|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 184.108.40.206
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: aldehyde ferredoxin oxidoreductase
Enzyme Commission Synonyms: AOR
Taxonomic Range: Archaea
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -13.707764 [Latendresse13]
Enzyme Commission Summary:
This is an oxygen-sensitive enzyme that contains tungsten-molybdopterin and iron-sulfur clusters. Catalyses the oxidation of aldehydes (including crotonaldehyde, acetaldehyde, formaldehyde and glyceraldehyde) to their corresponding acids. However, it does not oxidize glyceraldehyde 3-phosphate [see EC 220.127.116.11, glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)]. Can use ferredoxin or methyl viologen but not NAD(P)+ as electron acceptor.
Unification Links: KEGG:R07158
Johnson93a: Johnson JL, Rajagopalan KV, Mukund S, Adams MW (1993). "Identification of molybdopterin as the organic component of the tungsten cofactor in four enzymes from hyperthermophilic Archaea." J Biol Chem 268(7);4848-52. PMID: 8444863
Mukund91: Mukund S, Adams MW (1991). "The novel tungsten-iron-sulfur protein of the hyperthermophilic archaebacterium, Pyrococcus furiosus, is an aldehyde ferredoxin oxidoreductase. Evidence for its participation in a unique glycolytic pathway." J Biol Chem 266(22);14208-16. PMID: 1907273
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