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Information on EC 1.2.1.3 - aldehyde dehydrogenase (NAD+) and Organism(s) Rattus norvegicus and UniProt Accession P11884
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1.2.1.3 aldehyde dehydrogenase (NAD+)IUBMB Comments
Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
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Word Map
- 1.2.1.3
-
aldhs
-
retinoic
- metastasis
-
self-renewal
- isozymes
-
stem-like
-
smoke
- esophageal
-
drinker
-
nanog
-
flush
- myocardial
-
east
- retinaldehyde
-
tumorigenic
-
clinicopathological
-
case-control
-
smoking
- colorectal
-
epithelial-mesenchymal
- cyp2e1
-
chemoresistance
-
spheroid
-
alcohol-induced
- disulfiram
- mesenchymal
-
alcohol-related
-
sphere
-
detoxify
-
habit
- nitroglycerin
-
cell-like
- 4-hydroxy-2-nonenal
-
tumor-initiating
- trinitrate
-
mammosphere
- keratocytes
-
csc-like
-
sphere-forming
- cyanamide
-
aerodigestive
-
non-drinkers
- epcam
-
glyceryl
-
alcohol-dependent
-
tumorsphere
- chloral
- analysis
-
dehydrogenase-1
- synthesis
-
low-km
- medicine
- ichthyosis
The taxonomic range for the selected organisms is: Rattus norvegicus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
aldh2, aldh1, aldh1a1, aldehyde dehydrogenase 2, aldh1a3, aldh3a1, aldehyde dehydrogenase 1, aldh1a2, mitochondrial aldehyde dehydrogenase, aldehyde dehydrogenase-2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALDH2
AHD-M1
-
-
-
-
ALDDH
-
-
-
-
Aldehyde dehydrogenase [NAD+]
-
-
-
-
Aldehyde dehydrogenase, cytosolic
-
-
-
-
Aldehyde dehydrogenase, microsomal
-
-
-
-
aldehyde:NAD+ oxidoreductase
-
-
-
-
ALDH-E1
-
-
-
-
ALDH-E2
-
-
-
-
ALDH1
ALDH1-NL
-
-
-
-
ALDHI
-
-
-
-
ALDHX
-
-
-
-
ALHDII
-
-
-
-
Allergen Alt a 10
-
-
-
-
Brassica turgor-responsive/drought-induced gene 26 protein
-
-
-
-
Btg-26
-
-
-
-
CoA-independent aldehyde dehydrogenase
-
-
-
-
ETA-crystallin
-
-
-
-
gamma-aminobutyraldehyde dehydrogenase
-
-
-
-
K(+)-ACDH
-
-
-
-
K(+)-activated acetaldehyde dehydrogenase
-
-
-
-
m-methylbenzaldehyde dehydrogenase
-
-
-
-
Matured fruit 60 kDa protein
-
-
-
-
MF-60
-
-
-
-
Mg(2+)-ACDH
-
-
-
-
Mg(2+)-activated acetaldehyde dehydrogenase
-
-
-
-
NAD+-linked aldehyde dehydrogenase
-
-
-
-
NAD-aldehyde dehydrogenase
-
-
-
-
NAD-dependent 4-hydroxynonenal dehydrogenase
-
-
-
-
NAD-dependent aldehyde dehydrogenase
-
-
-
-
NAD-linked aldehyde dehydrogenase
-
-
-
-
Non-lens ALDH1
-
-
-
-
P51
-
-
-
-
PM-ALDH9
-
-
-
-
propionaldehyde dehydrogenase
-
-
-
-
R-aminobutyraldehyde dehydrogenase
-
-
-
-
RALDH
-
-
-
-
RALDH(II)
-
-
-
-
RalDH1
-
-
-
-
Retinal dehydrogenase
-
-
-
-
Turgor-responsive protein 26G
-
-
-
-
ALDH1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
Arginine and proline metabolism, Ascorbate and aldarate metabolism, beta-Alanine metabolism, Biosynthesis of secondary metabolites, Chloroalkane and chloroalkene degradation, Fatty acid degradation, Glycerolipid metabolism, Glycolysis / Gluconeogenesis, Histidine metabolism, Insect hormone biosynthesis, Limonene and pinene degradation, Lysine degradation, Microbial metabolism in diverse environments, Pantothenate and CoA biosynthesis, Pyruvate metabolism, Tryptophan metabolism, Valine, leucine and isoleucine degradation
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-, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
aldehyde:NAD+ oxidoreductase
Wide specificity, including oxidation of D-glucuronolactone to D-glucarate.
