Escherichia coli K-12 substr. MG1655 Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number:

Enzymes and Genes:
aldehyde-alcohol dehydrogenaseInferred from experiment: adhE
ethanol dehydrogenase / alcohol dehydrogenaseInferred from experiment: adhP

In Pathway: ethanol degradation I, mixed acid fermentation

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Direct generic reaction:
a primary alcohol + NAD+ ↔ an aldehyde + NADH + H+ (

Enzyme Commission Primary Name: alcohol dehydrogenase

Enzyme Commission Synonyms: aldehyde reductase, ADH, alcohol dehydrogenase (NAD), aliphatic alcohol dehydrogenase, ethanol dehydrogenase, NAD-dependent alcohol dehydrogenase, NAD-specific aromatic alcohol dehydrogenase, NADH-alcohol dehydrogenase, NADH-aldehyde dehydrogenase, primary alcohol dehydrogenase, yeast alcohol dehydrogenase

The final reaction in the fermentation pathway leading to ethanol.

Enzyme Commission Summary:
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.

Citations: [Jornvall77, THEORELL58]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reaction of [a primary alcohol + NAD+ ↔ an aldehyde + NADH + H+] (
i1: ethanol + NAD+ ↔ acetaldehyde + NADH + H+ (

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:


Jornvall77: Jornvall H (1977). "Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects." Eur J Biochem 72(3);443-52. PMID: 320001

THEORELL58: THEORELL H (1958). "Kinetics and equilibria in the liver alcohol dehydrogenase system." Adv Enzymol Relat Subj Biochem 20;31-49. PMID: 13605979

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by Pathway Tools version 19.5 (software by SRI International) on Tue Dec 1, 2015, biocyc11.