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Information on EC 1.2.1.4 - aldehyde dehydrogenase (NADP+)
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EC Tree
1.2.1.4 aldehyde dehydrogenase (NADP+)Specify your search results
Word Map
- 1.2.1.4
-
voltage-gated
-
kvbeta1
- beta-subunits
-
voltage-dependent
-
pore-forming
-
juxtaparanodal
-
paranodal
-
caspr
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
AKR1A4, aldehyde dehydrogenase (NADP+), aldehyde dehydrogenase 3A1, aldehyde reductase, ALDH, ALDH1, ALDH3A1, AlDHPyr1147, dehydrogenase, aldehyde (nicotinamide adenine dinucleotide phosphate), Kvbeta2, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde dehydrogenase (NADP+)
aldehyde dehydrogenase 3A1
ALDH3A1
AlDHPyr1147
dehydrogenase, aldehyde (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
NADP-acetaldehyde dehydrogenase
-
-
-
-
NADP-dependent aldehyde dehydrogenase
NADP-dependent aldehyde dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+
random kinetic mechanism
-
an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+
random kinetic mechanism
-
-
an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
aldehyde:NADP+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-87-9
-
97162-78-2
-
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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
2-cyanobenzaldehyde + NADP+ + H2O
2-cyanobenzoate + NADPH + H+
-
3% activity compared to 4-nitrobenzaldehyde
-
-
?
2-methlybutyraldehyde + NADP+ + H2O
2-methylbutanoate + NADPH + H+
-
16% activity compared to 4-nitrobenzaldehyde
-
-
?
2-nitrobenzaldehyde + NADP+ + H2O
2-nitrobenzoate + NADPH + H+
-
22% activity compared to 4-nitrobenzaldehyde
-
-
?
3-nitrobenzaldehyde + NADP+ + H2O
3-nitrobenzoate + NADPH + H+
-
53% activity compared to 4-nitrobenzaldehyde
-
-
?
4-cyanobenzaldehyde + NADP+ + H2O
4-cyanobenzoate + NADPH + H+
-
6% activity compared to 4-nitrobenzaldehyde
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
-
20% activity compared to 4-nitrobenzaldehyde
-
-
?
4-nitroacetophenone + NADP+ + H2O
?
-
2% activity compared to 4-nitrobenzaldehyde
-
-
?
4-nitrobenzaldehyde + NADP+ + H2O
4-nitrobenzoate + NADPH + H+
-
100% activity
-
-
?
butanal + NADP+ + H2O
butanoate + NADPH + H+
-
5% activity compared to 4-nitrobenzaldehyde
-
-
?
chloroacetaldehyde + NADP+ + H2O
chloroacetate + NADPH + H+
-
most effective substrate in the absence of Mg2+
-
-
?
crotonaldehyde + NADP+ + H2O
crotonate + NADPH + H+
-
2% activity compared to 4-nitrobenzaldehyde
-
-
?
glutaraldehyde + NADP+ + H2O
glutarate + NADPH + H+
-
-
-
-
?
hexanal + NADP+ + H2O
hexanoate + NADPH + H+
-
1% activity compared to 4-nitrobenzaldehyde
-
-
?
isobutanal + NADP+
isobutyrate + NADPH
-
19% of the activity with acetaldehyde
-
-
ir
methylglyoxal + NADP+ + H2O
?
-
7% activity compared to 4-nitrobenzaldehyde
-
-
?
phenylglyoxal + NADP+ + H2O
?
-
3% activity compared to 4-nitrobenzaldehyde
-
-
?
succinic semialdehyde + NADP+ + H2O
?
-
5% activity compared to 4-nitrobenzaldehyde
-
-
?
trans,trans-muconaldehyde + NADP+ + H2O
trans,trans-muconic acid + NADPH + H+
-
-
-
?
valeraldehyde + NADP+ + H2O
pentanoate + NADPH + H+
-
1% activity compared to 4-nitrobenzaldehyde
-
-
?
4-hydroxy-2-nonenal + NADP+ + H2O
(2E)-4-hydroxynon-2-enoate + NADPH + H+
-
-
-
-
?
4-hydroxy-2-nonenal + NADP+ + H2O
(2E)-4-hydroxynon-2-enoate + NADPH + H+
-
-
-
-
?
4-hydroxy-2-nonenal + NADP+ + H2O
(2E)-4-hydroxynon-2-enoate + NADPH + H+
-
-
-
-
?
acetaldehyde + NADP+
?
