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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:

Corynebacterium glutamicum ATCC 13032: Zn2+-dependent alcohol dehydrogenaseInferred from experiment: adhA
Escherichia coli K-12 substr. MG1655: ethanol dehydrogenase / alcohol dehydrogenaseInferred from experiment: adhP
aldehyde-alcohol dehydrogenaseInferred from experiment: adhE
Mycobacterium tuberculosis H37Rv: alcohol dehydrogenase: adhE
Saccharomyces cerevisiae: alcohol dehydrogenase IInferred from experiment: ADH1
alcohol dehydrogenase IIInferred from experiment: ADH2
alcohol dehydrogenase IIIInferred from experiment: ADH3
alcohol dehydrogenase IVInferred from experiment: ADH4

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.

Instance reactions:
butanal + NADH + H+ → n-butanol + NAD+ (1.1.1.-)

n-propanol + NAD+ ↔ propanal + NADH + H+ (1.1.1.1)

ethanol + NAD+ ↔ acetaldehyde + NADH + H+ (1.1.1.1)

phytol + NAD+ → phytenal + NADH + H+ (1.1.1.1)

1-octanol + NAD+ = octanal + NADH + H+ (1.1.1.73)

1-hexanol + NAD+ ← hexanal + NADH + H+ (1.1.1.-)

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

Taxonomic Range: Fungi, Archaea, Viridiplantae, Metazoa, Bacteria

Standard Gibbs Free Energy (ΔrG in kcal/mol): 23.084045Inferred 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: [Jornvall77, THEORELL58]

Gene-Reaction Schematic

Gene-Reaction Schematic

Instance reactions of [a primary alcohol + NAD+ ↔ an aldehyde + NADH + H+] (1.1.1.1):
i1: butanal + NADH + H+ → n-butanol + NAD+ (1.1.1.-)

i2: n-propanol + NAD+ ↔ propanal + NADH + H+ (1.1.1.1)

i3: ethanol + NAD+ ↔ acetaldehyde + NADH + H+ (1.1.1.1)

i4: phytol + NAD+ → phytenal + NADH + H+ (1.1.1.1)

i5: 1-octanol + NAD+ = octanal + NADH + H+ (1.1.1.73)

i6: 1-hexanol + NAD+ ← hexanal + NADH + H+ (1.1.1.-)

