Literature summary for 1.2.1.22 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.

Cloned(Commentary)

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

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
50000	-	SDS-PAGE	Escherichia coli

Organism

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

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

Synonyms

Synonyms	Comment	Organism
ALDH	-	Escherichia coli
Lactaldehyde dehydrogenase	-	Escherichia coli

Cofactor

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