Structural highlights
Function
[DYP_THEFY] Peroxidase that is able to convert a large number of compounds, but its physiological substrate is not known. Shows high reactivity towards anthraquinone dyes (e.g. Reactive Blue 19) and a modest activity towards standard peroxidase substrates (such as guaiacol and 2,6-dimethoxyphenol) and azo dyes (e.g. Reactive Blue 5). Is also able to oxidize aromatic sulfides enantioselectively, resulting in the corresponding (R)-sulfoxides, but with a poor efficiency. Does not display catalase activity.[1]
Publication Abstract from PubMed
A Dyp-type peroxidase enzyme from thermophilic cellulose degrader Thermobifida fusca (TfuDyP) was investigated for catalytic ability towards lignin oxidation. TfuDyP was characterised kinetically against a range of phenolic substrates, and a compound I reaction intermediate was observed via pre-steady state kinetic analysis at lambdamax 404 nm. TfuDyP showed reactivity towards Kraft lignin, and was found to oxidise a beta-aryl ether lignin model compound, forming an oxidised dimer. A crystal structure of TfuDyP was determined, to 1.8 A resolution, which was found to contain a diatomic oxygen ligand bound to the heme centre, positioned close to active site residues Asp-203 and Arg-315. The structure contains two channels providing access to the heme cofactor for organic substrates and hydrogen peroxide. Site-directed mutant D203A showed no activity towards phenolic substrates, but reduced activity towards ABTS, while mutant R315Q showed no activity towards phenolic substrates, nor ABTS.
Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds.,Rahmanpour R, Rea D, Jamshidi S, Fulop V, Bugg TD Arch Biochem Biophys. 2016 Mar 15;594:54-60. doi: 10.1016/j.abb.2016.02.019. Epub, 2016 Feb 18. PMID:26901432[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Bloois E, Torres Pazmino DE, Winter RT, Fraaije MW. A robust and extracellular heme-containing peroxidase from Thermobifida fusca as prototype of a bacterial peroxidase superfamily. Appl Microbiol Biotechnol. 2010 May;86(5):1419-30. doi:, 10.1007/s00253-009-2369-x. Epub 2009 Dec 5. PMID:19967355 doi:http://dx.doi.org/10.1007/s00253-009-2369-x
- ↑ Rahmanpour R, Rea D, Jamshidi S, Fulop V, Bugg TD. Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds. Arch Biochem Biophys. 2016 Mar 15;594:54-60. doi: 10.1016/j.abb.2016.02.019. Epub, 2016 Feb 18. PMID:26901432 doi:http://dx.doi.org/10.1016/j.abb.2016.02.019
