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| | <StructureSection load='1t2x' size='340' side='right'caption='[[1t2x]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1t2x' size='340' side='right'caption='[[1t2x]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1t2x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Fusarium_sp. Fusarium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1T2X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1t2x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_sp. Fusarium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T2X 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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gog|1gog]], [[1k3i|1k3i]]</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=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sac1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29916 Fusarium sp.])</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=1t2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2x OCA], [https://pdbe.org/1t2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t2x RCSB], [https://www.ebi.ac.uk/pdbsum/1t2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t2x ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Galactose_oxidase Galactose oxidase], with EC number [http://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'>[http://proteopedia.org/fgij/fg.htm?mol=1t2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2x OCA], [http://pdbe.org/1t2x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t2x RCSB], [http://www.ebi.ac.uk/pdbsum/1t2x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t2x ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t2/1t2x_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t2/1t2x_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Fusarium sp]] | | [[Category: Fusarium sp]] |
| - | [[Category: Galactose oxidase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Akumanyi, N]] | + | [[Category: Akumanyi N]] |
| - | [[Category: Dawkes, H]] | + | [[Category: Dawkes H]] |
| - | [[Category: Hurtado-Guerrero, R]] | + | [[Category: Hurtado-Guerrero R]] |
| - | [[Category: Knowles, P F]] | + | [[Category: Knowles PF]] |
| - | [[Category: McPherson, M J]] | + | [[Category: McPherson MJ]] |
| - | [[Category: Phillips, S E.V]] | + | [[Category: Phillips SEV]] |
| - | [[Category: Wilkinson, D]] | + | [[Category: Wilkinson D]] |
| - | [[Category: Blade beta propeller]]
| + | |
| - | [[Category: C383s mutant form]]
| + | |
| - | [[Category: Mutant form of copper containing enzyme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| 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; E.C. 1.1.3.9) is a copper- containing enzyme that oxidizes a range of primary alcohols to aldehydes. This broad substrate specificity is reflected in a high K(M) for substrates. Directed evolution has previously been used to select variants of GO that exhibit enhanced expression and kinetic properties. In assays using unpurified enzyme samples, the variant C383S displayed a 5-fold lower K(M) than wild-type GO. In the present study, we have constructed, expressed, purified and characterized a number of single, double and triple mutants at residues Cys383, Tyr436 and Val494, identified in one of the directed evolution studies, to examine their relative contributions to improved catalytic activity of GO. We report kinetic studies on the various mutant enzymes. In addition, we have determined the three-dimensional structure of the C383S variant. As with many mutations identified in directed evolution experiments, the availability of structural information does not provide a definitive answer to the reason for the improved K(M) in the C383S variant protein.
Structural and kinetic studies of a series of mutants of galactose oxidase identified by directed evolution.,Wilkinson D, Akumanyi N, Hurtado-Guerrero R, Dawkes H, Knowles PF, Phillips SE, McPherson MJ Protein Eng Des Sel. 2004 Feb;17(2):141-8. Epub 2004 Jan 12. PMID:15047910[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
- ↑ Wilkinson D, Akumanyi N, Hurtado-Guerrero R, Dawkes H, Knowles PF, Phillips SE, McPherson MJ. Structural and kinetic studies of a series of mutants of galactose oxidase identified by directed evolution. Protein Eng Des Sel. 2004 Feb;17(2):141-8. Epub 2004 Jan 12. PMID:15047910 doi:10.1093/protein/gzh018
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