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Literature summary for extracted from

  • Di Costanzo, L.; Gomez, G.A.; Christianson, D.W.
    Crystal structure of lactaldehyde dehydrogenase from Escherichia coli and inferences regarding substrate and cofactor specificity (2006), J. Mol. Biol., 366, 481-493.
    View publication on PubMedView publication on EuropePMC


Cloned (Comment) Organism
expression in Escherichia coli Escherichia coli
heterologous expression with taxadiene synthase in Escherichia coli BL21(DE3) Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
by the hanging-drop, vapor-diffusion method. Serendipitous crystal structure of unliganded lactaldehyde dehydrogenase determined by multiple isomorphous replacement using anomalous scattering, at 2.2 A resolution. Crystal structure of the ternary enzyme complex with products lactate and NADH at 2.1 A resolution, and binary complex complex with NADPH at 2.7 A resolution. The ternary complex reveals that the nicotinamide ring of NADH occupies two distinct conformations, one with the ring positioned in the active site in the so-called hydrolysis conformation and another with the ring extended out of the active site into the solvent region Escherichia coli
in complex with NADH and lactate Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
SDS-PAGE Escherichia coli


Organism UniProt Comment Textmining
Escherichia coli P25553

Purification (Commentary)

Purification (Comment) Organism
by gel filtration Escherichia coli
three chromatography steps Escherichia coli

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lactaldehyde + NAD+ + H2O
Escherichia coli L-lactate + NADH + H+


Subunits Comment Organism
tetramer 4 * 50000, crystal structure Escherichia coli


Synonyms Comment Organism
Escherichia coli
Lactaldehyde dehydrogenase
Escherichia coli


Cofactor Comment Organism Structure
additional information the negatively charged carboxylate group of E179 destabilizes the binding of the 2'-phosphate group of NADPH sterically and electrostatically, thereby accounting for the lack of enzyme activity with this cofactor Escherichia coli
NAD+ cofactor flexibility in the constricted active site plays a significant role in the mechanism of oxidation of lactaldehyde to lactate Escherichia coli