First nonenzymatic synthesis of kdo8P through a mechanism similar to that suggested for the enzyme kdo8P synthase

摘要

The mechanism of Kdo8P synthase, the enzyme that catalyzes the unusual condensation of D-arabinose 5-phosphate (A5P) with phosphoenolpyruvate (PEP) to form Kdo8P, remains a Fascinating subject for bioorganic research. This paper describes the synthesis of two intramolecular Models (1 and 2) bearing an enolpyruvate moiety at C-3 of the arabinose fraction. This means That their open-chain aldehyde forms closely mimic the proposed situation, whereby two substrates A5P and PEP evolve into a ternary complex with the synthase.