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Modular type I polyketide synthases (PKSs) produce some of the most chemically complex metabolites in nature through a series of multienzyme modules. Each module contains a variety of catalytic domains to selectively tailor the growing molecule. PKS O-methyltransferases ( O-MTs) are predicted to methylate β-hydroxyl or β-keto groups, but their activity and structure have not been reported. We determined the domain boundaries and characterized the catalytic activity and structure of the StiD and StiE O-MTs, which methylate opposite β-hydroxyl stereocenters in the myxobacterial stigmatellin biosynthetic pathway. Substrate stereospecificity was demonstrated for the StiD O-MT. Key catalytic residues were identified in the crystal structures and investigated in StiE O-MT via site-directed mutagenesis and further validated with the cyanobacterial CurL O-MT from the curacin biosynthetic pathway. Initial structural and biochemical analysis of PKS O-MTs supplies a new chemoenzymatic tool, with the unique ability to selectively modify hydroxyl groups during polyketide biosynthesis.

This data article presents a description of a benchmark dataset for the multiple depot vehicle scheduling problem (MDVSP). The MDVSP is to assign vehicles from different depots to timetabled trips to minimize the total cost of empty travel and waiting. The dataset has been developed to evaluate the heuristics of the MDVSP that are presented in "A new formulation and a column generation-based heuristic for the multiple depot vehicle scheduling problem" (Kulkarni et al., 2018). The dataset contains 60 problem instances of varying size. Researchers can use the dataset to evaluate the future algorithms for the MDVSP and compare the performance with the existing algorithms. The dataset includes a program that can be used to generate new problem instances of the MDVSP.