CAS REGISTRY NUMBER
COMMENTARY
9028-86-8
-
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
(R)-trans-4-hydroxy-2-nonenal + NAD+ + H2O
(2E,4R)-4-hydroxynon-2-enoic acid + NADH + H+
-
-
-
?
(S)-trans-4-hydroxy-2-nonenal + NAD+ + H2O
(2E,4S)-4-hydroxynon-2-enoic acid + NADH + H+
-
-
-
?
(2E)-4-hydroxy-2-nonenal + NAD+ + H2O
(2E)-4-hydroxy-2-nonenoic acid + NADH + H+
-
-
-
-
?
(R)-trans-4-hydroxy-2-nonenal + NAD+ + H2O
(2E,4R)-4-hydroxynon-2-enoic acid + NADH + H+
ALDH5A enantioselectively oxidizes (R)-trans-4-hydroxy-2-nonenal
-
-
?
(S)-trans-4-hydroxy-2-nonenal + NAD+ + H2O
(2E,4S)-4-hydroxynon-2-enoic acid + NADH + H+
-
-
-
?
3,4-dihydroxymandelic aldehyde + NAD+ + H2O
3,4-dihydroxymandelate + NADH
-
-
-
-
?
3,4-dihydroxyphenyl acetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetate + NADH + H+
-
-
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetic acid + NADH + H+
-
-
-
-
?
5-hydroxyindol acetaldehyde + NAD+ + H2O
5-hydroxyindol acetate + NADH + H+
-
-
-
-
?
7-methoxy-1-naphthaldehyde + NAD+ + H2O
7-methoxy-1-naphthoic acid + NADH + H+
-
-
-
-
?
chloroacetaldehyde + NAD+ + H2O
chloroacetate + NADH + H+
-
activity is twice as fast as with acetaldehyde, native enzyme and mutant enzyme E487K
-
-
?
hexanal + NAD+ + H2O
hexanoate + NADH + H+
-
-
-
-
?
p-(dimethylamino)cinnamaldehyde + NAD+ + H2O
p-(dimethylamino)cinnamate + NADH
-
-
-
-
?
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
-
esterase activity of the various isoenzymes is less than 7% of the activity with propanal and NAD+
-
-
?
phenylacetaldehyde + NAD+ + H2O
phenylacetate + NADH + H+
-
-
-
-
?
propanal + 3-acetylpyridine-NAD+ + H2O
propionate + 3-acetylpyridine-NADH
-
-
-
-
?
propanal + NAD+ + H2O
propionate + NADH
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
rats with an mutated allele for aldehyde dehydrogenase (ALDH2-2) show a low alcohol consumption phenotype. Homozygous ALDH2-2 rats derived from high-drinker F0 females showed a remarkly higher ethanol consumption than homozygous animals derived from low-drinker females. Mitochondria of F2 rats derived from high alcohol-consuming females were more active in oxidizing substrates that generate NADH for complex I
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
-
348682, 348690, 348695, 348700, 348707, 348715, 348717, 348791, 692281, 692337, 692623, 695139, 711651
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
mutations in Aldh2 strongly segregate with the phenotypes of low and high alcohol consumption and with kinetic differences in ALDH2, suggesting that pharmacogenetic differences affect voluntary alcohol consumption. Bases mutated in the coding region suggest that aldh2(2) in low drinkers is ancestral to the coding changes of either aldh2(1) or aldh2(3), which segregate with higher ethanol consumption
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
-
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
-
promotion-associated enzyme, no activity with phenobarbital-inducible enzyme
-
-
?
additional information
?
-
-
the microsomal membrane-bound enzyme is expected to catalyze the oxidation of such water-insoluble aldehydes produced on the surface of the microsomal membrane. The enzyme may also be involved in the conversion of fatty acids to alpha,omega-dicarboxylic acids
-
-
?
additional information
?
-
-
the majority of the vascular ALDH2 is present in the cytoplasm, suggesting that mitochondrial biotransformation of glyceryl trinitrate by ALDH2 plays a minor role in the overall vascular biotransformation
-
-
?
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
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
rats with an mutated allele for aldehyde dehydrogenase (ALDH2-2) show a low alcohol consumption phenotype. Homozygous ALDH2-2 rats derived from high-drinker F0 females showed a remarkly higher ethanol consumption than homozygous animals derived from low-drinker females. Mitochondria of F2 rats derived from high alcohol-consuming females were more active in oxidizing substrates that generate NADH for complex I
-
-
?
