Studies on the Mechanism of Ring Hydrolysis in Phenylacetate Degradation

Supplemental Data

Files in this Data Supplement:

  • Supplemental Figure 3 (.doc, 35 KB) - Mass spectrometric analysis of derivatized 3-oxo-5,6-dehydrosuberyl-CoA
  • Supplemental Figure 6 (.doc, 46 KB) - Partial sequence alignment of PaaZ (E. coli), BoxD (A. evansii), PacL (A. aromaticum), Bacillus ALDH (B. halodurans), ALDH2 (Bos taurus) and of V. harveyi ALDH
  • Supplemental Figure 5 (.doc, 25 KB) - Partial sequence alignment of a selection of PaaZ orthologues from Escherichia coli K12, Sinorhizobium meliloti 1021, Thiomonas intermedia K12, Rhodococcus erythropolis PR4, Flavobacteriaceae bacterium 3519-10 and Thermus thermophilus HB27, as well as (R)-specific enoyl-CoA hydratases from Aeromonas caviae and Candida tropicalis
  • Supplemental Table 1 (.doc, 403 KB) - Overview of all completely sequenced bacteria that harbor key genes (paaA, paaC) for phenylacetate catabolism and the distribution of paaZ, pacL and genes encoding Bacillus ALDH
  • Supplemental Figure 4 (.doc, 51 KB) - UV-vis spectrum of 3-oxo-5,6-dehydrosuberyl-CoA at pH 8.0, pH 10.0 and pH 8.0 with MgCl2
  • Supplemental Figure 2 (.doc, 35 KB) - Isotopic resolved mass spectrometric analysis of the product of oxepin-CoA conversion by PaaZ in the presence of 50% H218O and NADP+
  • Supplemental Figure 1 (.doc, 44 KB) - Mass spectrometric analysis of the derivative formed after oxepin-CoA hydrolysis by fusion protein PaaZ-E256Q