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Information on EC 1.3.1.102 - 2-alkenal reductase (NADP+)
for references in articles please use BRENDA:EC1.3.1.102
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.1 With NAD+ or NADP+ as acceptor
1.3.1.102 2-alkenal reductase (NADP+)
IUBMB Comments
Shows highest activity with 1-nitrocyclohexene but also has significant activity with 2-methylpentenal and trans-cinnamaldehyde . Involved in the detoxication of α,β-unsaturated aldehydes and ketones. Has very low activity with NAD as reductant (cf. EC 1.3.1.74, 2-alkenal reductase [NAD(P)+]).
The enzyme appears in viruses and cellular organisms
showSynonyms
ntdbr, alkenal double bond reductase, padbr1, padbr2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
allyl-ADH1
the amino acid sequences of the deduced allyl-ADHs are different in four amino acid residues
allyl-ADH2
the amino acid sequences of the deduced allyl-ADHs are different in four amino acid residues, allyl-ADH2 has the following mutations compared to ADH1: T17A, V30A, L345P,R278H
AOR
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an n-alkanal + NADP+ = an alk-2-enal + NADPH + H+
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
n-alkanal:NADP+ 2-oxidoreductase
Shows highest activity with 1-nitrocyclohexene but also has significant activity with 2-methylpentenal and trans-cinnamaldehyde [3]. Involved in the detoxication of alpha,beta-unsaturated aldehydes and ketones. Has very low activity with NAD as reductant (cf. EC 1.3.1.74, 2-alkenal reductase [NAD(P)+]).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1R,2S,4S)-neoisodihydrocarveol + NADP+
(1R,4S)-isodihydrocarvone + NADPH + H+
Substrates: -
Products: -
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r
(2E)-3-methylpent-2-enal + NADPH + H+
2-methylpentanal + NADP+
Substrates: -
Products: -
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?
(2R,4R)-carveol + NADP+
(R)-carvone + NADPH + H+
Substrates: -
Products: -
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r
(2R,4S)-carveol + NADP+
(S)-carvone + NADPH + H+
Substrates: -
Products: -
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r
(2S,4R)-carveol + NADP+
(R)-carvone + NADPH + H+
Substrates: -
Products: -
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r
(2S,4S)-carveol + NADP+
(S)-carvone + NADPH + H+
Substrates: -
Products: -
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r
(R)-pulegone + NADPH + H+
(1R,4R)-isomenthone + (1R,4S)-menthone + NADP+
Substrates: -
Products: -
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?
(S)-pulegone + NADPH + H+
(1S,4S)-isomenthone + (1S,4R)-menthone + NADP+
Substrates: -
Products: -
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?
1-cyclohexene-1-carboxaldehyde + NADPH + H+
cyclohexanecarbaldehyde + NADP+
Substrates: low yields
Products: -
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?
1-nitrocyclohexene + NADPH + H+
nitrocyclohexane + NADP+
Substrates: -
Products: -
Products: -
?
1-octen-3-one + NADPH + H+
octan-3-one + NADP+
Substrates: -
Products: -
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?
4-coumaryl aldehyde + NADP+
dihydro-4-coumaryl aldehyde + NADPH + H+
Substrates: -
Products: -
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?
caffeoyl aldehyde + NADP+
dihydrocaffeoyl aldehyde + NADPH + H+
Substrates: -
Products: -
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?
trans-3-nonen-2-one + NADPH + H+
nonan-2-one + NADP+
-
Substrates: -
Products: -
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?
trans-cinnamaldehyde + NADPH + H+
3-phenylpropanal + NADP+
Substrates: -
Products: -
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?
[(1E)-1-nitroprop-1-en-2-yl]benzene + NADPH + H+
[(2R)-1-nitropropan-2-yl]benzene + NADP+
Substrates: optically pure form of compound
Products: -
Products: -
?
[(1Z)-1-nitroprop-1-en-2-yl]benzene + NADPH + H+
[(2S)-1-nitropropan-2-yl]benzene + NADP+
Substrates: poor enantioselectivity
Products: -
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?
5-hydroxyconiferyl aldehyde + NADP+
dihydro-5-hydroxyconiferyl aldehyde + NADPH + H+
Substrates: -
Products: -
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?
5-hydroxyconiferyl aldehyde + NADP+
dihydro-5-hydroxyconiferyl aldehyde + NADPH + H+
Substrates: only enzyme mutant PaDBR1C56Y, no activity with the wild-type enzyme
Products: -
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?
coniferyl aldehyde + NADP+
dihydroconiferyl aldehyde + NADPH + H+
Substrates: -
Products: -
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?
coniferyl aldehyde + NADP+
dihydroconiferyl aldehyde + NADPH + H+
Substrates: only enzyme mutant PaDBR1C56Y, no activity with the wild-type enzyme
Products: -
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?
trans-2-nonenal + NADPH + H+
nonanal + NADP+
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme AOR shows acrolein-reducing activity in addition to the cytosolic acrolein detoxification enzyme in leaves of higher plants
Products: -
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?
additional information
?