3,4-dihydroxyphenylacetaldehyde + NAD+ + H2O
3,4-dihydroxyphenylacetic acid + NADH + H+
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
-
mutations in Aldh2 strongly segregate with the phenotypes of low and high alcohol consumption and with kinetic differences in ALDH2, suggesting that pharmacogenetic differences affect voluntary alcohol consumption. Bases mutated in the coding region suggest that aldh2(2) in low drinkers is ancestral to the coding changes of either aldh2(1) or aldh2(3), which segregate with higher ethanol consumption
-
-
?
additional information
?
-
-
the microsomal membrane-bound enzyme is expected to catalyze the oxidation of such water-insoluble aldehydes produced on the surface of the microsomal membrane. The enzyme may also be involved in the conversion of fatty acids to alpha,omega-dicarboxylic acids
-
-
?
additional information
?
-
-
the majority of the vascular ALDH2 is present in the cytoplasm, suggesting that mitochondrial biotransformation of glyceryl trinitrate by ALDH2 plays a minor role in the overall vascular biotransformation
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
-
-
348680, 348682, 348690, 348691, 348695, 348700, 348707, 348715, 348716, 348717, 656901, 677208, 692281, 692337, 692623, 695139, 711651, 713089, 740883
additional information
-
NADP+: promotion-associated enzyme shows 1% of the activity with NAD+, phenobarbital-associated enzyme shows no activity
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+ ions stimulate the enantioselective oxidation of (R)-trans-4-hydroxy-2-nonenal by ALDH2 while suppressing (S)-trans-4-hydroxy-2-nonenal oxidation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
c-Jun N-terminal protein kinase
incubation with catalytically active JNK leads to significant inhibition of ALDH2 activity. CCl4 exposure activates JNK which translocates to mitochondria and phosphorylates ALDH2 contributing to inhibition of ALDH2 activity
-
Chloral hydrate
-
inhibition of isoenzyme I and II from mitochondria and isoenzyme II from microsomes, no inhibition of isoenzyme I from microsomes
ethanol
-
chronic or binge ethanol-exposure significantly decreases ALDH1 activity via S-nitrosylation, activity is restored by addition of dithiothreitol, ALDH1 activity (using 0.015 mM propionaldehyde as a substrate) is significantly inhibited (by 61%) in chronically ethanol-fed rats
Disulfiram
-
inhibits activity of mitochondrial isoenzyme I with NAD+ and activity of isoenzyme I and II from microsomes and mitochondria with NADP+
Mg2+
Mg2+ ions suppresses (R)-trans-4-hydroxy-2-nonenal oxidation by ALDH5A to a greater extent than that of (S)-trans-4-hydroxy-2-nonenal
p-hydroxymercuribenzoate
-
0.05 mM, potent inhibition of isoenzyme I from microsomes and mitochondria, isoenzyme II from microsomes and mitochondria is less sensitive
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
(R)-trans-4-hydroxy-2-nonenal
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.0007
(S)-trans-4-hydroxy-2-nonenal
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.0004
acetaldehyde
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.023
(3,4-dihydroxyphenyl)(hydroxy)acetaldehyde
-
membrane-bound isoenzyme ALDH
5.8
acetaldehyde
ALDH5A, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.039
(R)-trans-4-hydroxy-2-nonenal
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.04
(S)-trans-4-hydroxy-2-nonenal
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
0.26
acetaldehyde
ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
3.5
acetaldehyde
ALDH5A, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.8
-
microsomal isoenzyme I and II and mitochondrial isoenzymes with NADP+
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
low expression of ALDH3A2 at the beginning development and high and constant expression during development
-
-
-
-
highest expression of ALDH2 at the beginning and the end of development
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
inhibition of ALDH2 leads to accumulation of cytotoxic 4-hydroxynonenal and malondialdehyde, which can cause cell death through activation of c-Jun N-terminal protein kinase and/or p38 kinase
malfunction
-
ALDH2 inhibition suppresses cocaine self-administration and seeking behavior and prevents cocaine- or cue-induced reinstatement in a rat model of cocaine relapse-like behavior
physiological function
-
ALDH-2 plays a major role in nitroglycerin biotransformation
