GMBH   (Germany)

^d IDT Biologika GmbH   (Germany)

Author keywords

Bee venom; Disulfide bonds; Phospholipase A2; Stability; Thermolysin

Indexed keywords

ALANINE; CYSTEINE; DISULFIDE; GUANIDINE; PHOSPHOLIPASE A2;

ARTICLE; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; ESCHERICHIA COLI; PROTEIN DEGRADATION;

AMINO ACID SUBSTITUTION; ANIMALS; BEE VENOMS; CATTLE; DISULFIDES; GLYCOSYLATION; MODELS, MOLECULAR; MUTATION; PHOSPHOLIPASES A2; PROTEIN CONFORMATION; PROTEIN STABILITY;

APOIDEA; BOVINAE; ESCHERICHIA COLI;

EID: 78651332255     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.09.012     Document Type: Article

References (34)

1. S.F. Betz Disulfide bonds and the stability of globular proteins Protein Sci. 2 1993 1551 1558
2. B.S. Mamathambika, and J.C. Bardwell Disulfide-linked protein folding pathways Annu. Rev. Cell Dev. Biol. 24 2008 211 235
3. M. Ramazzotti, C. Parrini, M. Stefani, G. Manao, and D. Degl'Innocenti The intrachain disulfide bridge is responsible of the unusual stability properties of novel acylphosphatase from Escherichia coli FEBS Lett. 580 2006 6763 6768
4. K. Ogawa, T. Sonoyama, T. Takeda, S. Ichiki, S. Nakamura, Y. Kobayashi, S. Uchiyama, K. Nakasone, S.J. Takayama, H. Mita, Y. Yamamoto, and Y. Sambongi Roles of a short connecting disulfide bond in the stability and function of psychrophilic Shewanella violacea cytochrome c (5) Extremophiles 11 2007 797 807
5. C. Schulenburg, U. Weininger, P. Neumann, H. Meiselbach, M.T. Stubbs, H. Sticht, J. Balbach, R. Ulbrich-Hofmann, and U. Arnold Impact of the C-terminal disulfide bond on the folding and stability of onconase ChemBioChem 11 2010 978 986
6. C.N. Pace, G.R. Grimsley, J.A. Thomson, and B.J. Barnett Conformational stability and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds J. Biol. Chem. 263 1988 11820 11825
7. J.M. Thornton Disulphide bridges in globular proteins J. Mol. Biol. 151 1981 261 287
8. P. Pecher, and U. Arnold The effect of additional disulfide bonds on the stability and folding of ribonuclease A Biophys. Chem. 141 2009 21 28
9. M. Matsumura, W.J. Becktel, M. Levitt, and B.W. Matthews Stabilization of phage T4 lysozyme by engineered disulfide bonds Proc. Natl. Acad. Sci. U.S.A. 86 1989 6562 6566
10. W.J. Wedemeyer, E. Welker, M. Narayan, and H.A. Scheraga Disulfide bonds and protein folding Biochemistry 39 2000 4207 4216
11. P.N. Bryan Protein engineering of subtilisin Biochim. Biophys. Acta 1543 2000 203 222
12. J. Mansfeld, G. Vriend, B.W. Dijkstra, O.R. Veltman, B. Van den Burg, G. Venema, R. Ulbrich-Hofmann, and V.G. Eijsink Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond J. Biol. Chem. 272 1997 11152 11156
13. J.E. Villafranca, E.E. Howell, S.J. Oatley, N.H. Xuong, and J. Kraut An engineered disulfide bond in dihydrofolate reductase Biochemistry 26 1987 2182 2189
14. 2 structure/function, mechanism, and signaling J. Lipid Res. 50 Suppl. 2009 S237 S242
15. 2 superfamily and its group numbering system Biochim. Biophys. Acta 1761 2006 1246 1259
16. 2: perspectives on biotechnological applications Biotechnol. Lett. 2009
17. 2 engineering. The roles of disulfide bonds in structure, conformational stability, and catalytic function Biochemistry 34 1995 15307 15314
18. 2: a novel concept in evaluating the contribution of the 'native-framework' of disulphides to the global conformational stability of proteins Biochem. J. 377 2004 685 692
19. 2 probed by the variants H48Q, H48N and H48K Protein Eng. 12 1999 497 503
20. 2: insight into the role of disulfide bonding patterns Biochemistry 44 2005 3369 3379
21. 2 variants with industrial impact Biotechnol. Bioeng. 98 2007 48 59
22. U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
23. 2 modified by manoalogue Biochemistry 30 1991 9559 9569
24. 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
25. J. Clarke, and A.R. Fersht Engineered disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation Biochemistry 32 1993 4322 4329
26. C.N. Pace, B.A. Shirley, and J.A. Thomson Measuring the conformational stability of a protein T.E. Creighton, Protein Structure - a Practical Approach 1989 IRL Press Oxford 311 330
27. C.N. Pace, E.J. Hebert, K.L. Shaw, D. Schell, V. Both, D. Krajcikova, J. Sevcik, K.S. Wilson, Z. Dauter, R.W. Hartley, and G.R. Grimsley Conformational stability and thermodynamics of folding of ribonucleases Sa, Sa2 and Sa3 J. Mol. Biol. 279 1998 271 286
28. C.C. Lester, X. Xu, J.H. Laity, S. Shimotakahara, and H.A. Scheraga Regeneration studies of an analog of ribonuclease A missing disulfide bonds 65-72 and 40-95 Biochemistry 36 1997 13068 13076
29. 2: the role of histidine-34, aspartate-64 and tyrosine-87 Biochemistry 35 1996 4591 4601
30. D.C. Poland, and H.A. Scheraga Comparison of theories of the helix-coil transition in polypeptides J. Chem. Phys. 43 1965 2071 2074
31. H. Hofmann, U. Weininger, C. Low, R.P. Golbik, J. Balbach, and R. Ulbrich-Hofmann Fast amide proton exchange reveals close relation between native-state dynamics and unfolding kinetics J. Am. Chem. Soc. 131 2009 140 146
32. L.M. Curto, J.J. Caramelo, G.R. Franchini, and J.M. Delfino Delta98Delta, a minimalist model of antiparallel beta-sheet proteins based on intestinal fatty acid binding protein Protein Sci. 18 2009 735 746
33. F. Gabel, P. Masson, M.T. Froment, B.P. Doctor, A. Saxena, I. Silman, G. Zaccai, and M. Weik Direct correlation between molecular dynamics and enzymatic stability: a comparative neutron scattering study of native human butyrylcholinesterase and its "aged" soman conjugate Biophys. J. 96 2009 1489 1494
34. 2 Adv. Protein Chem. 45 1994 53 88