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Literature summary for 1.1.1.1 extracted from

  • Dahl, K.H.; Eklund, H.; McKinley-McKee, J.S.
    Enantioselective affinity labelling of horse liver alcohol dehydrogenase. Correlation of inactivation kinetics with the three-dimensional structure of the enzyme (1983), Biochem. J., 211, 391-396.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
S-2-Chloro-3-(imidazol-5-yl)propionate inactivation at pH 8.2, R-2-chloro-3-(imidazol-5-yl)propionate has no effect Equus caballus

Organism

Organism UniProt Comment Textmining
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.
11-cis-retinal + NADH + H+
-
 Equus caballus 11-cis-retinol + NAD+
-
 ?
13-cis-retinal + NADH + H+
-
 Equus caballus 13-cis-retinol + NAD+
-
 ?

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Equus caballus
NADH
-
 Equus caballus