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Literature summary for 1.2.1.4 extracted from

  • Muraoka, H.; Watabe, Y.; Ogasawara, N.; Takahashi, H.
    Purification and properties of five NADP-dependent aldehyde dehydrogenases from Acetobacter aceti (1980), J. Ferment. Technol., 58, 501-507.
No PubMed abstract available
Search for more literature for 1.2.1.4

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline enzyme a, b, c, d and e Acetobacter aceti
Co2+ 1 mM, enzyme a and e Acetobacter aceti
diphosphate enzyme a, b, c, d and e Acetobacter aceti
EDTA enzyme a, b, c, d and e Acetobacter aceti
Fe2+ 0.1 mM, enzyme a, b, c, d and e Acetobacter aceti
ferricyanide enzyme a, b, c and e Acetobacter aceti
monoiodoacetate enzyme a, b, c, d and e Acetobacter aceti
PCMB enzyme a, b, c, d and e Acetobacter aceti
Sodium arsenate enzyme b, c and d Acetobacter aceti
Sodium azide enzyme b, c and d Acetobacter aceti
Zn2+ 0.1 mM, enzyme a, b, c, d and e Acetobacter aceti

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 1 mM, slight stimulation of enzyme c Acetobacter aceti
Mg2+ 0.1 mM, 1.5-2.0fold stimulation Acetobacter aceti
Mn2+ 0.1 mM, 1.5-2.0fold stimulation Acetobacter aceti

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58000
-
 1 * 58000, enzyme c, SDS-PAGE Acetobacter aceti
65000
-
 1 * 65000, enzyme a, SDS-PAGE Acetobacter aceti
70000
-
 1 * 70000, enzyme e, SDS-PAGE Acetobacter aceti
82000
-
 1 * 82000, enzyme b, SDS-PAGE Acetobacter aceti
87000
-
 1 * 87000, enzyme d, SDS-PAGE Acetobacter aceti

Organism

Organism UniProt Comment Textmining
Acetobacter aceti
-
 aldehyde dehydrogenase a, b, c, d, and e
-

Purification (Commentary)

Purification (Comment) Organism
aldehyde dehydrogenase a, b, c, d, and e Acetobacter aceti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + NADP+ + H2O enzyme a, b, c, d and e Acetobacter aceti acetate + NADPH + H+
-
 ?
benzaldehyde + NADP+ enzyme b and e Acetobacter aceti benzoate + NADPH
-
 ?
butanal + NADP+ + H2O n-butanal, enzyme a, b, c, d and e Acetobacter aceti butyrate + NADPH + H+
-
 ?
crotonaldehyde + NADP+ weak, enzyme a, b and c Acetobacter aceti crotonate + NADPH
-
 ?
formaldehyde + NADP+ + H2O weak activity with enzyme a, b, d and e Acetobacter aceti formate + NADPH + H+
-
 ?
glyceraldehyde + NADP+ weak, enzyme a, b and d Acetobacter aceti glycerate + NADPH
-
 ?
heptanal + NADP+ n-heptanal, enzyme b, c and e Acetobacter aceti heptanoate + NADPH
-
 ?
octanal + NADP+ + H2O n-octanal, enzyme b, c, d and e Acetobacter aceti octanoate + NADPH + H+
-
 ?
pentanal + NADP+ n-pentanal, enzyme a, b, c, d and e Acetobacter aceti pentanoate + NADPH
-
 ?
propanal + NADP+ + H2O enzyme a, b, c, d and e Acetobacter aceti propionate + NADPH + H+
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 58000, enzyme c, SDS-PAGE Acetobacter aceti
monomer 1 * 70000, enzyme e, SDS-PAGE Acetobacter aceti
monomer 1 * 87000, enzyme d, SDS-PAGE Acetobacter aceti
monomer 1 * 82000, enzyme b, SDS-PAGE Acetobacter aceti
monomer 1 * 65000, enzyme a, SDS-PAGE Acetobacter aceti

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 stable up to Acetobacter aceti
60
-
 loss of activity above Acetobacter aceti

pH Stability

pH Stability pH Stability Maximum Comment Organism
8 9 most stable from pH 8.0 to pH 9.0 Acetobacter aceti

Cofactor

Cofactor Comment Organism Structure
NADP+
-
 Acetobacter aceti