Unraveling Substrate Specificity and Catalytic Promiscuity of Aspergillus oryzae Catechol Oxidase

Leena Penttinen, Chiara Rutanen, Janne Jänis, Juha Rouvinen, Nina Hakulinen*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)2348-2352
Number of pages5
JournalCHEMBIOCHEM
Volume19
Issue number22
DOIs
Publication statusPublished - 16 Nov 2018
MoE publication typeA1 Journal article-refereed

Keywords

  • catechol oxidases
  • coupled binuclear copper enzymes
  • enzyme mechanisms
  • enzyme promiscuity
  • mass spectrometry

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