Relationship between Escherichia coli AppA phytase's thermostability and salt bridges

Journal of Bioscience and Bioengineering

Volumn 115, Issue 6, 2013, Pages 623-627

  Fei, Baojin ^a   Xu, Hui ^a   Zhang, Feiwei ^b   Li, Xinran ^a   Ma, Shuhan ^a   Cao, Yu ^a   Xie, Jie ^a   Qiao, Dairong ^a   Cao, Yi ^a  

^a SICHUAN UNIVERSITY   (China)

^b Chengdu Institute of Biological Products Co Ltd   (China)

Author keywords

Escherichia coli AppA phytase; Molecular dynamics simulation; Salt bridge; Site directed mutagenesis; Thermostability

Indexed keywords

MOLECULAR DYNAMICS SIMULATIONS; PHYTASES; SALT BRIDGES; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

MOLECULAR DYNAMICS; MOLECULAR MECHANICS;

ESCHERICHIA COLI;

APPA PHYTASE; BACTERIAL ENZYME; PHYTASE; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ARTICLE; CELL PH; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ASSAY; ESCHERICHIA COLI; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY; WILD TYPE;

6-PHYTASE; ACID PHOSPHATASE; ENZYME STABILITY; ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; HOT TEMPERATURE; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED;

ESCHERICHIA COLI;

EID: 84876990454     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2012.12.010     Document Type: Article

References (33)

