The role of disulfide bonds in the conformational stability and catalytic activity of phytase

Biochemistry and Cell Biology

Volumn 82, Issue 2, 2004, Pages 329-334

  Wang, Xiao Yun ^a   Meng, Fan Guo ^b   Zhou, Hai Meng ^b  

^a SHANDONG AGRICULTURAL UNIVERSITY   (China)

^b TSINGHUA UNIVERSITY   (China)

Author keywords

Disulfide bond; Inactivation; Phytase; Urea denaturation

Indexed keywords

CATALYST ACTIVITY; CHEMICAL BONDS; CONFORMATIONS; ENZYMES; FLUORESCENCE;

CIRCULAR DICHROISM (CD); CONFORMATIONAL STABILITY; DISULFIDE BONDS;

BIOCHEMISTRY;

DITHIOTHREITOL; PHYTASE;

ANALYTIC METHOD; ARTICLE; CATALYSIS; CHEMICAL REACTION; CIRCULAR DICHROISM; DENATURATION; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE; KINETICS; PROTEIN FOLDING;

6-PHYTASE; CATALYSIS; CIRCULAR DICHROISM; DISULFIDES; DITHIOTHREITOL; PROTEIN CONFORMATION; PROTEIN DENATURATION; UREA;

ASPERGILLUS; ASPERGILLUS NIGER;

EID: 2542483890     PISSN: 08298211     EISSN: None     Source Type: Journal    
DOI: 10.1139/o03-082     Document Type: Article

References (29)

