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| | <StructureSection load='6y0r' size='340' side='right'caption='[[6y0r]], [[Resolution|resolution]] 1.61Å' scene=''> | | <StructureSection load='6y0r' size='340' side='right'caption='[[6y0r]], [[Resolution|resolution]] 1.61Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6y0r]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Fusarium_graminearum Fusarium graminearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y0R OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6Y0R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6y0r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_graminearum Fusarium graminearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y0R FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chitO, FGRAMPH1_01T20975 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=229533 Fusarium graminearum])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chitO, FGRAMPH1_01T20975 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=229533 Fusarium graminearum])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6y0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y0r OCA], [http://pdbe.org/6y0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y0r RCSB], [http://www.ebi.ac.uk/pdbsum/6y0r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y0r ProSAT]</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=6y0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y0r OCA], [https://pdbe.org/6y0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y0r RCSB], [https://www.ebi.ac.uk/pdbsum/6y0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y0r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CHITO_GIBZE CHITO_GIBZE]] Catalyzes the selective oxidation of C1 hydroxyl moieties on chitooligosaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Chitooligosaccharides are homo- or heterooligomers of N-acetylglucosamine (GlcNAc) and D-glucosamine which are linked through beta-1,4-glycosidic bonds. For optimal substrate binding at least 2 GlcNAc units are needed, and chitooligosaccharide oxidase is most efficient on chitobiose, chitotriose and chitotetraose.<ref>PMID:17900572</ref> | + | [[https://www.uniprot.org/uniprot/CHITO_GIBZE CHITO_GIBZE]] Catalyzes the selective oxidation of C1 hydroxyl moieties on chitooligosaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Chitooligosaccharides are homo- or heterooligomers of N-acetylglucosamine (GlcNAc) and D-glucosamine which are linked through beta-1,4-glycosidic bonds. For optimal substrate binding at least 2 GlcNAc units are needed, and chitooligosaccharide oxidase is most efficient on chitobiose, chitotriose and chitotetraose.<ref>PMID:17900572</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Structural highlights
Function
[CHITO_GIBZE] Catalyzes the selective oxidation of C1 hydroxyl moieties on chitooligosaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hydrolysis. Chitooligosaccharides are homo- or heterooligomers of N-acetylglucosamine (GlcNAc) and D-glucosamine which are linked through beta-1,4-glycosidic bonds. For optimal substrate binding at least 2 GlcNAc units are needed, and chitooligosaccharide oxidase is most efficient on chitobiose, chitotriose and chitotetraose.[1]
Publication Abstract from PubMed
Chitooligosaccharide oxidase (ChitO) is a fungal carbohydrate oxidase containing a bicovalently bound FAD cofactor. The enzyme is known to catalyse the oxidation of chitooligosaccharides, oligomers of N-acetylated glucosamines derived from chitin degradation. In this study, the unique substrate acceptance was explored by testing a range of N-acetyl-D-glucosamine derivatives, revealing that ChitO preferentially accepts carbohydrates with a hydrophobic group attached to C2. The enzyme also accepts streptozotocin, a natural product used to treat tumours. Elucidation of the crystal structure provides an explanation for the high affinity towards C2-decorated glucosamines: the active site has a secondary binding pocket that accommodates groups attached at C2. Docking simulations are fully in line with the observed substrate preference. This work expands the knowledge on this versatile enzyme.
Analysis of the structure and substrate scope of chitooligosaccharide oxidase reveals high affinity for C2-modified glucosamines.,Savino S, Jensen S, Terwisscha van Scheltinga A, Fraaije MW FEBS Lett. 2020 Jun 3. doi: 10.1002/1873-3468.13854. PMID:32491191[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Heuts DP, Janssen DB, Fraaije MW. Changing the substrate specificity of a chitooligosaccharide oxidase from Fusarium graminearum by model-inspired site-directed mutagenesis. FEBS Lett. 2007 Oct 16;581(25):4905-9. doi: 10.1016/j.febslet.2007.09.019. Epub, 2007 Sep 19. PMID:17900572 doi:http://dx.doi.org/10.1016/j.febslet.2007.09.019
- ↑ Savino S, Jensen S, Terwisscha van Scheltinga A, Fraaije MW. Analysis of the structure and substrate scope of chitooligosaccharide oxidase reveals high affinity for C2-modified glucosamines. FEBS Lett. 2020 Jun 3. doi: 10.1002/1873-3468.13854. PMID:32491191 doi:http://dx.doi.org/10.1002/1873-3468.13854
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