L-DOPA dioxygenase cleaves L-DOPA with molecular oxygen - an essential step in the conversion of L-DOPA to the antibiotic, lincomycin. Diversifying the substrate pool of L-DOPA dioxygenase could yield new antibiotic structures, but enzymatic activity on non-native substrates is poor due to impaired oxygen binding. Using the recently solved crystal structure of L-DOPA dioxygenase from <i>Streptomyces sclerotialus</i> (SsDDO), active-site mutations were designed to improve activity on non-native substrates such as bromodopamine. Mutants L46W and L46R were prepared using site-directed mutagenesis, expressed and purified. Steady-state activity and crystallography were used to reveal how active site perturbations accommodate new substrates.

Mutagenesis of L-DOPA dioxygenase to improve activity on non-native substrates

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