Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution.

Abstract

2-Keto-3-deoxy-6-phosphogluconate (KDPG) aldolase catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. The enzyme is a class I aldolase whose reaction mechanism involves formation of Schiff base intermediates between Lys-133 and a keto substrate. A covalent adduct was trapped by flash freezing KDPG aldolase crystals soaked… (More)

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Cite this paper

@article{Allard2001CovalentIT, title={Covalent intermediate trapped in 2-keto-3-deoxy-6- phosphogluconate (KDPG) aldolase structure at 1.95-A resolution.}, author={J. Allard and Pawel Grochulski and Jurgeb Sygusch}, journal={Proceedings of the National Academy of Sciences of the United States of America}, year={2001}, volume={98 7}, pages={3679-84} }