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. Author manuscript; available in PMC: 2012 Feb 1.
Published in final edited form as: Bioorg Med Chem Lett. 2008 Jan 11;18(10):3039–3042. doi: 10.1016/j.bmcl.2008.01.026

Figure 1.

Figure 1

The carrier protein–ketosynthase crosslinking reaction. ACP is loaded with a prosthetic phosphopantetheinyl group through the actions of the ATP-dependent CoA biosynthetic enzymes and Sfp in the one-pot chemo-enzymatic synthesis. The structure of the chloroacrylate pantetheine analog (1) used in these crosslinking studies is also shown. Protein-protein affinity allows the active site cysteine of the KS domain (KASI or KASII) to attack the trans-chloroacrylate functionality, thereby forming a covalent bond to crosslink ACP to KS.