Any feedback?
Information on EC 1.2.99.6 - carboxylate reductase
for references in articles please use BRENDA:EC1.2.99.6Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.2.99.6 carboxylate reductaseIUBMB Comments
A tungsten protein. Methyl viologen can act as acceptor. In the reverse direction, non-activated acids are reduced by reduced viologens to aldehydes, but not to the corresponding alcohols.
Specify your search results
Word Map
- 1.2.99.6
- aldose
- reductases
-
nadph-dependent
-
aldo-keto
- aflatoxin
-
1.1.1.2
- desulfovibrio
- akr1a1
- polyols
- d-glucuronate
- sorbinil
-
dihydrodiols
- gigas
-
afars
- dl-glyceraldehyde
-
alpha-hydroxysteroids
- furfural
-
molybdenum-containing
- 3-deoxyglucosone
-
phosphopantetheinylation
- ethoxyquin
-
high-km
-
trans-dihydrodiols
-
tungsten-containing
- gamma-hydroxybutyrate
- tolrestat
- propionaldehyde
- molybdopterin
- oltipraz
- sporobolomyces
- epalrestat
- pterins
- 5-hydroxymethylfurfural
- l-gulonate
- p-nitrobenzaldehyde
-
hexonate
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
aldehyde reductase, aldehyde oxidoreductase, carboxylic acid reductase, carboxylate reductase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde ferredoxin oxidoreductase
-
-
-
-
aldehyde oxidoreductase
-
-
-
-
aldehyde reductase
-
-
-
-
AOR
-
-
-
-
BV-AIDH
-
-
-
-
Carboxylic acid reductase
-
-
-
-
Carboxylic acid reductase/aldehyde reductase
-
-
-
-
Reductase, carboxylate
-
-
-
-
W-AOR
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
An aldehyde + acceptor + H2O = a carboxylate + reduced acceptor
bi uni uni bi mechanism
-
An aldehyde + acceptor + H2O = a carboxylate + reduced acceptor
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
KEGG
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
aldehyde:acceptor oxidoreductase
A tungsten protein. Methyl viologen can act as acceptor. In the reverse direction, non-activated acids are reduced by reduced viologens to aldehydes, but not to the corresponding alcohols.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
125008-36-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,4-Dimethoxy-5-hydroxy-benzaldehyde + carbamoyl methyl viologen
3,4-Dimethoxy-5-hydroxy-benzoate + reduced carbamoyl methyl viologen
-
-
-
-
?
3,5-Dimethoxy-4-hydroxy-benzaldehyde + carbamoyl methyl viologen
3,5-Dimethoxy-4-hydroxy-benzoate + reduced carbamoyl methyl viologen
-
-
-
-
?
3-Chlorobenzoate + reduced carbamoyl methyl viologen
3-Chlorobenzaldehyde + carbamoyl methyl viologen
3-Fluorobenzoate + reduced carbamoyl methyl viologen
3-Fluorobenzaldehyde + carbamoyl methyl viologen
3-Hydroxybenzoate + reduced carbamoyl methyl viologen
3-Hydroxybenzaldehyde + carbamoyl methyl viologen
3-Methoxybenzoate + reduced carbamoyl methyl viologen
3-Methoxybenzaldhyde + carbamoyl methyl viologen
3-Methylbenzoate + reduced carbamoyl methyl viologen
3-Methylbenzaldehyde + carbamoyl methyl viologen
4-(Hydroxymethyl)benzoate + reduced carbamoyl methyl viologen
4-(Hydroxymethyl)benzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
4-Chlorobenzoate + reduced carbamoyl methyl viologen
4-Chlorobenzaldehyde + carbamoyl methyl viologen
4-Fluorobenzoate + reduced carbamoyl methyl viologen
4-Fluorobenzaldehyde + carbamoyl methyl viologen
4-Hydroxy-3-methoxy-benzaldehyde + carbamoyl methyl viologen
4-Hydroxy-3-methoxy-benzoate + reduced carbamoyl methyl viologen
-
-
-
-
?
4-Hydroxybenzaldehyde + carbamoyl methyl viologen
4-Hydroxybenzoate + reduced carbamoyl methyl viologen
-
r
-
?
