Applied Biochemistry and Biotechnology

, Volume 165, Issue 2, pp 397–405 | Cite as

Insights to Sequence Information of Polyphenol Oxidase Enzyme from Different Source Organisms

  • Neha Malviya
  • Mugdha Srivastava
  • Sanjeev Kumar Diwakar
  • Sarad Kumar Mishra


Polyphenol oxidases (PPOs) are widely distributed enzymes among animals, plants, bacteria, and fungi. PPOs often have significant role in many biologically essential functions including pigmentation, sclerotization, primary immune response, and host defense mechanisms. In the present study, forty-seven full-length amino acid sequences of PPO from bacteria, fungi, and plants were collected and subjected to multiple sequence alignment (MSA), domain identification, and phylogenetic tree construction. MSA revealed that six histidine, two phenylalanine, two arginine, and two aspartic acid residues were highly conserved in all the analyzed species, while a single cysteine residue was conserved in all the plant and fungal PPOs. Two major sequence clusters were constructed by phylogenetic analysis. One cluster was of the plant origin, whereas the other one was of the fungal and bacterial origin. Motif GGGMMGDVPTANDPIFWLHHCNVDRLWAVWQ was found in all the species of bacterial and fungus sources. In addition, seven new motifs which were unique for their group were also identified.


Polyphenol oxidase Sequence analysis Phylogenetic analysis Conserved regions Motifs 

Supplementary material

12010_2011_9259_MOESM1_ESM.doc (41 kb)
Supplement A (DOC 41 kb)
12010_2011_9259_MOESM2_ESM.doc (69 kb)
Supplement B (DOC 69 kb)
12010_2011_9259_MOESM3_ESM.doc (106 kb)
Supplement C (DOC 106 kb)


  1. 1.
    Mayer, A. M. (2006). Phytochemistry, 67, 2318–2331.CrossRefGoogle Scholar
  2. 2.
    Mason, H. (1955). Adv Enzymol, 16, 105–184.Google Scholar
  3. 3.
    Umit, U. M. (2007). Food Chem, 100, 909–913.CrossRefGoogle Scholar
  4. 4.
    Wichers, H. J., Recourt, K., Hendriks, M., Ebbelaar, C. F. M., Biancone, G., & Hoeberichts, F. A. (2003). Appl Microbiol Biotechnol, 61, 336–341.Google Scholar
  5. 5.
    Bailey, T. L., & Elkan, C. (1995). Mach Learn, 21(1–2), 51–80.Google Scholar
  6. 6.
    Bailey, T. L., & Gribskov, M. (1998). Bioinformatics, 14(1), 48–54.CrossRefGoogle Scholar
  7. 7.
    Tamura, K., Dudley, J., Nei, M., & Kumar, S. (2007). Mol Biol Evol, 24, 1596–1599.CrossRefGoogle Scholar
  8. 8.
    Marusek, C. M., Trobaugh, N. M., Flurkey, W. H., & Inlow, J. K. (2006). J Inorg Biochem, 100, 108–123.CrossRefGoogle Scholar
  9. 9.
    Garcia-Borron, J. C., & Solano, F. (2002). Pigment Cell Res, 15, 162–173.CrossRefGoogle Scholar
  10. 10.
    van Gelder, C. W. G., Flurkey, W. H., & Wichers, H. J. (1997). Phytochemistry, 45, 1309–1323.CrossRefGoogle Scholar
  11. 11.
    Gerdemann, C., Eicken, C., & Krebs, B. (2002). Acc Chem Res, 35, 183–191.CrossRefGoogle Scholar
  12. 12.
    Klabunde, T., Eicken, C., Sacchettini, J. C., & Krebs, B. (1998). Nat Struct Biol, 5, 1084–1090.CrossRefGoogle Scholar
  13. 13.
    Eickena, C., Krebs, B., & Sacchettini, J. C. (1999). Curr Opin Struct Biol, 9, 677–683.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Neha Malviya
    • 1
  • Mugdha Srivastava
    • 2
  • Sanjeev Kumar Diwakar
    • 1
  • Sarad Kumar Mishra
    • 1
  1. 1.Department of BiotechnologyDeen Dayal Upadhyay Gorakhpur UniversityGorakhpurIndia
  2. 2.Department of Botany, Atarra P.G. CollegeBundelkhand UniversityBundelkhandIndia

Personalised recommendations