6GSG

Crystal structure of Aspergillus oryzae catechol oxidase complexed with resorcinol

Summary for 6GSG

• Entry DOI: 10.2210/pdb6gsg/pdb
• Descriptor: Catechol oxidase, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, COPPER (II) ION, ... (8 entities in total)
• Functional Keywords: catechol oxidase, coupled binuclear copper enzyme, oxidoreductase
• Biological source: Aspergillus oryzae (strain ATCC 42149 / RIB 40)
• Total number of polymer chains: 1
• Total formula weight: 44233.73

Authors

Penttinen, L.,Hakulinen, N.,Rouvinen, J. (deposition date: 2018-06-14, release date: 2018-09-19, Last modification date: 2024-10-23)

Primary citation

Penttinen, L.,Rutanen, C.,Janis, J.,Rouvinen, J.,Hakulinen, N.
Unraveling Substrate Specificity and Catalytic Promiscuity of Aspergillus oryzae Catechol Oxidase.
Chembiochem, 19:2348-2352, 2018

PubMed Abstract: 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.

PubMed: 30204291
DOI: 10.1002/cbic.201800387

Experimental method

X-RAY DIFFRACTION (2.192 Å)