Related Experiment Video
Updated: Oct 18, 2026

Structural Biology and Analytical Chemistry Approaches for Characterizing C-Glycoside Metabolic Enzymes in Human Gut Microbiota
Published on: May 23, 2025
Initiating a structural study of 2-keto-3-deoxy-6-phosphogluconate aldolase from Escherichia coli
L V Buchanan1, N Mehta, L Pocivavsek
1Centre for Biomedical Sciences, North Haugh, The University, St Andrews, Fife KY16 9ST, Scotland.
Abstract:
2-Keto-3-deoxy-6-phosphogluconate aldolase (KDPG aldolase, E.C. 4.1. 2.14) is a member of the pyruvate/phosphoenolpyruvate aldolase family. It is also a synthetically useful enzyme, capable of catalyzing the stereoselective aldol addition of pyruvate to a range of unnatural electrophilic substrates. The recombinant protein was purified by a two-step HPLC protocol involving anion-exchange and hydrophobic chromatography. Dynamic light-scattering experiments indicated the protein to be monodisperse. Crystals were obtained using the sitting-drop vapour-diffusion method, with PEG 6K as precipitant. Diffraction data were collected on a frozen crystal to a resolution of 2.26 A on station PX9.6 at the Daresbury synchrotron. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.2, b = 77.9, c = 146.8 A.
Related Concept Videos
Base-Catalyzed Aldol Addition Reaction
Acid-Catalyzed Aldol Addition Reaction
Glycolysis: Preparatory Phase
Intramolecular Aldol Reaction
Dehydration of Aldols to Enals: Base-Catalyzed Aldol Condensation
Aldol Condensation with β-Diesters: Knoevenagel Condensation

