Protein Assembly Line Components in Prodigiosin Biosynthesis: Characterization of PigA,G,H,I,J

摘要: The red streptomycete metabolite prodigiosin has a unique tripyrrolic structure with two of the three pyrrolyl moieties in tandem. Five enzymes, PigA,G,H,I, and J, are involved dipyrrole (rings A B) formation. We have heterologously expressed purified from Escherichia coli these five enzymes. At first, pyrrole ring is formed on peptidyl carrier protein PigG by one possible ways: (i) action adenylation domain PigI that transforms l-proline into l-prolyl-AMP flavoprotein dehydrogenase PigA responsible for four-electron oxidation reaction; (ii) loading pyrrolyl-2-carboxyl-(S)-pantetheinyl moiety synthetic pyrrolyl-CoA using phosphopantetheinyl transferase Sfp. Subsequently, B constructed PigH after transfer to ketosynthase PigJ. consists domains: acyl proteins (ACPs) seryltransferase (SerT). Using HPLC nanospray-Fourier Transform Mass Spectrometry (nFTMS), we established all domains undergo post-translational modifications gained insight machinery 2,2-dipyrrole biosynthesis.