Lilia Kaustov

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In this report the mode of inhibition of mechanism-based inhibitor (2, K(i) = 0.4 microM) of 3-deoxy-d-manno-2-octulosonate-8-phosphate synthase (KDO8PS), which was designed to mimic the combined key features of its natural substrates arabinose-5-phosphate (A5P) and phoshoenolpyruvate (PEP) into a single molecule, was investigated. Our earlier solid-state(More)
15N¿(31)P¿ REDOR NMR experiments were applied to lyophilized binary complexes of 3-deoxy-D-manno-2-octulosonate-8-phosphate synthase (KDO8PS), with each of its natural substrates, phosphoenolpyruvate (PEP) and arabinose-5-phsophate (A5P), and with a mechanism-based inhibitor (K(i) = 0.4 microM), directly characterizing the active site basic residues(More)
Proton decoupled 31P and 13C solution NMR experiments were applied to mixtures of 3-deoxy-D-manno-2-octulosonate-8-phosphate (KDO8P) synthase, with each of its natural substrates, phosphoenolpyruvate and arabinose-5-phosphate (ASP), and product KDO8P to identify the formation of the enzyme-substrate and enzyme-product complexes. Effects arising from ligand(More)
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