Metabolic Modeling Tutorial
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BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 1.1.1.1

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.1.1.1

Enzymes and Genes:
aldehyde-alcohol dehydrogenase Inferred from experiment : adhE ( Escherichia coli K-12 substr. MG1655 )
ethanol dehydrogenase / alcohol dehydrogenase Inferred from experiment : adhP ( Escherichia coli K-12 substr. MG1655 )
alcohol dehydrogenase IV Inferred from experiment : ADH4 ( Saccharomyces cerevisiae )
alcohol dehydrogenase III Inferred from experiment : ADH3 ( Saccharomyces cerevisiae )
alcohol dehydrogenase II Inferred from experiment : ADH2 ( Saccharomyces cerevisiae )
alcohol dehydrogenase I Inferred from experiment : ADH1 ( Saccharomyces cerevisiae )
alcohol dehydrogenase : adhE ( Mycobacterium tuberculosis H37Rv )

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

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

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

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

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

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

Standard Gibbs Free Energy (ΔrG in kcal/mol): 23.084045 Inferred 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: ?

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

i2: ethanol + NAD+ ↔ acetaldehyde + NADH + H+ (1.1.1.1)

i3: phytol + NAD+ → phytenal + NADH + H+ (1.1.1.1)

i4: n-propanol + NAD+ ↔ propanal + NADH + H+ (1.1.1.1)

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

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 SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, BIOCYC14A.