6gsg: Difference between revisions
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The | ==Crystal structure of Aspergillus oryzae catechol oxidase complexed with resorcinol== | ||
<StructureSection load='6gsg' size='340' side='right' caption='[[6gsg]], [[Resolution|resolution]] 2.19Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6gsg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GSG FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PEO:HYDROGEN+PEROXIDE'>PEO</scene>, <scene name='pdbligand=RCO:RESORCINOL'>RCO</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=6gsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gsg OCA], [http://pdbe.org/6gsg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gsg RCSB], [http://www.ebi.ac.uk/pdbsum/6gsg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gsg ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Catechol oxidases and tyrosinases are coupled binuclear copper enzymes that oxidize various o-diphenolic compounds to corresponding o-quinones. Tyrosinases have an additional monooxygenation ability to hydroxylate monophenol to o-diphenol. It is still not clear what causes the difference in the catalytic activities. We solved a complex structure of Aspergillus oryzae catechol oxidase with resorcinol bound into the active site. Catalytic activity of A. oryzae catechol oxidase was studied, for the first time, by high-resolution FT-ICR mass spectrometry to shed light on the reaction mechanism. The enzyme was also found to catalyze monooxygenation of small phenolics, which provides a novel perspective for the discussion of differences in the catalytic activity between tyrosinases and catechol oxidases. According to the results, two binding modes for resorcinol are suggested and a reaction mechanism for coupled binuclear copper enzymes is discussed. | |||
Unraveling substrate specificity and catalytic promiscuity of Aspergillus oryzae catechol oxidase.,Penttinen L, Rutanen C, Janis J, Rouvinen J, Hakulinen N Chembiochem. 2018 Sep 11. doi: 10.1002/cbic.201800387. PMID:30204291<ref>PMID:30204291</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6gsg" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hakulinen, N]] | |||
[[Category: Penttinen, L]] | |||
[[Category: Rouvinen, J]] | [[Category: Rouvinen, J]] | ||
[[Category: | [[Category: Catechol oxidase]] | ||
[[Category: | [[Category: Coupled binuclear copper enzyme]] | ||
[[Category: Oxidoreductase]] | |||