1. Haefner S., Knietsch A., Scholten E., Braun J., Lohscheidt M., Zelder O. Biotechnological production and applications of phytases. Appl. Microbiol. Biotechnol. 2005, 68:588-597.
2. Selle P.H., Aaron J., Cowieson A.J., Ravindran V. Consequences of calcium interactions with phytate and phytase for poultry and pigs. Livestock Sci. 2009, 124:126-141.
3. Lei X.G., Stahl C.H. Biotechnological development of effective phytases for mineral nutrition and environmental protection. Appl. Microbiol. Biotechnol. 2001, 57:474-481.
4. Wyss M., Brugger R., Kronenberger A., Remy R., Fimbel R., Oesterhelt G., Lehmann M., van Loon A.P. Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties. Appl. Environ. Microbiol. 1999, 65:367-373.
5. Luo H., Huang H., Yang P., Wang Y., Yuan T., Wu N., Yao B., Fan Y. A novel phytase appA from Citrobacter amalonaticus CGMCC 1696: gene cloning and overexpression in Pichia pastoris. Curr. Microbiol. 2007, 55:185-192.
6. Szilágyi A., Závodszky P. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure 2000, 15:493-504.
7. Pack S.P., Yoo Y.J. Protein thermostability: structure-based difference of residual properties between thermophilic and mesophilic proteins. J. Mol. Catal. B: Enzym. 2003, 26:257-264.
8. Eijsink V.G., Bjørk A., Gåseidnes S., Sirevåg R., Synstad B., van den Burg B., Vriend G. Rational engineering of enzyme stability. J. Biotechnol. 2004, 113:105-120.
9. Kumar S., Tsai C.J., Nussinov R. Factors enhancing protein thermostability. Protein Eng. 2000, 13:179-191.
10. Querol E., Perez-Pons J.A., Mozo-Villarias A. Analysis of protein conformational characteristics related to thermostability. Protein Eng. 1996, 9:265-271.
11. Ragone R. Hydrogen-bonding classes in proteins and their contribution to the unfolding reaction. Protein Sci. 2001, 10:2075-2082.
12. Vieille C., Zeikus J.G. Thermozymes: identifying molecular determinants of protein structural and functional stability. Trends Biotechnol. 1996, 14:183-190.
13. Vieille C., Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 2001, 65:1-43.
14. Yip K.S., Stillman T.J., Britton K.L., Artymiuk P.J., Baker P.J., Sedelnikova S.E., Engel P.C., Pasquo A., Chiaraluce R., Consalvi V. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure 1995, 3:1147-1158.
15. Missimer J.H., Steinmetz M.O., Baron R., Winkler F.K., Kammerer R.A., Daura X., Van Gunsteren W.F. Configurational entropy elucidates the role of salt-bridge networks in protein thermostability. Protein Sci. 2007, 16:1349-1359.
16. Thomas A.S., Elcock A.H. Molecular simulations suggest protein salt bridges are uniquely suited to life at high temperatures. J. Am. Chem. Soc. 2004, 126:2208-2214.
17. Strop P., Mayo S.L. Contribution of surface salt bridges to protein stability. Biochemistry 2000, 39:1251-1255.
18. Dominy B.N., Minoux H., Brooks C.L. An electrostatic basis for the stability of thermophilic proteins. Proteins 2004, 57:128-141.
19. Chan C.H., Yu T.H., Wong K.B. Stabilizing salt-bridge enhances protein thermostability by reducing the heat capacity change of unfolding. PLoS One 2011, 6:e21624.
20. Ge M., Xia X.Y., Pan X.M. Salt bridges in the hyperthermophilic protein Ssh10b are resilient to temperature increases. J. Biol. Chem. 2008, 283:31690-31696.
21. Folch B., Rooman M., Dehouck Y. Thermostability of salt bridges versus hydrophobic interactions in proteins probed by statistical potentials. J. Chem. Inf. Model. 2008, 48:119-127.
22. Yi F., Yanrui D., Zhiguo C., Jun S., Wei F., Wenbo X. Study on the relationship between cyclodextrin glycosyltransferase thermostability and salt bridge formation by molecular dynamics simulation. Protein Pept. Lett. 2010, 17:1403-1411.
23. Eric R., Zachary A., Wood P., Andrew K., Xin G.L. Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/phytase expressed in Pichia pastoris. Arch. Biochem. Biophys. 2000, 382:105-112.
24. Kale L., Skeel R., Bhandarkar M., Brunner R., Gursoy A., Krawetz N., Phillips J., Shinozaki A., Varadarajan K., Schulten K. NAMD2: greater scalability for parallel molecular dynamics. J. Comput. Phys. 1999, 151:283-312.
25. Jorgensen W.L., Chandrasekhar J., Madura J.D., Impey R.W., Klein M.L. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 1983, 79:926-935.
26. Humphrey W., Dalke A., Schulten K. VMD: visual molecular dynamics. J. Mol. Graph. 1996, 14:33-38.
27. MacKerell A.D., Bashford D., Bellott M., Dunbrack R.L., Evanseck J.D., Field M.J., Fischer S., Gao J., Guo H., Ha S., other 19 authors All-atom empirical potential for molecular modeling and dynamics studies of proteins and nucleic acids. J. Phys. Chem. 1998, 102:3586-3616.
28. Darden T., York D., Pedersen L. Particle Mesh Ewald: an N log (N) method for Ewald sums in large systems. J. Chem. Phys. 1993, 98:10089-10092.
29. Ryckaert J.P., Ciccotti G., Berendsen H.J.C. Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 1977, 23:327-341.
30. Han Y.M., Lei X.G. Role of glycosylation in the functional expression of an Aspergillus niger phytase (phyA) in Pichia pastoris. Arch. Biochem. Biophys. 1999, 364:83-90.
31. Han Y.M., Wilson D.B., Lei X.G. Expression of an Aspergillus niger phytase gene (phyA) in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 1999, 65:1915-1918.
32. Zhu W., Qiao D., Huang M., Yang G., Xu H., Cao Y. Modifying thermostability of appA from Escherichia coli. Curr. Microbiol. 2010, 61:267-273.
33. Reetz M.T., Carballeira J.D., Vogel A. Iterative saturation mutagenesis on the basis of b factors as a strategy for increasing protein thermostability. Angew. Chem. Int. Ed. 2006, 45:7745-7751.