Dioxygenase enzymes are essential protein catalysts for the breakdown of catecholic rings, structural components of plant woody tissue. This powerful chemistry is used in nature to make antibiotics and other bioactive materials as well as degrade plant material, but we have a limited understanding of the breadth and depth of substrate space for these powerful enzymes. Here we report the steady-state kinetic analysis of dopamine derivatives substituted at the 6-position as substrates of L-DOPA dioxygenase, and an analysis of that activity as a function of the electron withdrawing nature of the substituent. The variety of substrates accepted by the enzyme is indicative of the utility of extradiol cleavage in semisynthetic and bioremediation applications

Steady-state kinetics on 6-substituted derivatives of dopamine as substrates of L-DOPA dioxygenase

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.