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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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
1.3.1.102
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RECOMMENDED NAME
GeneOntology No.
2-alkenal reductase (NADP+)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an n-alkanal + NADP+ = an alk-2-enal + NADPH + H+
show the reaction diagram
-
-
-
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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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cv. sour pummelo
-
-
Manually annotated by BRENDA team
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S5TMG0, S5U4F4
UniProt
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
S5TMG0;, S5U4F4;
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; 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
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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1R,2S,4S)-neoisodihydrocarveol + NADP+
(1R,4S)-isodihydrocarvone + NADPH + H+
show the reaction diagram
-
-
-
r
(2E)-3-methylpent-2-enal + NADPH + H+
2-methylpentanal + NADP+
show the reaction diagram
-
-
-
-
?
(2R,4R)-carveol + NADP+
(R)-carvone + NADPH + H+
show the reaction diagram
-
-
-
r
(2R,4S)-carveol + NADP+
(S)-carvone + NADPH + H+
show the reaction diagram
-
-
-
r
(2S,4R)-carveol + NADP+
(R)-carvone + NADPH + H+
show the reaction diagram
-
-
-
r
(2S,4S)-carveol + NADP+
(S)-carvone + NADPH + H+
show the reaction diagram
-
-
-
r
(R)-pulegone + NADPH + H+
(1R,4R)-isomenthone + (1R,4S)-menthone + NADP+
show the reaction diagram
-
-
-
-
?
(S)-pulegone + NADPH + H+
(1S,4S)-isomenthone + (1S,4R)-menthone + NADP+
show the reaction diagram
-
-
-
-
?
1-cyclohexene-1-carboxaldehyde + NADPH + H+
cyclohexanecarbaldehyde + NADP+
show the reaction diagram
-
low yields
-
-
?
1-nitrocyclohexene + NADPH + H+
nitrocyclohexane + NADP+
show the reaction diagram
-
-
-
-
?
1-octen-3-one + NADPH + H+
octan-3-one + NADP+
show the reaction diagram
-
-
-
-
?
4-coumaryl aldeyde + NADP+
dihydro-4-coumaryl aldehyde + NADPH + H+
show the reaction diagram
S5TMG0;, S5U4F4;
-
-
-
?
5-hydroxyconiferyl aldeyde + NADP+
dihydro-5-hydroxyconiferyl aldehyde + NADPH + H+
show the reaction diagram
acrolein + NADPH + H+
? + NADP+
show the reaction diagram
-
-
-
?
caffeoyl aldeyde + NADP+
dihydrocaffeoyl aldehyde + NADPH + H+
show the reaction diagram
S5TMG0;, S5U4F4;
-
-
-
?
citral + NADPH + H+
?
show the reaction diagram
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low yields
-
-
?
coniferyl aldeyde + NADP+
dihydroconiferyl aldehyde + NADPH + H+
show the reaction diagram
trans-2-nonenal + NADPH + H+
nonanal + NADP+
show the reaction diagram
trans-3-nonen-2-one + NADPH + H+
nonan-2-one + NADP+
show the reaction diagram
-
-
-
-
?
trans-cinnamaldehyde + NADPH + H+
3-phenylpropanal + NADP+
show the reaction diagram
-
-
-
-
?
[(1E)-1-nitroprop-1-en-2-yl]benzene + NADPH + H+
[(2R)-1-nitropropan-2-yl]benzene + NADP+
show the reaction diagram
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optically pure form of compound
-
-
?
