Streptomyces coelicolor phosphopantetheinyl transferase: a promiscuous activator of polyketide and fatty acid synthase acyl carrier proteins

摘要

Streptomyces coelicolor is host to a number of biosynthetic proteins requiring post-translational modification by thenaddition of phosphopantetheine groups. The S. coelicolor genome, was probed, in silico, with the sequence ofnEscherichia coli holo-Acyl Carrier Protein Synthase (ACPS). A single open reading frame (ORF) strongly matchingnthe E. coli ACPS was discovered. The putative S. coelicolor ACPS ORF was cloned and expressed and the resultingnprotein purified and characterised. S. coelicolor ACPS appears to be extremely promiscuous in its substratenspecificity, accepting varied acyl CoA substrates and protein substrates from Type I and Type II fatty acid synthasesn(FAS) as well as from Type I and Type II polyketide synthase (PKS) biosynthetic protein complexes. Thisnphosphopantetheinyl transferase thus has high potential for the synthesis of diverse holo- and acylated acyl carriernproteins.