Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 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
ethanol dehydrogenase / alcohol dehydrogenase Inferred 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 reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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, 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.

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

Summary:
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: [Jornvall77a, THEORELL58]

Gene-Reaction Schematic: ?

Instance reaction of [a primary alcohol + NAD+ ↔ an aldehyde + NADH + H+] (1.1.1.1):
i1: ethanol + NAD+ ↔ acetaldehyde + NADH + H+ (1.1.1.1)

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

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 SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, biocyc13.