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Unraveling substrate specificity and catalytic promiscuity of Aspergillus oryzae catechol oxidase

DOI: 10.1002/cbic.201800387 DOI Help

Authors: Leena Penttinen (University of Eastern Finland) , Chiara Rutanen (University of Eastern Finland) , Janne Jänis (University of Eastern Finland) , Juha Rouvinen (University of Eastern Finland) , Nina Hakulinen (University of Eastern Finland)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chembiochem

State: Published (Approved)
Published: September 2018
Diamond Proposal Number(s): 10291

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.

Journal Keywords: catechol oxidase; coupled binuclear copper enzyme; enzyme promiscuity; mass spectrometry

Diamond Keywords: Enzymes

Subject Areas: Chemistry, Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Added On: 03/10/2018 14:16

Discipline Tags:

Catalysis Life Sciences & Biotech Structural biology Chemistry Biochemistry

Technical Tags:

Diffraction Macromolecular Crystallography (MX)