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| | ==Structure of Thermobifida fusca DyP-type Peroxidase and Activity towards Kraft Lignin and Lignin Model Compounds== | | ==Structure of Thermobifida fusca DyP-type Peroxidase and Activity towards Kraft Lignin and Lignin Model Compounds== |
| - | <StructureSection load='5fw4' size='340' side='right' caption='[[5fw4]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='5fw4' size='340' side='right'caption='[[5fw4]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fw4]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FW4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FW4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fw4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca_YX Thermobifida fusca YX]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FW4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FW4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dye_decolorizing_peroxidase Dye decolorizing peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.19 1.11.1.19] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5fw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fw4 OCA], [http://pdbe.org/5fw4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fw4 RCSB], [http://www.ebi.ac.uk/pdbsum/5fw4 PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fw4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fw4 OCA], [https://pdbe.org/5fw4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fw4 RCSB], [https://www.ebi.ac.uk/pdbsum/5fw4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fw4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DYP_THEFY 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.<ref>PMID:19967355</ref> | + | [https://www.uniprot.org/uniprot/DYP_THEFY 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.<ref>PMID:19967355</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Dye decolorizing peroxidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Bugg, T D.H]] | + | [[Category: Thermobifida fusca YX]] |
| - | [[Category: Fulop, V]] | + | [[Category: Bugg TDH]] |
| - | [[Category: Jamshidi, S]] | + | [[Category: Fulop V]] |
| - | [[Category: Rahmanpour, R]] | + | [[Category: Jamshidi S]] |
| - | [[Category: Rea, D]] | + | [[Category: Rahmanpour R]] |
| - | [[Category: Decolorizing peroxidase]]
| + | [[Category: Rea D]] |
| - | [[Category: Dyp]]
| + | |
| - | [[Category: Lignin oxidation]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| 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
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