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Literature summary for 1.1.1.1 extracted from

  • LeBrun, L.A.; Park, D.H.; Ramaswamy, S.; Plapp, B.V.
    Participation of histidine-51 in catalysis by horse liver alcohol dehydrogenase (2004), Biochemistry, 43, 3014-3026.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
10 mg/ml purified double mutant H51Q/K228R in complex with NAD+ and 2,3- or 2,4-difluorobenzyl alcohol, in 50 mM ammonium N-[tris(hydroxymethyl)-methyl]-2-aminoethanesulfonate, pH 7.0, 5°C, 1 mM NAD+, 10 mM 2,3-difluorobenzyl alcohol or 2,4-difluorobenzyl alcohol, equilibrated against increasing concentrations of 2-methyl-2,4-pentanediole, crystal formation at 12% 2-methyl-2,4-pentanediole, X-ray diffraction structure determination and analysis Equus caballus

Protein Variants

Protein Variants Comment Organism
H51Q site-directed mutagenesis, shifting of pH dependency, increased activity at pH 8.0, decrease of the rate of isomerization of the enzyme-NAD+ complex, which becomes the limiting step for ethanol oxidation Equus caballus
H51Q/K228R site-directed mutagenesis, kinetic effects Equus caballus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information detailed kinetic mechanism, steady-state kinetics for wild-type and mutant enzymes, investigation of pH-dependency Equus caballus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ catalytic zinc ion Equus caballus

Organism

Organism UniProt Comment Textmining
Equus caballus P00327
-
-

Reaction

Reaction Comment Organism Reaction ID
a primary alcohol + NAD+ = an aldehyde + NADH + H+ reaction mechanism, His51 is involved, but not essential, in catalysis facilitating the deprotonation of the hydroxyl group of water or alcohol ligated to the catalytic zinc Equus caballus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Equus caballus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butanol + NAD+
-
Equus caballus n-butanal + NADH
-
?
ethanol + NAD+ isomerization of the enzyme-NAD+ complex is the rate-limiting step for acetaldehyde reduction by the wild-type enzyme Equus caballus acetaldehyde + NADH
-
r
n-propanol + NAD+
-
Equus caballus propanal + NADH
-
?

Synonyms

Synonyms Comment Organism
ADH
-
Equus caballus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Equus caballus

pH Range

pH Minimum pH Maximum Comment Organism
6 10
-
Equus caballus

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Equus caballus