Literature summary for 1.2.1.3 extracted from

Lee, Y.C.; Lin, D.T.; Ong, P.L.; Chen, H.L.; Lo, H.F.; Lin, L.L.
Contribution of conserved Glu255 and Cys289 residues to catalytic activity of recombinant aldehyde dehydrogenase from Bacillus licheniformis (2011), Biochemistry, 76, 1233-1241.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli M15 (pREP4) cells	Bacillus licheniformis

Protein Variants

Protein Variants	Comment	Organism
C289D	enzyme activity is nearly abolished in this mutant	Bacillus licheniformis
C289P	enzyme activity is nearly abolished in this mutant	Bacillus licheniformis
C289R	enzyme activity is nearly abolished in this mutant	Bacillus licheniformis
E255D	the mutant enzyme shows severely diminished activity	Bacillus licheniformis
E255K	the mutant enzyme shows severely diminished activity	Bacillus licheniformis

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
53000	-	x * 53000, SDS-PAGE	Bacillus licheniformis

Organism

Organism	UniProt	Comment	Textmining
Bacillus licheniformis	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
Ni2+-NTA resin column chromatography	Bacillus licheniformis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
propionaldehyde + NAD+ + H2O	-	Bacillus licheniformis	propionate + NADH + H+	-	?

Subunits

Subunits	Comment	Organism
?	x * 53000, SDS-PAGE	Bacillus licheniformis

Synonyms

Synonyms	Comment	Organism
ALDH	-	Bacillus licheniformis

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Bacillus licheniformis

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Release 2023.1 (January 2023)