Part:BBa_K4382002

Dye decolourising peroxidase (DyP1B)

Usage

Dyp1B enzyme belongs to a family of dyp-type peroxidase enzymes. DyP peroxidases comprise a novel superfamily of heme-containing peroxidases.They display both oxidative activity and hydrolytic activity and these enzymes are able to oxidize a variety of organic compounds of which some are poorly converted by established peroxidases, including dyes, β-carotene, and aromatic sulfides.They also show various cellular distributions, functioning not only inside cells but also outside of cells. Some are also cargo proteins of encapsulin.Microbial DyP peroxidases play a crucial role in oxidation of Mn(II) and lignin model compounds(Kraft lignin). In the context of our project, DyP1B will convert lignin to benzylic ketone which can be further converted to vanillin using BsDyP(BBa_K1336003) enzyme.

Biology

DyP1B is an oxidoreductase that uses hydrogen peroxide as an electron acceptor to catalyze the oxidation of substrate molecules.It contains heme as a cofactor which non covalently binds to the GXXDG motif in its primary sequence, which is the heme-binding region. The distal face of the heme interacts with three conserved residues; an aspartic acid , an arginine and a phenylalanine . The proximal histidine is the fifth ligand to the heme iron and a conserved aspartate is part of the GXXDG motif.The aspartate of the GXXDG motif swings into a proper position that is optimal for interaction with H2O2, thereby changing the conformation to what is known as the compound 1 form. This conserved Aspartate, which is distal to the H2O2 acts as a proton shuttle.The conversion of DyP1B into compound 1 leads to change in oxidation of iron attached to heme from +3 to +4.As a result this compound 1 can now oxidize lignocellulosic material.

References

1)Rahmanpour, R., & Bugg, T. D. H. (2015). Characterisation of DYP-type peroxidases from pseudomonas fluorescens PF-5: Oxidation of mn(ii) and polymeric lignin by DYP1B. Archives of Biochemistry and Biophysics, 574, 93–98. https://doi.org/10.1016/j.abb.2014.12.022

2)Sugano, Y., & Yoshida, T. (2021). DYP-type peroxidases: Recent advances and perspectives. International Journal of Molecular Sciences, 22(11), 5556. https://doi.org/10.3390/ijms22115556

3)Colpa, D. I., Fraaije, M. W., & van Bloois, E. (2014). DYP-type peroxidases: A promising and versatile class of enzymes. Journal of Industrial Microbiology and Biotechnology, 41(1), 1–7. https://doi.org/10.1007/s10295-013-1371-6

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal AgeI site found at 296
  
• 1000
  COMPATIBLE WITH RFC[1000]