4-Hydroxybenzoate + reduced carbamoyl methyl viologen
4-Hydroxybenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
4-Methoxybenzaldehyde + benzyl viologen
4-Methoxybenzoate + reduced carbamoyl methyl viologen
4-Methoxybenzoate + reduced carbamoyl methyl viologen
4-Methoxybenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
4-Methylbenzoate + reduced carbamoyl methyl viologen
4-Methylbenzaldehyde + carbamoyl methyl viologen
5-Phenyl-2,4-pentadienate + reduced carbamoyl methyl viologen
? + carbamoyl methyl viologen
-
-
-
-
?
Acetaldehyde + 2,6-dichlorophenol-indophenol
acetate + reduced 2,6-dichlorophenol-indophenol
Acetaldehyde + 3-(4',5'-dimethylthiazol-2-yl)-2,4-diphenyltetrazolium bromide
acetate + reduced 3-(4',5'-dimethylthiazol-2-yl)-2,4-diphenyltetrazolium bromide
acetaldehyde + benzyl viologen
acetic acid + reduced benzyl viologen
-
-
-
-
?
Acetaldehyde + carbamoyl methyl viologen
acetate + reduced carbamoyl methyl viologen
-
r
-
?
acetaldehyde + methyl viologen + H2O
acetate + reduced methyl viologen
-
-
-
-
r
benzaldehyde + 2,6-dichlorophenol indophenol
benzoate + reduced 2,6-dichlorophenol indophenol
Megalodesulfovibrio gigas
-
-
-
-
?
benzaldehyde + benzyl viologen
benzoic acid + reduced benzyl viologen
-
96% of activity compared to acetaldehyde
-
-
?
Cinnamaldehyde + carbamoyl methyl viologen
Cinnamate + reduced carbamoyl methyl viologen
-
r
-
?
crotonaldehyde + benzyl viologen
crotonic acid + reduced benzyl viologen
-
47% of activity compared to acetaldehyde
-
-
?
Crotonaldehyde + benzyl viologen
E-2-Butenoate + reduced benzyl viologen
-
at less than 1% of the activity with benzyl viologen
-
-
?
Crotonaldehyde + ES-1 ferredoxin
Crotonate + reduced ES-1 ferredoxin
-
-
-
-
?
decylaldehyde + 2,6-dichlorophenol indophenol
decanoate + reduced 2,6-dichlorophenol indophenol
Megalodesulfovibrio gigas
-
-
-
-
?
DL-glyceraldehyde + benzyl viologen
alpha,beta-dihydroxypropionic acid + reduced benzyl viologen
-
9% of activity compared to acetaldehyde
-
-
?
formaldehyde + benzyl viologen
formic acid + reduced benzyl viologen
-
2% of activity compared to acetaldehyde
-
-
?
Furfural + benzyl viologen
2-Furancarboxylic acid + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 77% of the activity relative to acetaldehyde
-
-
?
Glutaraldehyde + benzyl viologen
Glutarate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 16% of the activity relative to acetaldehyde
-
-
?
glutaraldehyde + benzyl viologen
glutaric acid + reduced benzyl viologen
-
19% of activity compared to acetaldehyde
-
-
?
Glyceraldehyde + benzyl viologen
Glycerate + reduced benzyl viologen
-
-
-
-
?
Glyceraldehyde + methyl viologen
Glycerate + reduced methyl viologen
-
-
-
-
?
Glycolaldehyde + benzyl viologen
Glycolate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 23% of the activity relative to acetaldehyde
-
-
?
glyoxylate + benzyl viologen
oxalic acid + reduced benzyl viologen
-
6% of activity compared to acetaldehyde
-
-
?
Hexanal + benzyl viologen
Hexanoate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 6% of the activity relative to acetaldehyde
-
-
?
isovaleraldehyde + benzyl viologen
isopentanoic acid + reduced benzyl viologen
-
66% of activity compared to acetaldehyde
-
-
?
Methanal + carbamoyl methyl viologen
Formate + reduced methyl viologen
-
-
-
-
?
Methanal + methyl viologen
Formate + reduced carbamoyl methyl viologen
-
-
-
-
?
octanal + 2,6-dichlorophenol indophenol
octanoate + reduced 2,6-dichlorophenol indophenol
Megalodesulfovibrio gigas
-
-
-
-
?
