L-DOPA dioxygenase is part of a mini-pathway to the synthon 3-vinyl-2,3-pyrroline-5-carboxylic acid (VPCA) that is elaborated and embedded within the final product structures of lincomycin, anthramycin, sibiromycin, tomaymycin and hormaomycin. Using the VPCA mini-pathway as a starting point, we searched sequence space to identify novel natural product pathways containing a VPCA synthon. From among these novel natural product pathways, representative L-DOPA dioxygenase gene products from Streptomyces hygroscopicus subsp.jinggangensis and Nocardia arthriditis were studied as pure proteins for their stability and activity on L-DOPA and related catechols in steady-state assays for catechol cleavage. These results were analyzed in comparison to characterized L-DOPA dioxygenases from Streptomyces lincolnensis and Streptomyces sclerotialus.
