EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
1.2.99.6 | 11937 |
Carboxylic acid reductase: a new tungsten enzyme catalyses the reduction of non-activated carboxylic acids to aldehydes |
Eur. J. Biochem. |
184 |
89-96 |
1989 |
Moorella thermoacetica |
2550230 |
1.2.99.6 | 11940 |
Further characterization of two different, reversible aldehyde oxidoreductases from Clostridium formicoaceticum, one containing tungsten and the other molybdenum |
Arch. Microbiol. |
162 |
303-309 |
1994 |
Clostridium formicaceticum |
- |
1.2.99.6 | 654439 |
Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles |
Biochem. Biophys. Res. Commun. |
308 |
73-78 |
2003 |
Megalodesulfovibrio gigas |
12890482 |
1.2.99.6 | 11939 |
Pterin cofactor, substrate specificity, and observations on the kinetics of the reversible tungsten-containing aldehyde oxidoreductase from Clostridium thermoaceticum |
Arch. Microbiol. |
164 |
110-118 |
1995 |
Moorella thermoacetica |
- |
1.2.99.6 | 11936 |
Purification and characterization of a benzylviologen-linked tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas |
J. Bacteriol. |
177 |
6195-6200 |
1995 |
Megalodesulfovibrio gigas |
7592385 |
1.2.99.6 | 11936 |
Purification and characterization of a benzylviologen-linked tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas |
J. Bacteriol. |
177 |
6195-6200 |
1995 |
Megalodesulfovibrio gigas NCIMB 9332 |
7592385 |
1.2.99.6 | 11943 |
Purification and some properties of the tungsten-containing carboxylic acid reductase from Clostridium formicoaceticum |
Biol. Chem. Hoppe-Seyler |
372 |
999-1005 |
1991 |
Clostridium formicaceticum |
1793519 |
1.2.99.6 | 11935 |
Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archaeon Thermococcus strain ES-1 |
J. Bacteriol. |
177 |
4757-4764 |
1995 |
Thermococcus sp. |
7642503 |
1.2.99.6 | 11935 |
Purification, characterization, and metabolic function of tungsten-containing aldehyde ferredoxin oxidoreductase from the hyperthermophilic and proteolytic archaeon Thermococcus strain ES-1 |
J. Bacteriol. |
177 |
4757-4764 |
1995 |
Thermococcus sp. ES-1 |
7642503 |
1.2.99.6 | 11938 |
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 |
14208-14216 |
1991 |
Pyrococcus furiosus |
1907273 |