Pentanal + benzyl viologen
Pentanoate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 9% of the activity relative to acetaldehyde
-
-
?
phenylacetaldehyde + benzyl viologen
phenylacetic acid + reduced benzyl viologen
-
20% of activity compared to acetaldehyde
-
-
?
Propanal + reduced 1,1',2,2'-tetramethylviologen
Propanoate + 1,1',2,2'-tetramethylviologen
-
-
-
-
?
propionaldehyde + benzyl viologen
propionic acid + reduced benzyl viologen
-
119% of activity compared to acetaldehyde
-
-
?
Pyridine 4-carboxylate + reduced carbamoyl methyl viologen
Pyridine 4-carboxaldehyde + carbamoyl methyl viologen
-
-
-
-
?
salicylaldehyde + benzyl viologen
salicylic acid + reduced benzyl viologen
-
4% of activity compared to acetaldehyde
-
-
?
terephthalaldehyde + carbamoyl methyl viologen
terephthalate + reduced carbamoyl methyl viologen
-
r
-
?
3-Chlorobenzoate + reduced carbamoyl methyl viologen
3-Chlorobenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
3-Chlorobenzoate + reduced carbamoyl methyl viologen
3-Chlorobenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
3-Fluorobenzoate + reduced carbamoyl methyl viologen
3-Fluorobenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
3-Fluorobenzoate + reduced carbamoyl methyl viologen
3-Fluorobenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
3-Hydroxybenzoate + reduced carbamoyl methyl viologen
3-Hydroxybenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
3-Hydroxybenzoate + reduced carbamoyl methyl viologen
3-Hydroxybenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
3-Methoxybenzoate + reduced carbamoyl methyl viologen
3-Methoxybenzaldhyde + carbamoyl methyl viologen
-
-
-
-
?
3-Methoxybenzoate + reduced carbamoyl methyl viologen
3-Methoxybenzaldhyde + carbamoyl methyl viologen
-
-
-
-
?
3-Methylbenzoate + reduced carbamoyl methyl viologen
3-Methylbenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
3-Methylbenzoate + reduced carbamoyl methyl viologen
3-Methylbenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
4-Chlorobenzoate + reduced carbamoyl methyl viologen
4-Chlorobenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
4-Chlorobenzoate + reduced carbamoyl methyl viologen
4-Chlorobenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
4-Fluorobenzoate + reduced carbamoyl methyl viologen
4-Fluorobenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
4-Fluorobenzoate + reduced carbamoyl methyl viologen
4-Fluorobenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
4-Methoxybenzaldehyde + benzyl viologen
4-Methoxybenzoate + reduced carbamoyl methyl viologen
Megalodesulfovibrio gigas
-
at 19% of the activity relative to acetaldehyde
-
-
?
4-Methoxybenzaldehyde + benzyl viologen
4-Methoxybenzoate + reduced carbamoyl methyl viologen
-
-
-
?
4-Methylbenzoate + reduced carbamoyl methyl viologen
4-Methylbenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
4-Methylbenzoate + reduced carbamoyl methyl viologen
4-Methylbenzaldehyde + carbamoyl methyl viologen
-
-
-
-
?
Acetaldehyde + 2,6-dichlorophenol-indophenol
acetate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
at 1.3% of the activity relative to benzyl viologen
-
-
?
Acetaldehyde + 2,6-dichlorophenol-indophenol
acetate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas NCIMB 9332
-
at 1.3% of the activity relative to benzyl viologen
-
-
?
Acetaldehyde + 3-(4',5'-dimethylthiazol-2-yl)-2,4-diphenyltetrazolium bromide
acetate + reduced 3-(4',5'-dimethylthiazol-2-yl)-2,4-diphenyltetrazolium bromide
Megalodesulfovibrio gigas
-
at 5% of the activity relative to benzyl viologen
-
-
?
Acetaldehyde + 3-(4',5'-dimethylthiazol-2-yl)-2,4-diphenyltetrazolium bromide
acetate + reduced 3-(4',5'-dimethylthiazol-2-yl)-2,4-diphenyltetrazolium bromide
Megalodesulfovibrio gigas NCIMB 9332
-
at 5% of the activity relative to benzyl viologen
-
-
?
