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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.3 53000
-
 x * 53000, SDS-PAGE Bacillus licheniformis

Organism

EC Number Organism UniProt Comment Textmining
1.2.1.3 Bacillus licheniformis
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.2.1.3 ALDH
-
 Bacillus licheniformis

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.3 NAD+
-
 Bacillus licheniformis