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Literature summary for 1.1.1.1 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
Search for more literature for 1.1.1.1

Inhibitors

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
 Equus caballus
-
liver
-
 Equus caballus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyl alcohol + acycloNAD+ acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety Equus caballus benzaldehyde + acycloNADH + H+
-
 ?
butan-1-ol + acycloNAD+ acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety Equus caballus butanal + acycloNADH + H+
-
 ?
ethanol + acycloNAD+ acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moietyhas been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety Equus caballus acetaldehyde + acycloNADH + H+
-
 ?
hexan-1-ol + acycloNAD+ acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety Equus caballus hexanal + acycloNADH + H+
-
 ?
additional information acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety.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 ?
-
 ?
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

Cofactor Comment Organism Structure
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]

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