4mih
From Proteopedia
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==Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant== | ==Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant== | ||
<StructureSection load='4mih' size='340' side='right' caption='[[4mih]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4mih' size='340' side='right' caption='[[4mih]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p2o, p2ox, pox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5306 Chrysosporium pruinosum (Gilman & Abbott) Carmich.])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">p2o, p2ox, pox ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5306 Chrysosporium pruinosum (Gilman & Abbott) Carmich.])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.10 1.1.3.10] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyranose_oxidase Pyranose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.10 1.1.3.10] </span></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=4mih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mih OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mih RCSB], [http://www.ebi.ac.uk/pdbsum/4mih PDBsum]</span></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=4mih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mih OCA], [http://pdbe.org/4mih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mih RCSB], [http://www.ebi.ac.uk/pdbsum/4mih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mih ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | {{Large structure}} | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH]] Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref> | [[http://www.uniprot.org/uniprot/P2OX_PHACH P2OX_PHACH]] Catalyzes the oxidation of various aldopyranoses and disaccharides on carbon-2 to the corresponding 2-keto sugars concomitant with the reduction of O(2) to H(2)O(2). Plays an important role in lignin degradation of wood rot fungi by supplying the essential cosubstrate H(2)O(2) for the ligninolytic peroxidases, lignin peroxidase and manganese-dependent peroxidase. The preferred substrate is D-glucose which is converted to 2-dehydro-D-glucose, an intermediate of a secondary metabolic pathway leading to the antibiotic cortalcerone. Acts also on D-xylose, together with D-glucose the major sugars derived from wood, on L-sorbose, D-galactose and 1,5-anhydroglucitol, a diagnostic marker of diabetes mellitus.<ref>PMID:9210340</ref> <ref>PMID:8661938</ref> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4mih" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Pyranose oxidase|Pyranose oxidase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 18:32, 4 August 2016
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Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant H158A mutant
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