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ALDH2_RAT
519
0
56488
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
250000
-
mitochondrial isoenzyme II, microsomal isoenzyme I and II, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
CCl4 exposure activates JNK, which translocates to mitochondria and phosphorylates ALDH2
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S74A
-
half-life of the mutant enzyme at 50°C is 1 min compared to the half-life of the native enzyme of 1 min. Mutation diminishes NAD+ binding, affecting both the on and the off rates, as well as the rate-limiting step. About 100fold higher Km-value for NAD+
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
55
50
-
half-life of mutant enzyme S74A is 1 min, half-life of native enzyme is 4 min
55
-
30 min, 20% loss of activity of diluted solution, 70% loss of activity of concentrated preparations
55
-
5 min, microsomal isoenzymes and mitochondrial isoenzyme I, more than 90% loss of activity. Mitochondrial isoenzyme II retains 20% of its original activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, phosphate buffer pH 7.4, containing 4 mM dithiothreitol or 10 mM 2-mercaptoethanol, stable for 8-10 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme from promotion phase of hepatocarcinogenesis and phenobarbital-inducible enzyme
-
membrane-bound ALDH, ALDH-I: soluble high Km ALDH, and ALDH-II: low Km ALDH
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ALDH activity in the cytoplasmic fraction of the liver remains practically unchanged during cold injury (dry ice, -63°)
-
cold injury (dry ice, -63°) is followed by a significant decrease in specific activity of ALDH in rat liver mitochondria (by 24% compared to intact animals)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
glyceryl trinitrate is used in the treatment of angina pectoris and cardiac failure, but the rapid onset of glyceryl trinitrate tolerance limits its clinical utility.The majority of the vascular ALDH2 is present in the cytoplasm, suggesting that mitochondrial biotransformation of glyceryl trinitrate by ALDH2 plays a minor role in the overall vascular biotransformation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lindahl, R.; Evces, S.
Rat liver aldehyde dehydrogenase. II. Isolation and characterization of four inducible isozymes
J. Biol. Chem.
259
11991-11996
1984
Rattus norvegicus
Siew, C.; Deitrich, R.A.
Localization and characteristics of rat liver mitochondrial aldehyde dehydrogenases
Arch. Biochem. Biophys.
176
638-649
1976
Rattus norvegicus
Farres, J.; Wang, X.; Takahashi, K.; Cunningham, S.J.; Wang, T.T.; Weiner, H.
Effects of changing glutamate 487 to lysine in rat and human liver mitochondrial aldehyde dehydrogenase. A model to study human (Oriental type) class 2 aldehyde dehydrogenase
J. Biol. Chem.
269
13854-13860
1994
Homo sapiens, Rattus norvegicus
Martini, R.; Murray, M.
Characterization of the in vivo inhibition of rat hepatic microsomal aldehyde dehydrogenase activity by metyrapone
Biochem. Pharmacol.
51
1187-1193
1996
Rattus norvegicus
Rout, U.K.; Weiner, H.
Involvement of Serine 74 in the Enzyme-Coenzyme Interaction of Rat Liver Mitochondrial Aldehyde Dehydrogenase
Biochemistry
33
8955-8961
1994
Rattus norvegicus
Poole, R.C.; Halestrap, A.P.
Purification of aldehyde dehydrogenase from rat liver mitochondria by alpha-cyanocinnamate affinity chromatography
Biochem. J.
259
105-110
1989
Rattus norvegicus
Bedino, S.; Testore, G.; Obert, F.
Initial characterization of aldehyde dehydrogenase from rat testis cytosol
Biol. Chem. Hoppe-Seyler
371
95-101
1990
Rattus norvegicus
Han, I.O.; Joo, C.N.
Purification and characterization of the rat liver mitochondrial aldehyde dehydrogenase
Hanguk Saenghwahakhoe Chi
24
353-360
1991
Rattus norvegicus
-
Nakayasu, H.; Mihara, K.; Sato, R.
Purification and properties of a membrane-bound aldehyde dehydrogenase from rat liver microsomes
Biochem. Biophys. Res. Commun.
83
697-703
1978
Rattus norvegicus
Koivula, T.; Koivusalo, M.
Partial purification and properties of a phenobarbital-induced aldehyde dehydrogenase of rat liver
Biochim. Biophys. Acta
410
1-11
1975
Rattus norvegicus
Lindahl, R.; Evces, S.
Rat liver aldehyde dehydrogenase. I. Isolation and characterization of four high Km normal liver isozymes
J. Biol. Chem.
259
11986-11990
1984
Rattus norvegicus
diFabio, J.; Ji, Y.; Vasiliou, V.; Thatcher, G.R.; Bennett, B.M.
