Cloning, Baeyer-Villiger Biooxidations, and Structures of the Camphor Pathway 2-Oxo-Δ³-4,5,5-Trimethylcyclopentenylacetyl-Coenzyme A Monooxygenase of Pseudomonas putida ATCC 17453

Supplemental material

Files in this Data Supplement:

• Supplemental file 1 - Protein purification (Material SM1); chiral GC analysis (Material SM2); spectroscopic data (Material SM3); synthesis of 2-oxo-Δ-3-4,5,5-trimethylcyclopentynyl acidic acid and synthesis of 2-oxo-Δ-3-4,5,5-trimethylcyclopentynyl CoA-ester (Fig. S1); structure-based sequence alignment of OTEMO, CHMO and PAMO based on their structure superposition (Fig. S2); SDS-PAGE of purified OTEMO and mutants (Fig. S3); structural superposition of OTEMO, CHMO, and PAMO (Fig. S4); surface comparison of all NADP-bound BVMO proteins (Fig. S5); superposition of open and closed forms of the OTEMO-FAD-NADP complexes showing the putative cork-bottle mechanism upon substrate binding (Fig. S6); electrostatic potential of the active site pocket viewed from the same orientation from Fig. S5a (Fig. S7); X-ray data collection and refinement statistics (Table S1); purification of OTEMO using a three-step chromatographic approach (Table S2).
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