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Information on EC 1.3.1.102 - 2-alkenal reductase (NADP+) and Organism(s) Nicotiana tabacum and UniProt Accession Q9SLN8

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IUBMB Comments
Shows highest activity with 1-nitrocyclohexene but also has significant activity with 2-methylpentenal and trans-cinnamaldehyde . 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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Nicotiana tabacum
UNIPROT: Q9SLN8
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The taxonomic range for the selected organisms is: Nicotiana tabacum
The enzyme appears in selected viruses and cellular organisms
Synonyms
ntdbr, alkenal double bond reductase, padbr1, padbr2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
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
allyl-alcohol dehydrogenase
-
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)+]).
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
-
-
-
?
citral + NADPH + H+
?
show the reaction diagram
low yields
-
-
?
trans-2-nonenal + NADPH + H+
nonanal + 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
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
poor enantioselectivity
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E)-3-methylpent-2-enal
substrate inhibition
1-octen-3-one
substrate inhibition
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
recombinant NtRed-1, pH 7.0 and 35°C
8.3
(S)-pulegone
recombinant NtRed-1, pH 7.0 and 35°C
0.057 - 0.4
1-nitrocyclohexene
0.0058
NADPH
app. Km value, pH 5.4 and 25°C, with 1-nitrocyclohexene
0.516 - 1
trans-cinnamaldehyde
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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+
0.66 - 9.2
(2E)-3-methylpent-2-enal
0.02
(2R,4R)-carveol
dehydrogenation, pH 8.0, 35°C, NADP+
0.025
(2R,4S)-carveol
dehydrogenation, pH 8.0, 35°C, NADP+
0.097
(2S,4R)-carveol
dehydrogenation, pH 8.0, 35°C, NADP+
0.077
(2S,4S)-carveol
dehydrogenation, pH 8.0, 35°C, NADP+
0.012 - 0.032
(R)-carvone
3.3
(R)-pulegone
recombinant NtRed-1, pH 7.0 and 35°C
0.01 - 0.025
(S)-carvone
2.8
(S)-pulegone
recombinant NtRed-1, pH 7.0 and 35°C
1.46 - 11
1-nitrocyclohexene
0.52 - 1.17
1-octen-3-one
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
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
recombinant NtRed-1, pH 7.0 and 35°C
16 - 25.6
1-nitrocyclohexene
2.1 - 2.8
trans-cinnamaldehyde
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.6
(2E)-3-methylpent-2-enal
app. Ki value, pH 5.4 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.11
Red-Toyopearl affinity column chromatography, pH 8.0, 35°C
4.6
DEAE-Toyopearl anion exchange column chromatography, pH 8.0, 35°C
5300
crude extract, pH 8.0, 35°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
with 1-nitrocyclohexene
7.4
reduction of the carbonyl group of (S)-carvone
8
dehydrogenation of (2S,4S)-carveol
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DBR_TOBAC
343
0
38088
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36300
native NtRed-1, SDS-PAGE
37000
alpha2, 2 * 37000, determined by SDS-PAGE
38000
recombinant NtRed-1, 2 * 38000, gel filtration chromatography
38080
allyl-ADH1, calculated from sequence
38480
recombinant NtRed-1, MALDI-TOF MS spectra
74000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
by DEAE-Toyopearl anion exchange column chromatography, followed by Red-Toyopearl affinity column chromatography
by DEAE–Toyopearl and Red–Toyopearl column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
NtRed-1 cloned in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirata, T.; Tamura, Y.; Yokobatake, N.; Shimoda, K.; Ashida, Y.
A 38 kDa allylic alcohol dehydrogenase from the cultured cells of Nicotiana tabacum
Phytochemistry
55
297-303
2000
Nicotiana tabacum (Q9SLN8)
Manually annotated by BRENDA team
Matsushima, A.; Sato, Y.; Otsuka, M.; Watanabe, T.; Yamamoto, H.; Hirata, T.
An enone reductase from Nicotiana tabacum: cDNA cloning, expression in Escherichia coli, and reduction of enones with the recombinant proteins
Bioorg. Chem.
36
23-28
2008
Nicotiana tabacum (Q9SLN8)
Manually annotated by BRENDA team
Mansell, D.J.; Toogood, H.S.; Waller, J.; Hughes, J.M.X.; Levy, C.W.; Gardiner, J.M.; Scrutton, N.S.
Biocatalytic asymmetric alkene reduction: crystal structure and characterization of a double bond reductase from Nicotiana tabacum
ACS Catal.
3
370-379
2013
Nicotiana tabacum (Q9SLN8)
Manually annotated by BRENDA team