-
-
Substrates: enzyme AOR shows acrolein-reducing activity in addition to the cytosolic acrolein detoxification enzyme in leaves of higher plants
Products: -
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?
additional information
?
-
-
Substrates: 2-alkenal reductase (AER) catalyzes the reduction of the alpha,beta-unsaturated bond of 2-alkenals to produce n-alkanals
Products: -
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?
additional information
?
-
Substrates: recombinant NtRed-1 does not catalyze dehydrogenation of (2S,4S)-carveol, indicating that the recombinant NtRed-1 lacks the catalytic function as allyl-alcohol dehydrogenase, although the recombinant NtRed-1 is designed from the nucleotide sequence of allyl-ADH
Products: -
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?
additional information
?
-
Substrates: results indicate that the enzyme catalyzes specifically the dehydrogenation of the secondary alcohols adjacent to the C-C double bond, no oxidation of saturated alcohols
Products: -
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?
additional information
?
-
Substrates: the enzymatic reaction is a reversible oxidoreduction and the reaction is enantioselective
Products: -
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?
additional information
?
-
Substrates: the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: docking of the ligand and substrate into the active cavity, overview. The catalytic efficiency of isozyme PaDBR1 is substantially less than that of PaDBR2, especially towards cinnamyl aldehydes carrying a methoxy group (coniferyl, 5-hydroxyconiferyl and sinapyl aldehydes). No activity with sinapyl aldehyde, cinnamyl aldehyde, 4-coumaric acid, caffeic acid, 4-coumaryl alcohol, caffeyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol, and sinapyl alcohol
Products: -
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?
additional information
?
-
Substrates: docking of the ligand and substrate into the active cavity, overview. The catalytic efficiency of isozyme PaDBR1 is substantially less than that of PaDBR2, especially towards cinnamyl aldehydes carrying a methoxy group (coniferyl, 5-hydroxyconiferyl and sinapyl aldehydes). No activity with sinapyl aldehyde, cinnamyl aldehyde, 4-coumaric acid, caffeic acid, 4-coumaryl alcohol, caffeyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol, and sinapyl alcohol
Products: -
Products: -
?
additional information
?
-
-
Substrates: docking of the ligand and substrate into the active cavity, overview. The catalytic efficiency of isozyme PaDBR1 is substantially less than that of PaDBR2, especially towards cinnamyl aldehydes carrying a methoxy group (coniferyl, 5-hydroxyconiferyl and sinapyl aldehydes). No activity with sinapyl aldehyde, cinnamyl aldehyde, 4-coumaric acid, caffeic acid, 4-coumaryl alcohol, caffeyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol, and sinapyl alcohol
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Substrates: enzyme AOR shows acrolein-reducing activity in addition to the cytosolic acrolein detoxification enzyme in leaves of higher plants
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme AOR shows acrolein-reducing activity in addition to the cytosolic acrolein detoxification enzyme in leaves of higher plants
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
Products: -
Products: -
?
additional information
?
-
-
Substrates: the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
utilization of NADP+ by the enzyme is four times greater than for NAD+
NADP+
utilization of NADP+ by the enzyme is four times greater than for NAD+
NADPH
more than 1600fold higher preference for NADPH compared with NADH
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-nonanone
-
competitive inhibition versus 3-nonen-2-one and noncompetitive inhibition versus NADPH
NADP+
-
competitive inhibition versus NADPH and noncompetitive inhibition versus 3-nonen-2-one
Zn2+
-
the addition of 0.25 mM Zn2+ inhibits enzyme activity more than 2fold
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0776
trans-2-nonenal
-
with trans-3-nonen-2-one as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C
0.0282
trans-3-nonen-2-one
-
with trans-3-nonen-2-one as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C
additional information
additional information
the Km-values for the (S)-alcohols are one order of magnitude lower than those for the (R)-alcohols, indicating that the enzyme has a higher affinity for the S-configuration than for the R-configuration
-
0.0943
4-coumaryl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2
0.1183
4-coumaryl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y
0.1663
4-coumaryl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56V
0.1719
4-coumaryl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR1
0.2026
5-hydroxyconiferyl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y
0.3081
5-hydroxyconiferyl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2
0.1437
caffeoyl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y
0.1812
caffeoyl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2
0.1933
caffeoyl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56V
0.2214
caffeoyl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR1
0.1726
coniferyl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y
0.2099
coniferyl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2
0.004
NADPH
-
with trans-2-nonenal as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C
0.0058
NADPH
app. Km value, pH 5.4 and 25°C, with 1-nitrocyclohexene
0.032
NADPH
-
with trans-3-nonen-2-one as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
(1R,2S,4S)-neoisodihydrocarveol
dehydrogenation, pH 8.0, 35°C, NADP+
0.003
(1R,4S)-isodihydrocarvone
hydrogenation to (1R,2S,4S)-neoisodihydrocarveol, pH 7.4, 35°C, NADP+
0.012
(R)-carvone
hydrogenation to (2R,4R)-carveol, pH 7.4, 35°C, NADP+
0.032
(R)-carvone
hydrogenation to (2S,4R)-carveol, pH 7.4, 35°C, NADP+
0.01
(S)-carvone
hydrogenation to (2R,4S)-carveol, pH 7.4, 35°C, NADP+
0.025
(S)-carvone
