6gsg

Crystal structure of Aspergillus oryzae catechol oxidase complexed with resorcinol

spinqualitylabelsall models 6gsg, resolution 2.19Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6gsg is a 1 chain structure with sequence from Aspergillus oryzae RIB40. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.192Å Ligands: BMA, CU, MAN, NAG, PEO, RCO, SEP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q2UNF9_ASPOR 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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