Figure 3 - Characterization of TdiA.
From the following article
Terrequinone A biosynthesis through L-tryptophan oxidation, dimerization and bisprenylation
Carl J Balibar, Annaleise R Howard-Jones & Christopher T Walsh
Nature Chemical Biology 3, 584 - 592 (2007) Published online: 12 August 2007
doi:10.1038/nchembio.2007.20
(a) Domain organization for TdiA. Inset table shows the ten amino acids conferring substrate specificity based on residue positions within PheA46 (shown in blue) for TdiA, four L-tryptophan–activating A domains and four 
-keto acid–activating A domains. Numbers in parentheses refer to the module number in multimodular NRPSs. (b) Michaelis-Menten plot for activation of IPA by TdiA. (c) HPLC traces (280 nm) showing products resulting from incubation of IPA with TdiA. Peaks corresponding to IPA appear at Rt 34.8 min and didemethylasterriquinone D at Rt 40.4 min. (d) Mass spectrum (ES-
) of didemethylasterriquinone D product resulting from TdiA incubation.
