twitter

MetaCyc Reaction: 1.1.1.1

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

EC Number: 1.1.1.1

Enzymes and Genes:

Saccharomyces cerevisiae: alcohol dehydrogenase / S-hydroxymethyl-glutathione dehydrogenaseInferred from experiment: SFA1
alcohol dehydrogenase IInferred from experiment: ADH1
alcohol dehydrogenase IIInferred from experiment: ADH2
alcohol dehydrogenase IIIInferred from experiment: ADH3
alcohol dehydrogenase IVInferred from experiment: ADH4
alcohol dehydrogenase VInferred from experiment: ADH5

In Pathway: L-isoleucine degradation II

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

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

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.

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

Standard Gibbs Free Energy (ΔrG): 2.541809 kcal/molInferred by computational analysis [Latendresse13]

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: [Jornvall77a, THEORELL58]

Gene-Reaction Schematic

Expand/Contract the Schematic connections:

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:1.1.1.1, ENZYME:EC:1.1.1.1, IUBMB-ExplorEnz:EC:1.1.1.1


References

Jornvall77a: Jornvall H (1977). "Differences between alcohol dehydrogenases. Structural properties and evolutionary aspects." Eur J Biochem 72(3);443-52. PMID: 320001

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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 MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 20.0 (software by SRI International) on Fri May 6, 2016, BIOCYC14.