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Literature summary for 1.1.1.1 extracted from

  • Jelski, W.; Szmitkowski, M.
    Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) in the cancer diseases (2008), Clin. Chim. Acta, 395, 1-5.
    View publication on PubMed
Search for more literature for 1.1.1.1

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Homo sapiens 5829
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
colorectum the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy colorectum Homo sapiens
-
cornea isozyme ADH4 Homo sapiens
-
esophagus isozyme ADH4, the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy esophagus Homo sapiens
-
kidney isozyme ADH1 Homo sapiens
-
liver the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy liver Homo sapiens
-
lung isozyme ADH1 Homo sapiens
-
serum
-
 Homo sapiens
-
skin
-
 Homo sapiens
-
stomach isozymes ADH5 and ADH4, the total alcohol dehydrogenase activity is significantly higher in cancer tissues than in healthy stomach Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2E)-4-hydroxynon-2-enal + NADH + H+ substrate of isozyme ADH4 Homo sapiens (2E)-non-2-ene-1,4-diol + NAD+
-
 r
ethanol + NAD+
-
 Homo sapiens acetaldehyde + NADH + H+
-
 r
p-nitrobenzaldehyde + NADH + H+ substrate of isozyme ADH4 Homo sapiens p-nitrobenzyl alcohol + NAD+
-
 r
retinal + NADH + H+ substrate of isozyme ADH4 Homo sapiens retinol + NAD+
-
 r

Subunits

Subunits Comment Organism
dimer
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
ADH
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Homo sapiens