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| | <StructureSection load='2jkx' size='340' side='right'caption='[[2jkx]], [[Resolution|resolution]] 1.84Å' scene=''> | | <StructureSection load='2jkx' size='340' side='right'caption='[[2jkx]], [[Resolution|resolution]] 1.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jkx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusairum_graminearum Fusairum graminearum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JKX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jkx]] 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=2JKX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JKX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.84Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t2x|1t2x]], [[1goh|1goh]], [[2vz3|2vz3]], [[1gof|1gof]], [[2vz1|2vz1]], [[1k3i|1k3i]], [[1gog|1gog]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Galactose_oxidase Galactose oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.9 1.1.3.9] </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=2jkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jkx OCA], [https://pdbe.org/2jkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jkx RCSB], [https://www.ebi.ac.uk/pdbsum/2jkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jkx 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=2jkx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jkx OCA], [https://pdbe.org/2jkx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jkx RCSB], [https://www.ebi.ac.uk/pdbsum/2jkx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jkx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/GAOA_GIBZE GAOA_GIBZE]] Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides (By similarity).
| + | [https://www.uniprot.org/uniprot/GAOA_GIBZA GAOA_GIBZA] Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides.<ref>PMID:13641238</ref> <ref>PMID:4441089</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fusairum graminearum]] | + | [[Category: Fusarium graminearum]] |
| - | [[Category: Galactose oxidase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Deacon, S E]] | + | [[Category: Deacon SE]] |
| - | [[Category: Firbank, S J]] | + | [[Category: Firbank SJ]] |
| - | [[Category: Knowles, P F]] | + | [[Category: Knowles PF]] |
| - | [[Category: Mahmoud, K]] | + | [[Category: Mahmoud K]] |
| - | [[Category: McPherson, M J]] | + | [[Category: McPherson MJ]] |
| - | [[Category: Phillips, S E.V]] | + | [[Category: Phillips SEV]] |
| - | [[Category: Spooner, R K]] | + | [[Category: Spooner RK]] |
| - | [[Category: Copper]]
| + | |
| - | [[Category: Copper enzyme]]
| + | |
| - | [[Category: Enzyme catalysis]]
| + | |
| - | [[Category: Kelch repeat]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Oxidase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Protein engineering]]
| + | |
| - | [[Category: Secreted]]
| + | |
| - | [[Category: Thioether bond]]
| + | |
| Structural highlights
Function
GAOA_GIBZA Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Galactose oxidase (GO; EC 1.1.3.9) catalyses the oxidation of a wide range of primary alcohols including mono-, oligo- and polysaccharides. High-resolution structures have been determined for GO, but no structural information is available for the enzyme with bound substrate or inhibitor. Previously, computer-aided docking experiments have been used to develop a plausible model for interactions between GO and the D-galactose substrate. Residues implicated in such interactions include Arg330, Gln406, Phe464, Phe194 and Trp290. In the present study we describe an improved expression system for recombinant GO in the methylotrophic yeast Pichia pastoris. We use this system to express variant proteins mutated at Arg330 and Phe464 to explore the substrate binding model. We also demonstrate that the Arg330 variants display greater fructose oxidase activity than does wild-type GO.
Enhanced fructose oxidase activity in a galactose oxidase variant.,Deacon SE, Mahmoud K, Spooner RK, Firbank SJ, Knowles PF, Phillips SE, McPherson MJ Chembiochem. 2004 Jul 5;5(7):972-9. PMID:15239055[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ COOPER JA, SMITH W, BACILA M, MEDINA H. Galactose oxidase from Polyporus circinatus, Fr. J Biol Chem. 1959 Mar;234(3):445-8 PMID:13641238
- ↑ Kosman DJ, Ettinger MJ, Weiner RE, Massaro EJ. The molecular properties of the copper enzyme galactose oxidase. Arch Biochem Biophys. 1974 Dec;165(2):456-67. PMID:4441089 doi:10.1016/0003-9861(74)90271-9
- ↑ Deacon SE, Mahmoud K, Spooner RK, Firbank SJ, Knowles PF, Phillips SE, McPherson MJ. Enhanced fructose oxidase activity in a galactose oxidase variant. Chembiochem. 2004 Jul 5;5(7):972-9. PMID:15239055 doi:10.1002/cbic.200300810
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