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Literature summary for 1.1.1.71 extracted from

  • Rhodes, M.J.C.
    Co-factor specificity of plant alcohol dehydrogenase (1973), Phytochemistry, 12, 307-314.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
4-chloromercuribenzoate
-
Cucumis melo
o-phenanthroline 1 mM, 30% inhibition after 3 h incubation Cucumis melo

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.024
-
NADH
-
Cucumis melo
0.32
-
NADPH
-
Cucumis melo
1.3
-
acetaldehyde cofactor NADH Cucumis melo
8.8
-
acetaldehyde cofactor NADPH Cucumis melo

Organism

Organism UniProt Comment Textmining
Cucumis melo
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate, DEAE-cellulose, Sephadex G-100 Cucumis melo

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + NADH + H+
-
Cucumis melo ethanol + NAD+
-
r
acetaldehyde + NADPH + H+
-
Cucumis melo ethanol + NADP+
-
r
retinaldehyde + NADH
-
Cucumis melo retinol + NAD+
-
?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.7
-
aldehyde reduction Cucumis melo
9.5
-
ethanol oxidation, cofactor NAD+ Cucumis melo

pH Range

pH Minimum pH Maximum Comment Organism
5 9 aldehyde reduction, cofactor NADH, NADP dependent activity occurs only at pHs below 7 Cucumis melo
7 10.5 ethanol oxidation, cofactor NAD+ Cucumis melo

Cofactor

Cofactor Comment Organism Structure
NAD(P)H
-
Cucumis melo