Brief CommunicationN-Acylation during Glidobactin Biosynthesis by the Tridomain Nonribosomal Peptide Synthetase Module GlbF

Add time:09/07/2019    Source:sciencedirect.com

SummaryGlidobactins are hybrid NRPS-PKS natural products that function as irreversible proteasome inhibitors. A variety of medium chain 2(E),4(E)-diene fatty acids N-acylate the peptidolactam core and contribute significantly to the potency of proteasome inhibition. We have expressed the initiation NRPS module GlbF (C-A-T) in Escherichia coli and observe soluble active protein only on coexpression with the 8 kDa MbtH-like protein, GlbE. Following adenylation and installation of Thr as a T-domain thioester, the starter condensation domain utilizes fatty acyl-CoA donors to acylate the Thr1 amino group and generate the fatty acyl-Thr1-S-pantetheinyl-GlbF intermediate to be used in subsequent chain elongation. Previously proposed to be mediated via acyl carrier protein fatty acid donors, direct utilization of fatty acyl-CoA donors for N-acylation of T-domain tethered amino acids is likely a common strategy for chain initiation in NRPS-mediated lipopeptide biosynthesis.

We also recommend Trading Suppliers and Manufacturers of Glidobactin A (cas 108351-50-4). Pls Click Website Link as below: cas 108351-50-4 suppliers

Prev:Short communicationHeterologous expression of a Photorhabdus luminescens syrbactin-like gene cluster results in production of the potent proteasome inhibitor Glidobactin A (cas 108351-50-4)
Next:A proteasome inhibitor produced by Burkholderia pseudomallei modulates intracellular growth)