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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.2.1.4 1,10-phenanthroline enzyme a, b, c, d and e Acetobacter aceti
1.2.1.4 Co2+ 1 mM, enzyme a and e Acetobacter aceti
1.2.1.4 diphosphate enzyme a, b, c, d and e Acetobacter aceti
1.2.1.4 EDTA enzyme a, b, c, d and e Acetobacter aceti
1.2.1.4 Fe2+ 0.1 mM, enzyme a, b, c, d and e Acetobacter aceti
1.2.1.4 ferricyanide enzyme a, b, c and e Acetobacter aceti
1.2.1.4 monoiodoacetate enzyme a, b, c, d and e Acetobacter aceti
1.2.1.4 PCMB enzyme a, b, c, d and e Acetobacter aceti
1.2.1.4 Sodium arsenate enzyme b, c and d Acetobacter aceti
1.2.1.4 Sodium azide enzyme b, c and d Acetobacter aceti
1.2.1.4 Zn2+ 0.1 mM, enzyme a, b, c, d and e Acetobacter aceti

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.1.4 58000
-
 1 * 58000, enzyme c, SDS-PAGE Acetobacter aceti
1.2.1.4 65000
-
 1 * 65000, enzyme a, SDS-PAGE Acetobacter aceti
1.2.1.4 70000
-
 1 * 70000, enzyme e, SDS-PAGE Acetobacter aceti
1.2.1.4 82000
-
 1 * 82000, enzyme b, SDS-PAGE Acetobacter aceti
1.2.1.4 87000
-
 1 * 87000, enzyme d, SDS-PAGE Acetobacter aceti

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.2.1.4 50
-
 stable up to Acetobacter aceti
1.2.1.4 60
-
 loss of activity above Acetobacter aceti

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.2.1.4 8 9 most stable from pH 8.0 to pH 9.0 Acetobacter aceti

Cofactor

EC Number Cofactor Comment Organism Structure
1.2.1.4 NADP+
-
 Acetobacter aceti