Structure and mechanism of the Propionibacterium acnes polyunsaturated fatty acid isomerase -- Liavonchanka et al. 103 (8): 2576 Data Supplement - HTML Page - index.htslp -- Proceedings of the National Academy of Sciences

Liavonchanka et al. 10.1073/pnas.0510144103.

Supporting Figures

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Supporting Figure 5
Supporting Figure 6

Supporting Figure 5

Fig. 5. Sequence conservation between Propionibacterium acnes PUFA isomerase (PAI), Ptilota filicina polyenoic fatty acid isomerase (PFI), and UDP-galactopyranose mutase. The N-terminal FAD-binding motif (boxed in magenta) is the most conserved in all three proteins. Secondary structure elements of PAI are shown on the top.

Supporting Figure 6

Fig. 6. Analysis of the fatty acid content in PAI crystals obtained after cocrystallization of PAI with linoleic acid (LA) and conjugated a-linolenic acid (CLnA). (a) The standard chromatogram (blue curve) shows the separation of LA and conjugated LA (CLA) at retention times of 11.1 and 12.7 min, respectively. Only CLA is present in the complex crystals (black curve), proving that LA is quantitatively converted to the product CLA. Left and right ordinates correspond to the signals from CLA in the crystals and the standard, respectively. (b) Silver-ion HPLC chromatogram of the separation of a-linolenic acid (LnA) (blue curve) and CLnA extracted from crystals (black curve). (c) CLnA harbors a conjugated triene group as revealed by its characteristic UV-spectrum (triplet of absorption maxima).