Acetaldehyde + benzyl viologen
acetate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
-
-
-
?
Acetaldehyde + benzyl viologen
acetate + reduced benzyl viologen
Megalodesulfovibrio gigas NCIMB 9332
-
-
-
-
?
Acetaldehyde + benzyl viologen
acetate + reduced benzyl viologen
-
r
-
-
?
Acetaldehyde + benzyl viologen
acetate + reduced benzyl viologen
-
r
-
-
?
Acetaldehyde + methyl viologen
acetate + reduced methyl viologen
Megalodesulfovibrio gigas
-
at 19% of the activity relative to benzyl viologen
-
-
?
Acetaldehyde + methyl viologen
acetate + reduced methyl viologen
Megalodesulfovibrio gigas NCIMB 9332
-
at 19% of the activity relative to benzyl viologen
-
-
?
Acetaldehyde + methyl viologen
acetate + reduced methyl viologen
-
-
-
-
?
Benzaldehyde + benzyl viologen
Benzoate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 93% of the activity relative to acetaldehyde
-
-
?
Benzaldehyde + benzyl viologen
Benzoate + reduced benzyl viologen
Megalodesulfovibrio gigas NCIMB 9332
-
at 93% of the activity relative to acetaldehyde
-
-
?
Benzaldehyde + benzyl viologen
Benzoate + reduced benzyl viologen
-
-
-
-
?
Benzaldehyde + benzyl viologen
Benzoate + reduced benzyl viologen
-
-
-
-
?
Benzaldehyde + carbamoyl methyl viologen
Benzoate + reduced carbamoyl methyl viologen
-
-
-
-
?
Benzaldehyde + carbamoyl methyl viologen
Benzoate + reduced carbamoyl methyl viologen
-
only reverse reaction described
-
-
?
Benzaldehyde + carbamoyl methyl viologen
Benzoate + reduced carbamoyl methyl viologen
-
r
-
?
Butanal + NH2CO-methyl viologen
Butanoate + reduced NH2CO-methyl viologen
-
-
-
-
?
Butanal + NH2CO-methyl viologen
Butanoate + reduced NH2CO-methyl viologen
-
only reverse reaction described
-
-
?
Butanal + NH2CO-methyl viologen
Butanoate + reduced NH2CO-methyl viologen
-
-
-
-
?
Butyraldehyde + benzyl viologen
Butanoate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 16% of the activity relative to acetaldehyde
-
-
?
Butyraldehyde + benzyl viologen
Butanoate + reduced benzyl viologen
-
101% of activity compared to acetaldehyde
-
-
?
Crotonaldehyde + methyl viologen
Crotonate + reduced methyl viologen
-
-
-
-
?
Crotonaldehyde + methyl viologen
Crotonate + reduced methyl viologen
-
-
-
-
?
Indoleacetaldehyde + benzyl viologen
Indoleacetate + reduced benzyl viologen
-
-
-
-
?
Indoleacetaldehyde + benzyl viologen
Indoleacetate + reduced benzyl viologen
-
-
-
-
?
Isovaleraldehyde + benzyl viologen
Isovalerate + reduced benzyl viologen
-
-
-
-
?
Isovaleraldehyde + benzyl viologen
Isovalerate + reduced benzyl viologen
-
-
-
-
?
Isovaleraldehyde + benzyl viologen
Isovalerate + reduced benzyl viologen
-
-
-
-
?
Methanal + benzyl viologen
Formate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 16% of the activity relative to acetaldehyde
-
-
?
Phenylacetaldehyde + benzyl viologen
Phenylacetate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 31% of the activity relative to acetaldehyde
-
-
?
Phenylacetaldehyde + benzyl viologen
Phenylacetate + reduced benzyl viologen
-
-
-
-
?
Phenylacetaldehyde + benzyl viologen
Phenylacetate + reduced benzyl viologen
-
-
-
-
?
Phenylacetaldehyde + benzyl viologen
Phenylacetate + reduced benzyl viologen
-
-
-
-
?
Propanal + benzyl viologen
Propanoate + reduced benzyl viologen
-
only reverse reaction described
-
?
Propanal + benzyl viologen
Propanoate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 117% of the activity relative to acetaldehyde
-
-
?