1. Abkevich, V.I., and Shakhnovich, E.I. 2000. What can disulfide bonds tell us about protein energetics, function and folding: simulations and bioinformatics analysis. J. Mol. Biol. 300: 975-985.
2. Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
3. Branza-Nichita, N., Lazar, C., Durantel, D., Dwek, R.A., and Zitzmannb, N. 2002. Role of disulfide bond formation in the folding and assembly of the envelope glycoproteins of a pestivirus. Biochem. Biophys. Res. Commun. 296: 470-476.
4. Chen, Q.X., Zhang, W., Zheng, W.Z., Zhang, Z., Yan, S.X., Zhang, T., and Zhou, H.M. 1996. Comparison of inactivation and unfolding of green crab (Scylla serrata) alkaline phosphatase during denaturation by guanidinium chloride. J. Protein Chem. 15: 359-365.
5. Chen, S.L., Chen, Q.X., Yang, H.P., Qiu, W.J., Wang, L.T., and Zhou, H.M. 1997. Unfolding and inactivation of Penneus penicillatus acid phosphatase during denaturation by guanidium chloride. Biochem. Mol. Biol. Int. 42: 517-525.
6. Clarke, J., Henrick, K., and Fersht, A.R. 1995a. Disulfide mutants of barnase I: changes in stability and structure assessed by biophysical methods and X-ray crystallography. J. Mol. Biol. 253: 493-504.
7. Clarke, J., Hounslow, A.M., and Fersht, A.R. 1995b. Disulfide mutants of barnase II: changes in structure and local stability identified by hydrogen exchange. J. Mol. Biol. 253: 505-513.
8. Dvorakava, J., Volfova, O., and Kopecky, J. 1997. Characterization of phytase produced by Aspergillus niger. Folia Microbiol. 42: 349-352.
9. Flinn, J.P., Pallaghy, P.K., Lew, M.J., Murphy, R., Angus, J.A., and Norton, R.S. 1999. Role of disulfide bridges in the folding, structure and biological activity of g-conotoxin GVIA. Biochim. Biophys. Acta, 1434: 177-190.
10. Gashikar, A.G., and Rao, N.M. 1996. Role of the intersubunit disulfide bond in the unfolding pathway of dimeric red kidney bean purple acid phosphtase. Biochim. Biophys. Acta, 1296: 76-84.
11. Kostrewa, D., Gruninger-Leitch, Darcy, F.A., Broger, C., Mitchell, D., and van Loon, A.P. 1997. Crystal structure of phytase from Aspergillus ficuum at 2.5 A resolution. Nat. Struct. Biol. 4: 185-190.
12. Lelanda, P.A., Staniszewskia, K.E., Kima, B.M., and Rainesa, R.T. 2000. A synapomorphic disulfide bond is critical for the conformationalstability and cytotoxicity of an amphibian ribonuclease. FEBS Letters, 477: 203-207.
13. Lundblad, R.L. 1995. Techniques in protein modification. CRC Press Inc., Boca Raton, Fla. pp. 91-103.
14. Mullaney, E.J., Daly, C.B., Kim, T., Porres, J.M., Lei, X.G., Sethumadhavan, K., and Ullah, A.H.J. 2002. Site-directed mutagenesis of Aspergillus niger NRRL 3135 phytase at residue 300 to enhance catalysis at pH 4.0. Biochem. Biophys. Res. Commun. 297: 1016-1020.
15. Pandy, A., Szakacs, G., Soccol, C.R., Rodriguez-Leon, J.A., and Soccol, V.T. 2001. Production, purification and properties of microbial phytase. Bioresour. Technol. 77: 203-214.
16. Rodriguez, E., Wood, Z.A., Karplus, P.A., and Lei, X.G. 2000. Site-directed mutagenesis improves catalytic efficiency and thermostability of Escherichia coli pH 2.5 acid phosphatase/ phytase expressed in Pichia pastoris. Arch. Biochem. Biophys. 382: 105-112.
17. Singh, R.R., and Rao, A.G.A. 2002. Reductive unfolding and oxidative refolding of a Bowman-Birk inhibitor from horsegram seeds (Dolichos biflorus): evidence for 'hyperreactive' disulfide bonds and rate-limiting nature of disulfide isomerization in folding. Biochim. Biophys. Acta, 1597: 280-291.
18. Ullah, A.H.J. 1988. Aspergillus ficuum phytase: partial primary structure, substrate selectivity, and kinetic characterization. Prep. Biochemistry, 18: 459-471.
19. Ullah, A.H.J., and Dischinger, Jr. H.C. 1993. Aspergillus-ficuum phytase complete primary structure elucidation by chemical sequencing. Biochem. Biophys. Res. Commun. 192: 747-753.
20. Ullah, A.H.J., and Mullaney, E.J. 1996. Disulfide bonds are necessary for structure and activity in Aspergillus ficuum phytase. Biochem. Biophys. Res. Commun. 227: 311-317.
21. Ullah, A.H., Sethumdhavan, K., Lei, X.G., and Mullaney, E.J. 2000. Biochemical characterization of cloned Aspergillus fumigatus phytase (phy A). Biochem. Biophys. Res. Commun. 275: 279-285.
22. Varallyay, E., Lengyel, Z., Gra, L., and Szilagyi, L. 1997. The role of disulfide bond C191-C220 in trypsin and chymotrypsin. Biophys. Res. Commun. 230: 592-596.
23. Wang, H.R., Zhang, T., and Zhou, H.M. 1995. Comparison of inactivation and conformational changes of aminoacylase during guanidinium chloride denaturation. Biochim. Biophys. Acta, 1248: 97-106.
24. Wang, G.F., Cao, Z.F., Zhou, H.M., and Zhao, Y.F. 2000. Comparison of inactivation and unfolding of methanol dehydrogenase during denaturation in guanidine hydrochloride and urea. Int. J. Biochem. Cell Biol. 32: 873-878.
25. Wodzinski, R.J., and Ullah, A.H. 1996. Phytase. Adv. Appl. Microbiol. 42: 263-302.
26. Woirn, A., and Pluickthun, A. 1998. An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly. FEBS Lett. 427: 357-361.
27. Wu, B.N., Park, Y.D., Tian, W.X., and Zhou, H.M. 2001. Unfolding and inactivation of fatty acid synthase from chicken liver during urea denaturation. Biochim. Biophys. Acta, 1549: 112-121.
28. Yao, B., Zhang, C.Y., Wang, J.H., and Fan, Y.L. 1998a. Recombinant Pichia pastoris over-expressing bioactive phytase. Sci. China (C), 41: 330-336.
29. Yao, B., Zhang, C.Y., Wang, J.H., Fan, Y.L., Shi, X.Y., Wang, Y.R., and Li, S.M. 1998b. Isolation of Aspergillus niger 963 with phytase activity and cloning its phytase gene phy A2. J. Agri. Biotech. (China), 6: 1-6.