Ralph H. Lambalot

TL;DR: This work has identified a large family of proteins having 12-22 % similarity with ACPS, which are putative P-pant transferases, and found three of these proteins, E. coli EntD and o195, and subtilis Sfp, have been overproduced, purified and found to have P- pant transferase activity.

TL;DR: The 70,000-fold purification of wild-type ACPS and the overproduction and initial characterization of recombinant ACPS from E. coli are reported and dpj, an essential gene of previously unknown function, is identified as the structural gene for ACPS.

TL;DR: The results suggest that in vitro, both PHA synthases are very specific and provide further support for their active site structural similarities and differ from studies in vivo.

TL;DR: It is shown that a conditional acpS mutant accumulates apoACPin vivo under nonpermissive conditions in a manner similar to the E. coli MP4 strain, and it is demonstrated that the gene product, YhhU, of a previously identified E. Escherichia coli open reading frame can completely suppress theacpS conditional, lethal phenotype upon overexpression of the protein.

TL;DR: It is demonstrated that E. coli holo-ACP synthase (ACPS), a fatty acid biosynthesis enzyme, can catalyze P-pant transfer in vitro to the Streptomyces PKS ACPs required for the biosynthesis of the polyketide antibiotics granaticin, frenolicin, oxytetracycline and tetracenomycin.