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Literature summary 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)

EC Number Crystallization (Comment) Organism
1.1.1.1 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

EC Number Protein Variants Comment Organism
1.1.1.1 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
1.1.1.1 H51Q/K228R site-directed mutagenesis, kinetic effects Equus caballus

KM Value [mM]

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

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Equus caballus P00327
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.1 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
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
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 butanol + NAD+
-
 Equus caballus n-butanal + NADH
-
 ?
1.1.1.1 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
1.1.1.1 n-propanol + NAD+
-
 Equus caballus propanal + NADH
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 ADH
-
 Equus caballus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.1 8
-
 assay at Equus caballus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.1 6 10
-
 Equus caballus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 NAD+
-
 Equus caballus