Demonstration of starter unit interprotein transfer from a fatty acid synthase to a multidomain, nonreducing polyketide synthase.
The pathway for substrate transacylation between a fungal type I fatty acid synthase (FAS) and a nonreducing polyketide synthase (NR-PKS) was determined by in vitro reconstitution of dissected domains. System kinetics were influenced by domain dissections, and the FAS phosphopantetheinyl transferase (PPT) monodomain exhibited coenzyme A selectivity for the post-translational activation of the FAS acyl carrier protein (ACP).
Department of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
Jennifer
J
Foulke-Abel
Craig A
CA
Townsend
D000213:Acyl Carrier Protein / Q000378:metabolism; D000215:Acylation; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D003065:Coenzyme A / Q000378:metabolism; D064429:Fatty Acid Synthases / Q000737:chemistry / Q000378:metabolism*; D005227:Fatty Acids / Q000378:metabolism; D048630:Polyketide Synthases / Q000737:chemistry / Q000378:metabolism*; D060066:Protein Interaction Maps; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D017855:Transferases (Other Substituted Phosphate Groups) / Q000737:chemistry / Q000378:metabolism
D000213:Acyl Carrier Protein; D001426:Bacterial Proteins; D005227:Fatty Acids; C082662:phosphopantetheinyl transferase; D048630:Polyketide Synthases; D064429:Fatty Acid Synthases; D017855:Transferases (Other Substituted Phosphate Groups); D003065:Coenzyme A