1.2.99.6: carboxylate reductase

This is an abbreviated version!
For detailed information about carboxylate reductase, go to the full flat file.

Word Map on EC 1.2.99.6

Reaction

an aldehyde
+
acceptor
+
H2O
=
a carboxylate
+
reduced acceptor

Synonyms

aldehyde ferredoxin oxidoreductase, aldehyde oxidoreductase, aldehyde reductase, AOR, BV-AIDH, Carboxylic acid reductase, Carboxylic acid reductase/aldehyde reductase, Reductase, carboxylate, W-AOR

ECTree

     1 Oxidoreductases
         1.2 Acting on the aldehyde or oxo group of donors
             1.2.99 With unknown physiological acceptors
                1.2.99.6 carboxylate reductase

Reference

Reference on EC 1.2.99.6 - carboxylate reductase

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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heider, J.; Ma, K.; Adams, M.W.W.
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., Thermococcus sp. ES-1
Manually annotated by BRENDA team
Hensgens, C.M.H.; Hagen, W.R.; Hansen, T.A.
Purification and characterization of a benzylviologen-linked tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas
J. Bacteriol.
177
6195-6200
1995
Desulfovibrio gigas, Desulfovibrio gigas NCIMB 9332
Manually annotated by BRENDA team
White, H.; Strobl, G.; Feicht, R.; Simon, H.
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
Manually annotated by BRENDA team
Mukund, S.; Adams, M.W.W.
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
Manually annotated by BRENDA team
Huber, C.; Skopan, H.; Feicht, R.; White, H.; Simon, H.
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
-
Manually annotated by BRENDA team
Huber, C.; Caldeira, J.; Jongejan, J.A.; Simon, H.
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
-
Manually annotated by BRENDA team
White, H.; Simon, H.
The role of tungstate and/or molybdate in the formation of aldehyde oxidoreductase in Clostridium thermoaceticum and other acetogens, immunological distances of such enzymes
Arch. Microbiol.
158
81-84
1992
Moorella thermoacetica, no activity in Butyribacterium methylotrophicum, no activity in Clostridium aceticum, no activity in Eubacterium limosum
Manually annotated by BRENDA team
Strobl, G.; Feicht, R.; White, H.; Lottspeich, F.; Simon, H.
The tungsten-containing aldehyde oxidoreductase from Clostridium thermoaceticum and its complex with a viologen-accepting NADPH oxidoreductase
Biol. Chem. Hoppe-Seyler
373
123-132
1992
Moorella thermoacetica
Manually annotated by BRENDA team
White, H.; Feicht, R.; Huber, C.; Lottspeich, F.; Simon, H.
Purification and some properties of the tungsten-containing carboxylic acid reductase from Clostridium formicoaceticum
Biol. Chem. Hoppe-Seyler
372
999-1005
1991
Clostridium formicaceticum
Manually annotated by BRENDA team
Andrade, S.L.A.; Brondino, C.D.; Kamenskaya, E.O.; Levashov, A.V.; Moura, J.J.G.
Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles
Biochem. Biophys. Res. Commun.
308
73-78
2003
Desulfovibrio gigas
Manually annotated by BRENDA team
Rauh, D.; Graentzdoerffer, A.; Granderath, K.; Andreesen, J.R.; Pich, A.
Tungsten-containing aldehyde oxidoreductase of Eubacterium acidaminophilum. Isolation, characterization and molecular analysis
Eur. J. Biochem.
271
212-219
2004
Peptoclostridium acidaminophilum
Manually annotated by BRENDA team