Propanal + methyl viologen
Propanoate + reduced methyl viologen
-
only reverse reaction described
-
?
Propanal + methyl viologen
Propanoate + reduced methyl viologen
-
-
-
-
?
Propanal + NH2CO-methyl viologen
Propanoate + reduced carbamoyl methyl viologen
-
-
-
-
?
Propanal + NH2CO-methyl viologen
Propanoate + reduced carbamoyl methyl viologen
-
only reverse reaction described
-
?
Propanal + NH2CO-methyl viologen
Propanoate + reduced carbamoyl methyl viologen
-
r
-
-
?
Salicylaldehyde + benzyl viologen
Salicylate + reduced benzyl viologen
Megalodesulfovibrio gigas
-
at 14% of the activity relative to acetaldehyde
-
-
?
Salicylaldehyde + benzyl viologen
Salicylate + reduced benzyl viologen
-
-
-
-
?
additional information
?
-
-
in contast to the dimeric enzyme form the heptameric enzyme form also catalyzes the reversible reduction of the oxidized carbamoyl methyl viologen with NADPH
-
-
?
additional information
?
-
-
its physiological role is proposed as the oxidation of glyceraldehyde to glycerate in a unique, partially nonphosphorylated glycolytic pathway that generates acetyl-CoA from glucose without participation of nicotinamide nucleotides
-
-
?
additional information
?
-
-
the enzyme possibly functions to oxidize aldehydes generated during amino acid catabolism, it is also possible that the enzyme generates aldehydes from organic acids produced by fermentation
-
-
?
additional information
?
-
-
the enzyme possibly functions to oxidize aldehydes generated during amino acid catabolism, it is also possible that the enzyme generates aldehydes from organic acids produced by fermentation
-
-
?
additional information
?
-
-
the enzyme possibly functions to oxidize aldehydes generated during amino acid catabolism, it is also possible that the enzyme generates aldehydes from organic acids produced by fermentation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
its physiological role is proposed as the oxidation of glyceraldehyde to glycerate in a unique, partially nonphosphorylated glycolytic pathway that generates acetyl-CoA from glucose without participation of nicotinamide nucleotides
-
-
?
additional information
?
-
-
the enzyme possibly functions to oxidize aldehydes generated during amino acid catabolism, it is also possible that the enzyme generates aldehydes from organic acids produced by fermentation
-
-
?
additional information
?
-
-
the enzyme possibly functions to oxidize aldehydes generated during amino acid catabolism, it is also possible that the enzyme generates aldehydes from organic acids produced by fermentation
-
-
?
additional information
?
-
-
the enzyme possibly functions to oxidize aldehydes generated during amino acid catabolism, it is also possible that the enzyme generates aldehydes from organic acids produced by fermentation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
the heptameric enzyme form contains 1.7 mol of FAD per mol of enzyme, seems to be a component of the gamma-subunit
molybdopterin
-
the tungsten-containing enzyme is bound to the mononucleotide form of the molybdopterin cofactor
pterin
-
the dimeric enzyme form contains 0.8-1.1 mol of pterine per mol of enzyme
pterin
-
the heptameric enzyme form contains 2.5 mol of pterine per mol of enzyme
pterin
-
contains 1.6 mol of pterin-6-carboxylic acid per mol of enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Tungsten
Iron
-
the heptameric enzyme form contains 75-90 mol of iron per mol of enzyme
Iron
-
the dimeric enzyme form contains 25-33 mol of iron per mol of enzyme
Tungsten
Megalodesulfovibrio gigas
-
enzyme contains 0.68 gatom of tungsten per mol of subunit
Tungsten
-
the heptameric enzyme form contains 3.4 mol of tungsten per mol of enzyme
Tungsten
-
the dimeric form contains 0.8 mol of tungsten per mol of enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
K3Fe(CN)6
-
tungsten-containing enzyme and molybdenum-containing enzyme
CN-
-
inactivates tungsten-containing enzyme, molybdenum-containing enzyme is insensitive
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Direct enzyme assay evidence confirms aldehyde reductase function of Ydr541cp and Ygl039wp from Saccharomyces cerevisiae.
Astrocytoma
The role of aldehyde reductase AKR1A1 in the metabolism of gamma-hydroxybutyrate in 1321N1 human astrocytoma cells.