Acetobacter acetigenus
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
Gluconobacter gluconicus
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
enzyme a, b, c, d and e
-
-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
-
131% of the activity with isovaleraldehyde
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
removal of aldehydes and alcohols in cells under stress
-
-
?
benzaldehyde + NADP+
benzoate + NADPH
-
l40% of the activity with acetaldehyde
-
-
?
benzaldehyde + NADP+
benzoate + NADPH
-
6% of the activity with isovaleraldehyde
-
-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
-
8% activity compared to 4-nitrobenzaldehyde
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
n-butanal, enzyme a, b, c, d and e
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
n-butanal, 2% of the activity with acetaldehyde
-
-
ir
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
weak activity with enzyme a, b, d and e
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
low activity
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
low activity
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
-
2% of the activity with acetaldehyde
-
-
ir
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
-
?
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
ir
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
ir
isobutyraldehyde + NADP+ + H2O
isobutyrate + NADPH + H+
-
-
-
ir
isobutyraldehyde + NADP+ + H2O
isobutyrate + NADPH + H+
-
-
-
ir
octanal + NADP+ + H2O
octanoate + NADPH + H+
-
n-octanal, enzyme b, c, d and e
-
-
?
pentanal + NADP+
pentanoate + NADPH
-
n-pentanal, enzyme a, b, c, d and e
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
enzyme a, b, c, d and e
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
much lower activity than with acetaldehyde
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
102% of the activity with acetaldehyde
-
-
ir
propanal + NADP+ + H2O
propionate + NADPH + H+
-
181% of the activity with isovaleraldehyde
-
-
?
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
-
-
-
-
?
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
-
-
-
ir
propionaldehyde + NADP+ + H2O
propanoate + NADPH + H+
-
-
-
ir
additional information
?
-
-
the constitutive enzyme may function in the intracellular detoxification of short chain aldehydes by conversion to corresponding fatty acids
-
-
?
additional information
?
-
-
the constitutive enzyme may function in the intracellular detoxification of short chain aldehydes by conversion to corresponding fatty acids
-
-
?
additional information
?
-
-
enzyme is involved in the oxidation of alkanes
-
-
?
additional information
?
-
-
no activity with glycolaldehyde and glyceraldehyde
-
-
?
additional information
?
-
no activity with phenylacetaldehyde, chlorobenzaldehyde, betaine aldehyde and succinic semialdehyde
-
-
?
additional information
?
-
no activity with phenylacetaldehyde, chlorobenzaldehyde, betaine aldehyde and succinic semialdehyde
-
-
?
additional information
?
-
-
no activity with 4-chlorobenzaldehyde, 4-fluorbenzaldehyde, tolualdehyde, anisaldehyde, formaldehyde, octanal, cinnamaldehyde, and isatin
-
-
?
additional information
?
-
-
enzyme is partly repressed during growth on glucose
-
-
?
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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 + NADP+
?
Acetobacter acetigenus
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
Gluconobacter gluconicus
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
acetaldehyde + NADP+
?
-
enzyme is involved in assimilation of ethanol
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
removal of aldehydes and alcohols in cells under stress
-
-
?
additional information
?
-
-
the constitutive enzyme may function in the intracellular detoxification of short chain aldehydes by conversion to corresponding fatty acids
-
-
?
additional information
?
-
-
the constitutive enzyme may function in the intracellular detoxification of short chain aldehydes by conversion to corresponding fatty acids
-
-
?
additional information
?
-
-
enzyme is involved in the oxidation of alkanes
-
-
?
additional information
?
-
-
enzyme is partly repressed during growth on glucose
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
-
reaction with NAD+ is less than 1% of the activity with NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Mn2+
Rb+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
in unilamellar liposomes produced by phosphatidylcholine, the enzyme activity decreases to 1% or less of the original activity. About 10% of the original activity can be preserved in unilamellar liposomes prepared from bacterial phospholipids
-
additional information
-
ALDH3A1 is inactivated and covalently cross-linked by direct UV-exposure
-
additional information
-
ALDH3A1 is inactivated and covalently cross-linked by direct UV-exposure
-
additional information
-
ALDH3A1 is inactivated and covalently cross-linked by direct UV-exposure
-
additional information
-
ALDH3A1 is inactivated and covalently cross-linked by direct UV-exposure
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
Comparative subcellular distribution of benzaldehyde and acetaldehyde dehydrogenase activities in two hepatoma cell lines and in normal hepatocytes.
Carcinoma, Hepatocellular
Oxidative metabolism of 4-hydroxy-2,3-nonenal during diethyl-nitrosamine-induced carcinogenesis in rat liver.
Demyelinating Diseases
Potassium channel distribution, clustering, and function in remyelinating rat axons.
