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Alteration in substrate specificity of horse liver alcohol dehydrogenase by an acyclic nicotinamide analog of NAD(+)

Malver, O.; Sebastian, M.J.; Oppenheimer, N.J.; DNA Repair 23, 95-100 (2014)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
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
Commentary
Organism
Structure
1.1.1.1
0.3
-
acycloNAD+
substrate butan-1-ol, pH 8.0, 25C
Equus caballus
1.1.1.1
0.33
-
acycloNAD+
substrate hexan-1-ol, pH 8.0, 25C; substrate propan-1-ol, pH 8.0, 25C
Equus caballus
1.1.1.1
0.36
-
acycloNAD+
substrate ethanol, pH 8.0, 25C
Equus caballus
1.1.1.1
0.61
-
acycloNAD+
substrate benzyl alcohol, pH 8.0, 25C
Equus caballus
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.1.1.1
Equus caballus
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
1.1.1.1
commercial preparation
-
Equus caballus
-
1.1.1.1
liver
-
Equus caballus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.1
benzyl alcohol + NAD+
acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
738096
Equus caballus
benzaldehyde + acycloNADH + H+
-
-
-
?
1.1.1.1
butan-1-ol + NAD+
acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
738096
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acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moietyhas been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
738096
Equus caballus
acetaldehyde + acycloNADH + H+
-
-
-
?
1.1.1.1
hexan-1-ol + NAD+
acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
738096
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acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety.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
738096
Equus caballus
?
-
-
-
-
1.1.1.1
propan-1-ol + NAD+
acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
738096
Equus caballus
propanal + acycloNADH + H+
-
-
-
?
Cofactor
EC Number
Cofactor
Commentary
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
Commentary
Organism
Structure
1.1.1.1
9.7
-
Cyclohexanol
pH 8.0, 25C
Equus caballus
1.1.1.1
96
-
propan-2-ol
pH 8.0, 25C
Equus caballus
Cofactor (protein specific)
EC Number
Cofactor
Commentary
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
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.1.1.1
Cyclohexanol
competitive
Equus caballus
1.1.1.1
propan-2-ol
competitive
Equus caballus
Ki Value [mM] (protein specific)
EC Number
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
1.1.1.1
9.7
-
Cyclohexanol
pH 8.0, 25C
Equus caballus
1.1.1.1
96
-
propan-2-ol
pH 8.0, 25C
Equus caballus
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.1.1.1
0.3
-
acycloNAD+
substrate butan-1-ol, pH 8.0, 25C
Equus caballus
1.1.1.1
0.33
-
acycloNAD+
substrate hexan-1-ol, pH 8.0, 25C; substrate propan-1-ol, pH 8.0, 25C
Equus caballus
1.1.1.1
0.36
-
acycloNAD+
substrate ethanol, pH 8.0, 25C
Equus caballus
1.1.1.1
0.61
-
acycloNAD+
substrate benzyl alcohol, pH 8.0, 25C
Equus caballus
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
1.1.1.1
commercial preparation
-
Equus caballus
-
1.1.1.1
liver
-
Equus caballus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.1.1.1
benzyl alcohol + NAD+
acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
738096
Equus caballus
benzaldehyde + acycloNADH + H+
-
-
-
?
1.1.1.1
butan-1-ol + NAD+
acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
738096
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
738096
Equus caballus
acetaldehyde + acycloNADH + H+
-
-
-
?
1.1.1.1
hexan-1-ol + NAD+
acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
738096
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
738096
Equus caballus
?
-
-
-
-
1.1.1.1
propan-1-ol + NAD+
acycloNAD+ i.e. NAD+-analogue, where the nicotinamide ribosyl moiety has been replaced by the nicotinamide (2-hydroxyethoxy)methyl moiety
738096
Equus caballus
propanal + acycloNADH + H+
-
-
-
?