Carcinogenesis
A novel aldehyde reductase with activity towards a metabolite of aflatoxin B1 is expressed in rat liver during carcinogenesis and following the administration of an anti-oxidant.
Carcinogenesis
Glutathione-S-transferase, alcohol dehydrogenase and aldehyde reductase activities during diethylnitrosamine-carcinogenesis in rat liver.
Carcinogenesis
Transgenic expression of aflatoxin aldehyde reductase (AKR7A1) modulates aflatoxin B1 metabolism but not hepatic carcinogenesis in the rat.
Carcinoma
Increased resistance of tumor cells to daunorubicin after transfection of cDNAs coding for anthracycline inactivating enzymes.
Carcinoma, Hepatocellular
Glutathione-S-transferase, alcohol dehydrogenase and aldehyde reductase activities during diethylnitrosamine-carcinogenesis in rat liver.
Carcinoma, Hepatocellular
Metabolic activation of polycyclic aromatic hydrocarbon trans-dihydrodiols by ubiquitously expressed aldehyde reductase (AKR1A1).
Carcinoma, Hepatocellular
Role of aldehyde metabolizing enzymes in mediating effects of aldehyde products of lipid peroxidation in liver cells.
Carcinoma, Hepatocellular
Specific differences in gene expression profile revealed by cDNA microarray analysis of glutathione S-transferase placental form (GST-P) immunohistochemically positive rat liver foci and surrounding tissue.
Cataract
Lens aldehyde reductase and dehydrogenase, and their possible involvement in diabetes and cataract formation.
Colorectal Neoplasms
Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 in a region frequently altered in human tumour cells.
Diabetes Complications
Expression of human aldose and aldehyde reductases. Site-directed mutagenesis of a critical lysine 262.
Diabetes Complications
Molecular modelling and synthesis of spiroimidazolidine-2,4-diones with dual activities as hypoglycemic agents and selective inhibitors of aldose reductase.
Diabetes Complications
Reductive detoxification of acrolein as a potential role for aldehyde reductase (AKR1A) in mammals.
Diabetes Complications
Rhodanine-3-acetamide derivatives as aldose and aldehyde reductase inhibitors to treat diabetic complications: synthesis, biological evaluation, molecular docking and simulation studies.
Diabetes Complications
Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications.
Diabetes Mellitus
Coumarin-thiazole and -oxadiazole derivatives: Synthesis, bioactivity and docking studies for aldose/aldehyde reductase inhibitors.
Diabetic Neuropathies
X-ray structure of the V301L aldo-keto reductase 1B10 complexed with NADP(+) and the potent aldose reductase inhibitor fidarestat: Implications for inhibitor binding and selectivity.
Hepatitis
Induction of aldose reductase gene expression in LEC rats during the development of the hereditary hepatitis and hepatoma.
Hypernatremia
The role of polyols in cerebral cell volume regulation in hypernatremic and hyponatremic states.
Hyponatremia
The role of polyols in cerebral cell volume regulation in hypernatremic and hyponatremic states.
Infections
Genome sequence and transcriptome profiles of pathogenic fungus Paecilomyces penicillatus reveal its interactions with edible fungus Morchella importuna.
Laryngeal Neoplasms
Increased aldehyde reductase expression mediates acquired radioresistance of laryngeal cancer cells via modulating p53.
Leukemia, Myeloid
NADPH-dependent reductases and polyol formation in human leukemia cell lines.
Leukemia, Myeloid, Acute
[Induction of cell differentiation and development of new anticancer drugs]
Metabolic Diseases
Coumarin-thiazole and -oxadiazole derivatives: Synthesis, bioactivity and docking studies for aldose/aldehyde reductase inhibitors.
Neoplasms
Aflatoxin B1 aldehyde reductase (AFAR) genes cluster at 1p35-1p36.1 in a region frequently altered in human tumour cells.
Neoplasms
Differential protein expression in honeybee (Apis mellifera L.) larvae: underlying caste differentiation.
Neoplasms
Genetic variation of Aflatoxin B(1) aldehyde reductase genes (AFAR) in human tumour cells.
Neoplasms
In silico designing of novel inhibitors for triple inhibition of Aldose Reductase, Aldose Reductase like protein 1, and Aldehyde Reductase.