[(1Z)-1-nitroprop-1-en-2-yl]benzene + NADPH + H+
[(2S)-1-nitropropan-2-yl]benzene + NADP+
show the reaction diagram
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poor enantioselectivity
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-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acrolein + NADPH + H+
? + NADP+
show the reaction diagram
Q9ZUC1
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-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
-
utilization of NADP+ by the enzyme is four times greater than for NAD+
NADP+
NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E)-3-methylpent-2-enal
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substrate inhibition
1-octen-3-one
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substrate inhibition
2-nonanone
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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
NADPH
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uncompetitive inhibition
Zn2+
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the addition of 0.25 mM Zn2+ inhibits enzyme activity more than 2fold
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
590
(1R,2S,4S)-neoisodihydrocarveol
-
pH 8.0, 35°C, NADP+
0.837 - 1.032
(2E)-3-methylpent-2-enal
38
(2R,4R)-carveol
-
pH 8.0, 35°C, NADP+
52
(2R,4S)-carveol
-
pH 8.0, 35°C, NADP+
1.9
(2S,4R)-carveol
-
pH 8.0, 35°C, NADP+
2.5
(2S,4S)-carveol
-
pH 8.0, 35°C, NADP+
1.4
(R)-pulegone
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recombinant NtRed-1, pH 7.0 and 35°C
8.3
(S)-pulegone
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recombinant NtRed-1, pH 7.0 and 35°C
0.057 - 0.4
1-nitrocyclohexene
0.0943 - 0.1719
4-coumaryl aldeyde
-
0.2026 - 0.3081
5-hydroxyconiferyl aldeyde
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0.1437 - 0.2214
caffeoyl aldeyde
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0.1726 - 0.2099
coniferyl aldeyde
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0.004 - 0.032
NADPH
0.0776
trans-2-nonenal
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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
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with trans-3-nonen-2-one as cosubstrate, in 100 mM Tris (pH 7.2), at 25°C
0.516 - 1
trans-cinnamaldehyde
additional information
additional information
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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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
(1R,2S,4S)-neoisodihydrocarveol
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dehydrogenation, pH 8.0, 35°C, NADP+
0.003
(1R,4S)-isodihydrocarvone
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hydrogenation to (1R,2S,4S)-neoisodihydrocarveol, pH 7.4, 35°C, NADP+
0.66 - 9.2
(2E)-3-methylpent-2-enal
0.02
(2R,4R)-carveol
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dehydrogenation, pH 8.0, 35°C, NADP+
0.025
(2R,4S)-carveol
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dehydrogenation, pH 8.0, 35°C, NADP+
0.097
(2S,4R)-carveol
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dehydrogenation, pH 8.0, 35°C, NADP+
0.077
(2S,4S)-carveol
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dehydrogenation, pH 8.0, 35°C, NADP+
0.012 - 0.032
(R)-carvone
3.3
(R)-pulegone
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recombinant NtRed-1, pH 7.0 and 35°C
0.01 - 0.025
(S)-carvone
2.8
(S)-pulegone
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recombinant NtRed-1, pH 7.0 and 35°C
1.46 - 11
1-nitrocyclohexene
0.52 - 1.17
1-octen-3-one
0.037 - 0.278
4-coumaryl aldeyde
-
0.161 - 0.169
5-hydroxyconiferyl aldeyde
-
0.068 - 0.277
caffeoyl aldeyde
-
0.118 - 0.134
coniferyl aldeyde
-
1.3
NADPH
-
app. Kcat, pH 7.3 and 25°C, with 1-nitrocyclohexene
0.87 - 2.92
trans-2-nonenal
1.1 - 3.5
trans-cinnamaldehyde
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4
(R)-pulegone
-
recombinant NtRed-1, pH 7.0 and 35°C
0.34
(S)-pulegone
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recombinant NtRed-1, pH 7.0 and 35°C
16 - 25.6
1-nitrocyclohexene
0.22 - 2.95
4-coumaryl aldeyde
-
0.55 - 0.8
5-hydroxyconiferyl aldeyde
-
0.35 - 1.93
caffeoyl aldeyde
-
0.56 - 0.78
coniferyl aldeyde
-
2.1 - 2.8
trans-cinnamaldehyde
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
(2E)-3-methylpent-2-enal
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app. Ki value, pH 5.4 and 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0018
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant wild-type isozyme PaDBR1, substrate coniferyl aldeyde
0.0026
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56A, substrate coniferyl aldeyde
0.0027
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant wild-type isozyme PaDBR1, substrate 5-hydroxyconiferyl aldeyde
0.0041
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56A, substrate 4-coumaryl aldeyde
0.0046
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56A, substrate 5-hydroxyconiferyl aldeyde
0.0078
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56A, substrate caffeoyl aldeyde
0.0079
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56S, substrate 4-coumaryl aldeyde
0.008 - 4
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate 5-hydroxyconiferyl aldeyde; pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate coniferyl aldeyde
