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Literature summary extracted from

  • Malver, O.; Sebastian, M.J.; Oppenheimer, N.J.
    Alteration in substrate specificity of horse liver alcohol dehydrogenase by an acyclic nicotinamide analog of NAD(+) (2014), DNA Repair, 23, 95-100.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.1 Cyclohexanol competitive Equus caballus
1.1.1.1 propan-2-ol competitive Equus caballus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.1 0.3
-
 acycloNAD+ substrate butan-1-ol, pH 8.0, 25°C Equus caballus
1.1.1.1 0.33
-
 acycloNAD+ substrate hexan-1-ol, pH 8.0, 25°C Equus caballus
1.1.1.1 0.33
-
 acycloNAD+ substrate propan-1-ol, pH 8.0, 25°C Equus caballus
1.1.1.1 0.36
-
 acycloNAD+ substrate ethanol, pH 8.0, 25°C Equus caballus
1.1.1.1 0.61
-
 acycloNAD+ substrate benzyl alcohol, pH 8.0, 25°C Equus caballus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Equus caballus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.1 commercial preparation
-
 Equus caballus
-
1.1.1.1 liver
-
 Equus caballus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 benzyl alcohol + acycloNAD+ acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety Equus caballus benzaldehyde + acycloNADH + H+
-
 ?
1.1.1.1 butan-1-ol + acycloNAD+ acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety Equus caballus butanal + acycloNADH + H+
-
 ?
1.1.1.1 ethanol + acycloNAD+ acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moietyhas been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety Equus caballus acetaldehyde + acycloNADH + H+
-
 ?
1.1.1.1 hexan-1-ol + acycloNAD+ acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety Equus caballus hexanal + acycloNADH + H+
-
 ?
1.1.1.1 additional information acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety. There is no detectable reduction of acycloNAD+ by secondary alcohols although these alcohols serve as competitive inhibitors. AcycloNAD+ converts horse liver ADH from a broad spectrum alcohol dehydrogenase, capable of utilizing either primary or secondary alcohols, into an exclusively primary alcohol dehydrogenase Equus caballus ?
-
 ?
1.1.1.1 propan-1-ol + acycloNAD+ acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety Equus caballus propanal + acycloNADH + H+
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 acycloNAD+ NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety. The chemical properties are comparable to those of beta-NAD+ with a redox potential of -324 mV and a 341 nm lambdamax for the reduced form. The stereochemistry of the hydride transfer in the oxidation of n-butanol is identical to that for the reaction with beta-NAD+. There is no detectable reduction of acycloNAD+ by secondary alcohols although these alcohols serve as competitive inhibitors. AcycloNAD+ converts horse liver ADH from a broad spectrum alcohol dehydrogenase, capable of utilizing either primary or secondary alcohols, into an exclusively primary alcohol dehydrogenase Equus caballus

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.1.1 9.7
-
 Cyclohexanol pH 8.0, 25°C Equus caballus
1.1.1.1 96
-
 propan-2-ol pH 8.0, 25°C Equus caballus