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Literature summary for 1.1.1.71 extracted from

  • Hirschberg, D.; Cederlund, E.; Crosas, B.; Jonsson, A.; Tryggvason, S.; Farres, J.; Pares, X.; Bergmann, T.; Jörnvall, H.
    N-terminal acetylation in a third protein family of vertebrate alcohol dehydrogenase/retinal reductase found through a proteomics approach in enzyme characterization (2001), Cell. Mol. Life Sci., 58, 1323-1326.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36500
-
1 * 36500, 2-D gel electrophoresis Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
a primary alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+ the enzyme is an aldo-keto reductase Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
alimentary canal digestive tract Gallus gallus
-

Subunits

Subunits Comment Organism
monomer 1 * 36500, 2-D gel electrophoresis Gallus gallus

Synonyms

Synonyms Comment Organism
ADH
-
Gallus gallus
retinol-active alcohol dehydrogenase
-
Gallus gallus