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Enzyme Nomenclature
Information on EC 1.2.1.4 - aldehyde dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.2.1.4
Word Map on EC 1.2.1.4
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.2.1.4
-
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RECOMMENDED NAME
GeneOntology No.
aldehyde dehydrogenase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+
random kinetic mechanism
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an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+
random kinetic mechanism
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an aldehyde + NADP+ + H2O = a carboxylate + NADPH + H+
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
redox reaction
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-
-
-
reduction
oxidation
-
-
-
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reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
aldehyde:NADP+ oxidoreductase
-
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CAS REGISTRY NUMBER
COMMENTARY
9028-87-9
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97162-78-2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
IFO 3262, IFO 3263, IFO 3264, IFO 3265, IFO 3266, IFO 3267, IFO 3268, IFO 3269, IFO 3270
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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; IFO 3171, IFO 3272, IFO 3274; IFO 3189, IFO 3287; IFO 3244; IFO 3260; IFO 3275, IFO 3276; IFO 3293, IFO 12257, IFO 12258, IFO 3294; IFO IFO 3462
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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+
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6% activity compared to 4-nitrobenzaldehyde
-
-
?
4-hydroxybenzaldehyde + NADP+ + H2O
4-hydroxybenzoate + NADPH + H+
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20% activity compared to 4-nitrobenzaldehyde
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-
?
4-nitroacetophenone + NADP+ + H2O
?
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2% activity compared to 4-nitrobenzaldehyde
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-
?
4-nitrobenzaldehyde + NADP+ + H2O
4-nitrobenzoate + NADPH + H+
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100% activity
-
-
?
butanal + NADP+ + H2O
butanoate + NADPH + H+
-
5% activity compared to 4-nitrobenzaldehyde
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-
?
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
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19% of the activity with acetaldehyde
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-
ir
methylglyoxal + NADP+ + H2O
?
-
7% activity compared to 4-nitrobenzaldehyde
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-
?
phenylglyoxal + NADP+ + H2O
?
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3% activity compared to 4-nitrobenzaldehyde
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-
?
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+
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-
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-
?
acetaldehyde + NADP+
?
Acetobacter acetigenus
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
Acetobacter ascendens
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
Gluconobacter gluconicus
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+
?
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enzyme is involved in assimilation of ethanol
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acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
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enzyme a, b, c, d and e
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-
?
acetaldehyde + NADP+ + H2O
acetate + NADPH + H+
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131% of the activity with isovaleraldehyde
-
-
?
an aldehyde + NADP+ + H2O
an acid + NADPH + H+
-
removal of aldehydes and alcohols in cells under stress
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-
?
benzaldehyde + NADP+
benzoate + NADPH
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l40% of the activity with acetaldehyde
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-
?
benzaldehyde + NADP+
benzoate + NADPH
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6% of the activity with isovaleraldehyde
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-
?
benzaldehyde + NADP+ + H2O
benzoate + NADPH + H+
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8% activity compared to 4-nitrobenzaldehyde
-
-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
-
n-butanal, enzyme a, b, c, d and e
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-
?
butanal + NADP+ + H2O
butyrate + NADPH + H+
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n-butanal, 2% of the activity with acetaldehyde
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-
ir
formaldehyde + NADP+ + H2O
formate + NADPH + H+
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weak activity with enzyme a, b, d and e
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-
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formaldehyde + NADP+ + H2O
formate + NADPH + H+
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low activity
-
-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
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low activity
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-
?
formaldehyde + NADP+ + H2O
formate + NADPH + H+
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2% of the activity with acetaldehyde
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ir
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
-
-
?
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
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ir
glyceraldehyde + NADP+ + H2O
glycerate + NADPH + H+
-
-
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ir
isobutyraldehyde + NADP+ + H2O
isobutyrate + NADPH + H+
-
-
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ir
isobutyraldehyde + NADP+ + H2O
isobutyrate + NADPH + H+
-
-
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ir
octanal + NADP+ + H2O
octanoate + NADPH + H+
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n-octanal, enzyme b, c, d and e
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-
?
pentanal + NADP+
pentanoate + NADPH
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n-pentanal, enzyme a, b, c, d and e
-
-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
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enzyme a, b, c, d and e
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-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
-
much lower activity than with acetaldehyde
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-
?
propanal + NADP+ + H2O
propionate + NADPH + H+
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102% of the activity with acetaldehyde
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-
ir
propanal + NADP+ + H2O
propionate + NADPH + H+
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181% of the activity with isovaleraldehyde
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-
?
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
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-
-
additional information
?
-
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the constitutive enzyme may function in the intracellular detoxification of short chain aldehydes by conversion to corresponding fatty acids
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additional information
?
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enzyme is involved in the oxidation of alkanes
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-
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additional information
?
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no activity with glycolaldehyde and glyceraldehyde
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-
-
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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-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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+
?
Acetobacter ascendens
-
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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INHIBITORS
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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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
-
influence of pH-value and buffer of the Km-value for hexanal
-
additional information
additional information
-
Km-values of NADP+ and decanal as a function of the lauryl sarcosin concentration
-
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
cancerous pneumocytes develop significant higher levels of ALDH3A1 expression than normal pneumocytes
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
58000
82000
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 58000, enzyme c, SDS-PAGE; 1 * 65000, enzyme a, SDS-PAGE; 1 * 70000, enzyme e, SDS-PAGE; 1 * 82000, enzyme b, SDS-PAGE; 1 * 87000, enzyme d, SDS-PAGE
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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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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ENGINEERING
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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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.4)
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