hydrogenation to (2S,4S)-carveol, pH 7.4, 35°C, NADP+
0.037
4-coumaryl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56V
0.098
4-coumaryl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR1
0.249
4-coumaryl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y
0.278
4-coumaryl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2
0.161
5-hydroxyconiferyl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y
0.169
5-hydroxyconiferyl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2
0.068
caffeoyl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56V
0.132
caffeoyl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR1
0.238
caffeoyl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2
0.277
caffeoyl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y
0.118
coniferyl aldehyde
pH and temperature not specified in the publication, recombinant wild-type isozyme PaDBR2
0.134
coniferyl aldehyde
pH and temperature not specified in the publication, recombinant isozyme PaDBR1 mutant C56Y
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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
0.0018
pH and temperature not specified in the publication, purified recombinant wild-type isozyme PaDBR1, substrate coniferyl aldeyde
0.0026
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56A, substrate coniferyl aldeyde
0.0027
pH and temperature not specified in the publication, purified recombinant wild-type isozyme PaDBR1, substrate 5-hydroxyconiferyl aldeyde
0.0041
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56A, substrate 4-coumaryl aldeyde
0.0046
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56A, substrate 5-hydroxyconiferyl aldeyde
0.0078
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56A, substrate caffeoyl aldeyde
0.0079
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56S, substrate 4-coumaryl aldeyde
0.008 - 4
0.0091
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56S, substrate caffeoyl aldeyde
0.0115
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56S, substrate coniferyl aldeyde
0.0116
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56S, substrate 5-hydroxyconiferyl aldeyde
0.0124
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate 4-coumaryl aldeyde
0.015
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate caffeoyl aldeyde
0.0177
pH and temperature not specified in the publication, purified recombinant wild-type isozyme PaDBR1, substrate caffeoyl aldeyde
0.022
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56F, substrate 5-hydroxyconiferyl aldeyde
0.0234
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56Y, substrate 5-hydroxyconiferyl aldeyde
0.0237
pH and temperature not specified in the publication, purified recombinant wild-type isozyme PaDBR1, substrate 4-coumaryl aldeyde
0.0239
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56Y, substrate coniferyl aldeyde
0.0271
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56F, substrate coniferyl aldeyde
0.0454
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56F, substrate caffeoyl aldeyde
0.0497
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56Y, substrate caffeoyl aldeyde
0.066
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56F, substrate 4-coumaryl aldeyde
0.0743
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56Y, substrate 4-coumaryl aldeyde
4.6
DEAE-Toyopearl anion exchange column chromatography, pH 8.0, 35°C
0.008 - 4
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate 5-hydroxyconiferyl aldeyde
0.008 - 4
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate coniferyl aldeyde
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
suppression of chloroplastic alkenal/one oxidoreductase represses the carbon catabolic pathway in Arabidopsis leaves during night. Phosphoenolpyruvate carboxylase activity decreases and starch degradation during the night is suppressed in aor (RNAi). In contrast, the phenotype of aor (RNAi) is rescued when aor (RNAi) plants are grown under constant light conditions. The smaller plant sizes observed in aor mutants grown under day/night cycle conditions are attributable to the decrease in carbon utilization during the night. The acrolein reducing activity decreases to about 60% and 75%in aor-1 and aor-4 mutant lines, respectively, compared with the wild-type. Lack of AtAOR in chloroplasts induces oxidative stress. Phenotype analysis, detailed overview
physiological function
evolution
tyrosine at position 56 of PaDBR2 is highly conserved among oxidoreductases, and is proposed to be involved in binding with NADPH. In isozyme PaDBR1, this position is occupied by a Cystein residue
evolution
tyrosine at position 56 of PaDBR2 is highly conserved among oxidoreductases, and is proposed to be involved in binding with NADPH. In isozyme PaDBR1, this position is occupied by a cysteine residue
physiological function
lipid-derived reactive carbonyl species (RCS) possess electrophilic moieties and cause oxidative stress by reacting with cellular components. Arabidopsis thaliana has a chloroplast-localized alkenal/one oxidoreductase (AtAOR) for the detoxification of lipid-derived RCS, especially alpha,beta-unsaturated carbonyls. The detoxification of lipid-derived RCS by AtAOR in chloroplasts contributes to the protection of dark respiration and supports plant growth during the night
physiological function
-
the aluminium-induced increase in root expression level of gene encoding 2-alkenal reductase (NADP+-dependent) might contribute to plant Al-tolerance by the detoxification of reactive carbonyls
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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). DBR_TOBAC
343
0
38088
Swiss-Prot
other Location (Reliability: 2)
A0A5B6YZA1_DAVIN
338
0
37801
TrEMBL
other Location (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
74000
74000
approximately, gel filtration chromatography on a TSK G3000SW HPLC column
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
?
x * 55000, about, recombinant His-tagged enzyme, SDS-PAGE
homodimer
each monomer is composed of two domains, a substrate binding or ca