0.0091
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56S, substrate caffeoyl aldeyde
0.0115
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56S, substrate coniferyl aldeyde
0.0116
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56S, substrate 5-hydroxyconiferyl aldeyde
0.0124
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate 4-coumaryl aldeyde
0.015
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate caffeoyl aldeyde
0.0177
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant wild-type isozyme PaDBR1, substrate caffeoyl aldeyde
0.022
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56F, substrate 5-hydroxyconiferyl aldeyde
0.0234
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56Y, substrate 5-hydroxyconiferyl aldeyde
0.0237
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant wild-type isozyme PaDBR1, substrate 4-coumaryl aldeyde
0.0239
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56Y, substrate coniferyl aldeyde
0.0271
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56F, substrate coniferyl aldeyde
0.0454
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56F, substrate caffeoyl aldeyde
0.0497
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56Y, substrate caffeoyl aldeyde
0.066
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56F, substrate 4-coumaryl aldeyde
0.0743
S5TMG0;, S5U4F4;
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56Y, substrate 4-coumaryl aldeyde
0.11
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Red-Toyopearl affinity column chromatography, pH 8.0, 35°C
4.6
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DEAE-Toyopearl anion exchange column chromatography, pH 8.0, 35°C
5300
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crude extract, pH 8.0, 35°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
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with 1-nitrocyclohexene
7.4
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reduction of the carbonyl group of (S)-carvone
8
-
dehydrogenation of (2S,4S)-carveol
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Nicotiana tabacum;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36300
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native NtRed-1, SDS-PAGE
37000
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alpha2, 2 * 37000, determined by SDS-PAGE
38000
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recombinant NtRed-1, 2 * 38000, gel filtration chromatography
38080
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allyl-ADH1, calculated from sequence
38480
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recombinant NtRed-1, MALDI-TOF MS spectra
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
determination of the X-ray crystal structures of holo-, binary (NADP(H)-bound), and ternary (NADP+ and 4-hydroxy-3-methoxycinnamaldehyde-bound) NtDBR complexes
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by DEAE-Toyopearl anion exchange column chromatography, followed by Red-Toyopearl affinity column chromatography
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by DEAE–Toyopearl and Red–Toyopearl column chromatography
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recombinant His-tagged isozyme PaDBR1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration; recombinant His-tagged isozyme PaDBR2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
S5TMG0;, S5U4F4;
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His-tagged isozyme PaDBR1 in Escherichia coli strain BL21(DE3); DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His-tagged isozyme PaDBR2 in Escherichia coli strain BL21(DE3)
S5TMG0;, S5U4F4;
gene aor, real-time PCR. enzyme expression analysis
gene cloned into pET21b (Novagen), without a stop codon, to incorporate a C-terminal His6-tag and transformed Escherichia coli strain BL21(DE3)pLysS (Stratagene)
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NtRed-1 cloned in Escherichia coli
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quantitative RT-PCR enzyme expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
boron and aluminium induce the enzyme expression in Citrus grandis roots
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C56A
S5TMG0;, S5U4F4;
site-directed mutagenesis, the mutant shows altered substrate specificity with cinnamoyl aldehydes compared to wild-type enzyme
C56F
S5TMG0;, S5U4F4;
site-directed mutagenesis, the mutant shows altered substrate specificity and increased activity with cinnamoyl aldehydes compared to wild-type enzyme
C56S
S5TMG0;, S5U4F4;
site-directed mutagenesis, the mutant shows altered substrate specificity with cinnamoyl aldehydes compared to wild-type enzyme
C56V
S5TMG0;, S5U4F4;
site-directed mutagenesis, the mutant shows altered substrate specificity with cinnamoyl aldehydes compared to wild-type enzyme
C56Y
S5TMG0;, S5U4F4;
site-directed mutagenesis, the mutation turns the substrate selectivity and catalytic efficiency of isozyme PaDBR1 indistinguishable from those of isozyme PaDBR2, Docking arrangement of PaDBR1C56Y with NADP+/p-coumaryl aldehyde, overview. Increased activity compared to wild-type enzyme
additional information
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.102)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)