Role of mitochondrial aldehyde dehydrogenase in nitrate tolerance
Mol. Pharmacol.
64
1109-1116
2003
Rattus norvegicus
Sapag, A.; Tampier, L.; Valle-Prieto, A.; Quintanilla, M.E.; Moncada, C.; Israel, Y.
Mutations in mitochondrial aldehyde dehydrogenase (ALDH2) change cofactor affinity and segregate with voluntary alcohol consumption in rats
Pharmacogenetics
13
509-515
2003
Rattus norvegicus
Quintanilla, M.E.; Tampier, L.; Valle-Prieto, A.; Sapag, A.; Israel, Y.
Complex I regulates mutant mitochondrial aldehyde dehydrogenase activity and voluntary ethanol consumption in rats
FASEB J.
19
36-42
2005
Rattus norvegicus (P11884)
Yoon, M.; Madden, M.C.; Barton, H.A.
Developmental expression of aldehyde dehydrogenase in rat: a comparison of liver and lung development
Toxicol. Sci.
89
386-398
2006
Rattus norvegicus
Brichac, J.; Ho, K.K.; Honzatko, A.; Wang, R.; Lu, X.; Weiner, H.; Picklo, M.J.
Enantioselective oxidation of trans-4-hydroxy-2-nonenal is aldehyde dehydrogenase isozyme and Mg2+ dependent
Chem. Res. Toxicol.
20
887-895
2007
Rattus norvegicus (P11884), Rattus norvegicus (P51650)
Westerlund, M.; Belin, A.C.; Felder, M.R.; Olson, L.; Galter, D.
High and complementary expression patterns of alcohol and aldehyde dehydrogenases in the gastrointestinal tract: implications for Parkinsons disease
FEBS J.
274
1212-1223
2007
Mus musculus, Rattus norvegicus
Moon, K.H.; Abdelmegeed, M.A.; Song, B.J.
Inactivation of cytosolic aldehyde dehydrogenase via S-nitrosylation in ethanol-exposed rat liver
FEBS Lett.
581
3967-3972
2007
Rattus norvegicus
Badawy, A.A.; Morgan, C.J.
Tryptophan metabolites as potent inhibitors of aldehyde dehydrogenase activity and potential alcoholism-aversion therapeutic agents
Int. Congr. Ser.
1304
344-351
2007
Saccharomyces cerevisiae, Rattus norvegicus
-
Shoeb, M.; Xiao, T.L.; Hodge, R.P.; Ansari, N.H.
A specific and sensitive enzyme activity assay for aldehyde dehydrogenase 1A1 (ALDH1A1)
J. Cell Tissue Res.
8
1203-1209
2008
Bos taurus, Rattus norvegicus
-
Chen, H.W.; Kuo, H.T.; Hwang, L.C.; Kuo, M.F.; Yang, R.C.
Proteomic alteration of mitochondrial aldehyde dehydrogenase 2 in sepsis regulated by heat shock response
Shock
28
710-716
2007
Rattus norvegicus
Soloveva, A.G.; Zimin, Y.V.; Razmakhov, A.M.
Kinetic parameters of liver aldehyde dehydrogenase in rats with cold injury
Bull. Exp. Biol. Med.
148
191-192
2009
Rattus norvegicus
Zhang, X.J.; Chang, L.; Zhang, Y.M.; Deng, S.; Li, Y.J.; Peng, J.
Comparing the role of glutathione-S-transferase and mitochondrial aldehyde dehydrogenase in nitroglycerin biotransformation and the correlation with calcitonin gene-related peptide
Eur. J. Pharmacol.
617
97-101
2009
Rattus norvegicus
Moon, K.H.; Lee, Y.M.; Song, B.J.
Inhibition of hepatic mitochondrial aldehyde dehydrogenase by carbon tetrachloride through JNK-mediated phosphorylation
Free Radic. Biol. Med.
48
391-398
2010
Rattus norvegicus (P11884)
Yao, L.; Fan, P.; Arolfo, M.; Jiang, Z.; Olive, M.F.; Zablocki, J.; Sun, H.L.; Chu, N.; Lee, J.; Kim, H.Y.; Leung, K.; Shryock, J.; Blackburn, B.; Diamond, I.
Inhibition of aldehyde dehydrogenase-2 suppresses cocaine seeking by generating THP, a cocaine use-dependent inhibitor of dopamine synthesis
Nat. Med.
16
1024-1028
2010
Rattus norvegicus
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