Neoplasms
Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gabP and expression of the GABA permease gene.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.056
4-hydroxy-2-nonenal
-
in the cytosolic extracts of the ALDH3A1-transfected HCE cells
0.056
4-hydroxy-2-nonenal
-
in the cytosolic extracts of the ALDH3A1-transfected HCE cells
0.056
4-hydroxy-2-nonenal
-
in the cytosolic extracts of the ALDH3A1-transfected HCE cells
0.056
4-hydroxy-2-nonenal
-
in the cytosolic extracts of the ALDH3A1-transfected HCE cells
additional information
additional information
-
Km-values of NADP+ and decanal as a function of the lauryl sarcosin concentration
-
additional information
additional information
-
influence of pH-value and buffer of the Km-value for hexanal
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00312
-
native enzyme, with NAD+ as cofactor, pH and temperature not specified in the publication
0.00315
-
mutant enzyme A200E, with NAD+ as cofactor, pH and temperature not specified in the publication
0.0113
-
mutant enzyme A200E/V210Q, with NAD+ as cofactor, pH and temperature not specified in the publication
0.012
-
mutant enzyme A200E/V210Q, with NADP+ as cofactor, pH and temperature not specified in the publication
0.06
-
mutant enzyme A200E, with NADP+ as cofactor, pH and temperature not specified in the publication
0.853
-
wild type enzyme from cornea, using propionaldehyde and NAD+ as substrates
3
-
native enzyme, with NADP+ as cofactor, pH and temperature not specified in the publication
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9.2
-
pH 5.0: 10% of maximal activity, pH 9.2: 15% of maximal activity
8 - 11.5
-
pH 8.5: about 60% of maximal activity, pH 11.5: about 80% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 700926D, highest activity in cells grown with ethanol
-
-
brenda
IFO 3262, IFO 3263, IFO 3264, IFO 3265, IFO 3266, IFO 3267, IFO 3268, IFO 3269, IFO 3270
-
-
brenda
IFO 3130, IFO 3172, IFO 3289, IFO 3290, IFO 3291, IFO 12528, var. alpha IFO 3254, var. alpha IFO 3255, var. alpha IFO 3256, var. alpha IFO 3257, var. alpha IFO 3258
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cancerous pneumocytes develop significant higher levels of ALDH3A1 expression than normal pneumocytes
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (1052 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
82000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and in complex with isobutyraldehyde and/or NADP+, capillary counterdiffusion method
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A200E
-
the mutant shows strongly reduced activity (50fold) with NADP+ compared to the wild type enzyme
A200E/V210Q
-
the mutant shows strongly reduced activity (250fold) with NADP+ and about 3fold increased activity with NAD+ compared to the wild type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-8°C, 16% glycerol, 1 mM dithiothreitol, 12% loss of activity after 6 months
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Source 30Q column chromatography and Superdex 200 gel filtration
using a Q-sepharose anion exchange column for enzyme preparation of mouse liver, using nickel agarose affinity chromatography for purification of recombinant protein
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
medicine
-
ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
medicine
-
ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
medicine
-
ALDH3A1 contributes to the detoxification of various aldehydes produced in response to oxidative stress
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vandecasteele, J.P.; Guerrillot, L.
Aldehyde dehydrogenases from Pseudomonas aeruginosa
Methods Enzymol.
89
484-490
1982
Pseudomonas aeruginosa
brenda
Guerrillot, L.; Vandecasteele, J.P.
Purification and characterization of two aldehyde dehydrogenases from Pseudomonas aeruginosa
Eur. J. Biochem.
81
185-192
1977
Pseudomonas aeruginosa
brenda
Hommel, R.; Kurth, J.; Kleber, H.P.
NADP+-dependent aldehyde dehydrogenase from Acetobacter rancens CCM 1774: purification and properties
J. Basic Microbiol.
28
25-33
1988
Acetobacter pasteurianus, Acetobacter pasteurianus CCM 1774
-
brenda
Aurich, H.; Sorger, H.; Bergmann, R.; Lasch, J.
Kinetics of membrane-bound aldehyde dehydrogenase from Acinetobacter calcoaceticus
Biol. Chem. Hoppe-Seyler
368
101-109
1987
Acinetobacter calcoaceticus
brenda
Aurich, H.; Sorger, H.; Bergmann, R.; Lasch, J.; Koelsch, R.