Unification Links: KEGG:R07326, Rhea:10739

Relationship Links: BRENDA:EC:1.1.1.1, ENZYME:EC:1.1.1.1, IUBMB-ExplorEnz:EC:1.1.1.1, UniProt:RELATED-TO:O06012, UniProt:RELATED-TO:O45687, UniProt:RELATED-TO:O49053, UniProt:RELATED-TO:O49054, UniProt:RELATED-TO:O49058, UniProt:RELATED-TO:O49061, UniProt:RELATED-TO:O65459, UniProt:RELATED-TO:O74540, UniProt:RELATED-TO:O82791, UniProt:RELATED-TO:O94038, UniProt:RELATED-TO:P00325, UniProt:RELATED-TO:P00326, UniProt:RELATED-TO:P00327, UniProt:RELATED-TO:P00328, UniProt:RELATED-TO:P00329, UniProt:RELATED-TO:P00330, UniProt:RELATED-TO:P00331, UniProt:RELATED-TO:P00332, UniProt:RELATED-TO:P00333, UniProt:RELATED-TO:P00334, UniProt:RELATED-TO:P04707, UniProt:RELATED-TO:P05336, UniProt:RELATED-TO:P06525, UniProt:RELATED-TO:P06757, UniProt:RELATED-TO:P06758, UniProt:RELATED-TO:P07159, UniProt:RELATED-TO:P07160, UniProt:RELATED-TO:P07161, UniProt:RELATED-TO:P07162, UniProt:RELATED-TO:P07246, UniProt:RELATED-TO:P07327, UniProt:RELATED-TO:P07754, UniProt:RELATED-TO:P08319, UniProt:RELATED-TO:P08843, UniProt:RELATED-TO:P09369, UniProt:RELATED-TO:P09370, UniProt:RELATED-TO:P0A9Q7, UniProt:RELATED-TO:P10127, UniProt:RELATED-TO:P10807, UniProt:RELATED-TO:P10847, UniProt:RELATED-TO:P10848, UniProt:RELATED-TO:P11766, UniProt:RELATED-TO:P12311, UniProt:RELATED-TO:P12711, UniProt:RELATED-TO:P12854, UniProt:RELATED-TO:P12886, UniProt:RELATED-TO:P13603, UniProt:RELATED-TO:P14219, UniProt:RELATED-TO:P14673, UniProt:RELATED-TO:P14674, UniProt:RELATED-TO:P14675, UniProt:RELATED-TO:P14940, UniProt:RELATED-TO:P17648, UniProt:RELATED-TO:P18332, UniProt:RELATED-TO:P19631, UniProt:RELATED-TO:P19854, UniProt:RELATED-TO:P20306, UniProt:RELATED-TO:P20368, UniProt:RELATED-TO:P20369, UniProt:RELATED-TO:P21898, UniProt:RELATED-TO:P22245, UniProt:RELATED-TO:P22246, UniProt:RELATED-TO:P22797, UniProt:RELATED-TO:P23236, UniProt:RELATED-TO:P23237, UniProt:RELATED-TO:P23277, UniProt:RELATED-TO:P23278, UniProt:RELATED-TO:P23361, UniProt:RELATED-TO:P23991, UniProt:RELATED-TO:P25139, UniProt:RELATED-TO:P25141, UniProt:RELATED-TO:P25405, UniProt:RELATED-TO:P25406, UniProt:RELATED-TO:P25437, UniProt:RELATED-TO:P25988, UniProt:RELATED-TO:P26325, UniProt:RELATED-TO:P26719, UniProt:RELATED-TO:P28032, UniProt:RELATED-TO:P28332, UniProt:RELATED-TO:P28469, UniProt:RELATED-TO:P28474, UniProt:RELATED-TO:P30350, UniProt:RELATED-TO:P32771, UniProt:RELATED-TO:P33010, UniProt:RELATED-TO:P33744, UniProt:RELATED-TO:P37473, UniProt:RELATED-TO:P37686, UniProt:RELATED-TO:P38113, UniProt:RELATED-TO:P39462, UniProt:RELATED-TO:P40394, UniProt:RELATED-TO:P41680, UniProt:RELATED-TO:P41681, UniProt:RELATED-TO:P42327, UniProt:RELATED-TO:P42328, UniProt:RELATED-TO:P43067, UniProt:RELATED-TO:P44557, UniProt:RELATED-TO:P46415, UniProt:RELATED-TO:P48815, UniProt:RELATED-TO:P48977, UniProt:RELATED-TO:P49383, UniProt:RELATED-TO:P49384, UniProt:RELATED-TO:P49645, UniProt:RELATED-TO:P50381, UniProt:RELATED-TO:P51635, UniProt:RELATED-TO:P54202, UniProt:RELATED-TO:P73138, UniProt:RELATED-TO:P77316, UniProt:RELATED-TO:P78870, UniProt:RELATED-TO:P79896, UniProt:RELATED-TO:P80338, UniProt:RELATED-TO:P80360, UniProt:RELATED-TO:P80467, UniProt:RELATED-TO:P80512, UniProt:RELATED-TO:P81431, UniProt:RELATED-TO:P84328, UniProt:RELATED-TO:Q6LCE4, UniProt:RELATED-TO:Q7LZ46, UniProt:RELATED-TO:Q7LZI0, UniProt:RELATED-TO:Q7M1S7, UniProt:RELATED-TO:Q7M4Z9, UniProt:RELATED-TO:Q9CEN0, UniProt:RELATED-TO:Q9GN94, UniProt:RELATED-TO:Q9JRB0, UniProt:RELATED-TO:Q9JVR8, UniProt:RELATED-TO:Q9K0P0, UniProt:RELATED-TO:Q9P6C8, UniProt:RELATED-TO:Q9RI47, UniProt:RELATED-TO:Q9UAT1, UniProt:RELATED-TO:Q03384, UniProt:RELATED-TO:Q03505, UniProt:RELATED-TO:Q05847, UniProt:RELATED-TO:Q06099, UniProt:RELATED-TO:Q07288, UniProt:RELATED-TO:Q07321, UniProt:RELATED-TO:Q07588, UniProt:RELATED-TO:Q09009, UniProt:RELATED-TO:Q09010, UniProt:RELATED-TO:Q09669, UniProt:RELATED-TO:Q17334, UniProt:RELATED-TO:Q24641, UniProt:RELATED-TO:Q26653, UniProt:RELATED-TO:Q27595, UniProt:RELATED-TO:Q39782, UniProt:RELATED-TO:Q39783, UniProt:RELATED-TO:Q40249, UniProt:RELATED-TO:Q41241, UniProt:RELATED-TO:Q41242 ... [15 more not displayed]


References

Jornvall77: 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 19.5 (software by SRI International) on Fri Apr 29, 2016, biocyc13.