Skip to main content
Log in

An in-silico insight into the characteristics of β-propeller phytase

  • Original Articles
  • Published:
Interdisciplinary Sciences: Computational Life Sciences Aims and scope Submit manuscript

Abstract

Phytase is an enzyme that is found extensively in the plant kingdom and in some species of bacteria and fungi. This paper identifies and analyses the available full length sequences of β-propeller phytases (BPP). BPP was chosen due to its potential applicability in the field of aquaculture. The sequences were obtained from the Uniprot database and subject to various online bioinformatics tools to elucidate the physio-chemical characteristics, secondary structures and active site compositions of BPP. Protparam and SOPMA were used to analyse the physiochemical and secondary structure characteristics, while the Expasy online modelling tool and CASTp were used to model the 3-D structure and identify the active sites of the BPP sequences. The amino acid compositions of the four sequences were compared and composed in a graphical format to identify similarities and highlight the potentially important amino acids that form the active site of BPP. This study aims to analyse BPP and contribute to the clarification of the molecular mechanism involved in the enzyme activity of BPP and contribute in part to the possibility of constructing a synthetic version of BPP.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Bjellqvist, B., Hughes, G.J., Pasquali, C., Paquet, N., Ravier, F., Sanchez, J.C., Frutiger, S., Hochstrasser, D. 1993.The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 14, 1023–1031.

    Article  CAS  PubMed  Google Scholar 

  2. Bohn, L., Meyer, A.S., Rasmussen, S.K. 2008. Phytate: impact on environment and human nutrition. A challenge for molecular breeding. Journal of Zhejiang University SCIENCE B 9, 165–191.

    Article  CAS  Google Scholar 

  3. Campbell, G.L., Bedford, M.R. 1992. Enzyme applications for monogastric feeds: A review. Canadian Journal of Animal Science 72, 449–466.

    Article  CAS  Google Scholar 

  4. Cheng, C., Lim, B.L. 2006. Beta-propeller phytases in the aquatic environment. Archives of Microbiology. 185, 1–13.

    Article  CAS  PubMed  Google Scholar 

  5. Cheryan, M. 1980. Phytic acid interactions in food systems. Critical reviews in food science and nutrition 13, 297–335.

    Article  CAS  PubMed  Google Scholar 

  6. Fu, S., Sun, J., Qian, L., Li, Z. 2008. Bacillus phytases: present scenario and future perspectives. Applied Biochemistry and Biotechnology 151, 1–8.

    Article  CAS  PubMed  Google Scholar 

  7. Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M.R., Appel, R.D., Bairoch, A. 2005. Protein Identification and Analysis Tools on the ExPASy Server. In: John M. Walker (ed) The Proteomics Protocols Handbook. Humana press, pp 571–607.

    Chapter  Google Scholar 

  8. Guruprasad, K., Reddy, B.V., Pandit, M.W. 1990. Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein engineering 4, 155.

    Article  CAS  PubMed  Google Scholar 

  9. Ikai, A. 1980. Thermostability and aliphatic index of globular proteins. Journal of Biochemistry 88, 1895.

    CAS  PubMed  Google Scholar 

  10. Kyte, J., Doolittle, R.F. 1982. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology 157, 105–132.

    Article  CAS  PubMed  Google Scholar 

  11. Lehmann, M. 2004. Consensus phytases, European patent EP0897985.

    Google Scholar 

  12. Liang, J., Edelsbrunner, H., Woodward, C. 1998. Anatomy of protein pockets and cavities: measurement of binding site geometry and implications for ligand design. Protein science 7, 1884–1897.

    Article  CAS  PubMed Central  PubMed  Google Scholar 

  13. Mendoza, C. 2002. Effect of genetically modified low phytic acid plants on mineral absorption. International Journal of Food Science & Technology 37, 759–767.

    Article  CAS  Google Scholar 

  14. Mullaney, E.J., Ullah, A.H.J. 2003. The term phytase comprises several different classes of enzymes. Biochemical and biophysical research communications 312, 179–184.

    Article  CAS  PubMed  Google Scholar 

  15. Raboy, V. 2009. Approaches and challenges to engineering seed phytate and total phosphorus. Plant Science 177, 281–296.

    Article  CAS  Google Scholar 

  16. Richards, F.M. 1977. Areas, Volumes, Packing, and Protein Structure. Annual Review of Biophysics and Bioengineering 6, 151–176.

    Article  CAS  PubMed  Google Scholar 

  17. Selle, P.H., Ravindran, V. 2007. Microbial phytase in poultry nutrition. Animal Feed Science and Technology, 135, 1–41.

    Article  CAS  Google Scholar 

  18. Stephen, A., Dupe, I., Oluwole, A., Martin, N., Don, F. 2010. Characterizing Fecal and Manure Phosphorus from Pigs Fed Phytase Supplemented Diets. Journal of Agricultural Science 2, 3–12.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Smriti Gaur.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Mathew, A., Verma, A. & Gaur, S. An in-silico insight into the characteristics of β-propeller phytase. Interdiscip Sci Comput Life Sci 6, 133–139 (2014). https://doi.org/10.1007/s12539-013-0010-2

Download citation

  • Received:

  • Revised:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12539-013-0010-2

Key words

Navigation