Wechselwirkungen der Aldehyddehydrogenase aus Acinetobacter calcoaceticus mit Membranlipiden. 1. Einflu¯ von Detergentien, Proteinasen und Phospholipasen auf die Solubilisierung und Aktivitaet des Enzyms
J. Basic Microbiol.
25
623-629
1985
Acinetobacter calcoaceticus
-
brenda
Aurich, H.; Bergmann, R.; Lasch, J.; Koelsch, R.; Sorger, H.
Wechselwirkungen der Aldehyddehydrogenase aus Acinetobacter calcoaceticus mit Membranlipiden. 2. Rekonstitution in kuenstlichen Membranvesikeln
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Acinetobacter calcoaceticus
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Sasaki, S.; Sugawara, Y.
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Muraoka, H.; Watabe, Y.; Ogasawara, N.; Takahashi, H.
Purification and properties of five NADP-dependent aldehyde dehydrogenases from Acetobacter aceti
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Adachi, O.; Matsushita, K.; Shinagawa, E.; Ameyama, M.
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Acetobacter aceti, Acetobacter acetigenus, Acetobacter orleanensis, Acetobacter ascendens, Frateuria aurantia, Gluconobacter oxydans, Acetobacter pasteurianus, Gluconobacter albidus, Gluconobacter cerinus, Gluconobacter gluconicus, Gluconacetobacter liquefaciens, Gluconobacter roseus, Gluconobacter sphaericus
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Sugawara, Y.; Sasaki, S.
Purification and properties of aldehyde dehydrogenase from Proteus vulgaris
Biochim. Biophys. Acta
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Seegmiller, J.E.
Triphosphopyridine nucleotide-linked aldehyde dehydrogenase from yeast
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Saccharomyces cerevisiae
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Jacobson, M.K.; Bernofsky, C.
Mitochondrial acetaldehyde dehydrogenase from Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Dickinson, F.M.
The purification and some properties of the Mg(2+)-activated cytosolic aldehyde dehydrogenase of Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Ho, K.K.; Weiner, H.
Isolation and characterization of an aldehyde dehydrogenase encoded by the aldB gene of Escherichia coli
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Escherichia coli
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Estey, T.; Piatigorsky, J.; Lassen, N.; Vasiliou, V.
ALDH3A1: a corneal crystallin with diverse functions
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Oryctolagus cuniculus, Homo sapiens, Mammalia, Mus musculus
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Short, D.M.; Lyon, R.; Watson, D.G.; Barski, O.A.; McGarvie, G.; Ellis, E.M.
Metabolism of trans, trans-muconaldehyde, acytotoxic metabolite of benzene, in mouse liver by alcohol dehydrogenase Adh1 and aldehyde reductase AKR1A4
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Mus musculus (Q540D7)
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Lassen, N.; Bateman, J.B.; Estey, T.; Kuszak, J.R.; Nees, D.W.; Piatigorsky, J.; Duester, G.; Day, B.J.; Huang, J.; Hines, L.M.; Vasiliou, V.
Multiple and additive functions of ALDH3A1 and ALDH1A1: cataract phenotype and ocular oxidative damage in Aldh3a1(-/-)/Aldh1a1(-/-) knock-out mice
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Patel, M.; Lu, L.; Zander, D.S.; Sreerama, L.; Coco, D.; Moreb, J.S.
ALDH1A1 and ALDH3A1 expression in lung cancers: correlation with histologic type and potential precursors
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Homo sapiens
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Alka, K.; Ryan, B.J.; Dolly, J.O.; Henehan, G.T.
Substrate profiling and aldehyde dismutase activity of the Kvbeta2 subunit of the mammalian Kv1 potassium channel
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42
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Mihasan, M.; Stefan, M.; Hritcu, L.; Artenie, V.; Brandsch, R.
Evidence of a plasmid-encoded oxidative xylose-catabolic pathway in Arthrobacter nicotinovorans pAO1
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Paenarthrobacter nicotinovorans
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Mukhopadhyay, A.; Wei, B.; Weiner, H.
Mitochondrial NAD dependent aldehyde dehydrogenase either from yeast or human replaces yeast cytoplasmic NADP dependent aldehyde dehydrogenase for the aerobic growth of yeast on ethanol
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Saccharomyces cerevisiae
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Bezsudnova, E.Y.; Petrova, T.E.; Artemova, N.V.; Boyko, K.M.; Shabalin, I.G.; Rakitina, T.V.; Polyakov, K.M.; Popov, V.O.
NADP-dependent aldehyde dehydrogenase from archaeon Pyrobaculum sp.1860: structural and functional features
Archaea
2016
9127857
2016
Pyrobaculum ferrireducens (G7VCG0), Pyrobaculum ferrireducens 1860 (G7VCG0)
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