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EC Tree
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ADH1, allyl-ADH, NtRed-1,
more
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ADH1
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allyl alcohol + NADP+ = acrolein + NADPH + H+
allyl alcohol + NADP+ = acrolein + NADPH + H+
3-methyl-2-buten-1-ol-dependent inducible activity
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allyl alcohol + NADP+ = acrolein + NADPH + H+
also acts on saturated primary alcohols
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allyl alcohol + NADP+ = acrolein + NADPH + H+
3-methyl-2-buten-1-ol-dependent inducible activity
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-
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allyl-alcohol:NADP+ oxidoreductase
Also acts on saturated primary alcohols.
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(2S,4S)-carveol + NADP+
(S)-carvone + NADPH
-
-
-
r
(R)-(+)-perillyl alcohol + NADP+
?
-
-
-
-
r
(R)-pulegone + NADP+
(1R,4R)-isomenthone + (1R,4S)-menthone + NADPH + H+
recombinant enzyme
reaction is not stereospecific as with the native enzyme
-
?
(R)-pulegone + NADP+
(1R,4R)-isomenthone + NADPH + H+
native enzyme
-
-
?
(S)-carvone + NADPH
(2S,4S)-carveol + NADP+
-
-
-
r
(S)-pulegone + NADP+
(1S,4S)-isomenthone + (1S,4R)-menthone + NADPH + H+
recombinant enzyme
-
-
?
1-butanol + NADP+
?
-
-
-
-
r
2,3-butylene glycol + NADP+
?
-
-
-
-
r
2-buten-1-ol + NADP+
?
-
-
-
-
r
2-buten-2-ol + NADPH
but-2-enal
3-aminobenzyl alcohol + NADP+
?
-
-
-
-
r
3-chloro-2-buten-1-ol + NADP+
3-chloro-2-butenaldehyde + NADPH
3-methyl-1-butanol + NADP+
?
-
-
-
-
r
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
3-methyl-3-buten-1-ol + NADP+
?
-
-
-
-
r
allyl alcohol + NADP+
acrolein + NADPH
allyl alcohol + NADP+
acrolein + NADPH + H+
benzyl alcohol + NADP+
?
-
-
-
-
r
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
saturated primary alcohols + NADP+
?
-
i.e. ethyl alcohol, n-propyl alcohol, n-butyl acohol, isobutyl alcohol, propylene glycol
-
-
r
additional information
?
-
2-buten-2-ol + NADPH
but-2-enal
-
-
-
-
?
2-buten-2-ol + NADPH
but-2-enal
-
-
-
-
?
3-chloro-2-buten-1-ol + NADP+
3-chloro-2-butenaldehyde + NADPH
-
-
-
-
?
3-chloro-2-buten-1-ol + NADP+
3-chloro-2-butenaldehyde + NADPH
-
-
-
-
?
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
-
-
-
?
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
-
can use substrate as sole carbon source
-
?
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
-
-
-
?
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
-
can use substrate as sole carbon source
-
?
allyl alcohol + NADP+
acrolein + NADPH
-
-
-
r
allyl alcohol + NADP+
acrolein + NADPH
-
-
-
-
r
allyl alcohol + NADP+
acrolein + NADPH
-
specific for the (S)-isomer of secondary allylic alcohols, several stereomers tested for activity in both reaction directions
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-
r
allyl alcohol + NADP+
acrolein + NADPH + H+
-
-
-
?
allyl alcohol + NADP+
acrolein + NADPH + H+
-
-
-
-
?
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
-
-
-
?
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
-
-
-
-
?
additional information
?
-
(R)-carvone, (S)-carvone, (1S,5S)-verbenone, (1R,5R)-verbenone, oxalacetic acid, and (2S,4S)-carveol do not serve as substrate
-
-
?
additional information
?
-
-
(R)-carvone, (S)-carvone, (1S,5S)-verbenone, (1R,5R)-verbenone, oxalacetic acid, and (2S,4S)-carveol do not serve as substrate
-
-
?
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3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
allyl alcohol + NADP+
acrolein + NADPH
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
-
can use substrate as sole carbon source
-
?
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
-
can use substrate as sole carbon source
-
?
allyl alcohol + NADP+
acrolein + NADPH
-
-
-
-
r
allyl alcohol + NADP+
acrolein + NADPH
-
-
-
-
r
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NAD+
-
exhibits less than 5% of the activity with NADP+
NAD(P)H
-
-
NADP+
-
NADP+
-
activity 4times greater than with NAD+
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additional information
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is sensitive against metal ion chelators
additional information
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is not sensitive against metal ion chelators
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3-methyl-2-buten-1-al
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product inhibition, therefore the product must be removed via reaction with hydrazine during the enzyme assay
p-chloromercuribenzoate
-
can be overcome by addition of gluthathione
additional information
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not: monoiodoacetate
-
EDTA
-
-
EDTA
-
only at concentration of 100 mM 50% reduction
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0.012
(R)-(+)-perillyl alcohol
-
-
8.3
(S)-pulegone
recombinant enzyme, pH 7.0, 35°C
0.011
3-aminobenzyl alcohol
-
-
0.007
3-chloro-2-buten-1-ol
-
-
0.27
3-methyl-1-butanol
-
-
0.04
3-methyl-2-buten-1-ol
-
-
1.7
3-methyl-3-buten-1-ol
-
-
0.036
cinnamyl alcohol
-
-
0.025
(R)-pulegone
native enzyme, pH 7.0, 35°C
1.4
(R)-pulegone
recombinant enzyme, pH 7.0, 35°C
0.064
NAD+
-
with 3-methyl-2-buten-1-ol
0.118
NAD+
-
with benzyl alcohol
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3.3
(R)-pulegone
recombinant enzyme, pH 7.0, 35°C
2.8
(S)-pulegone
recombinant enzyme, pH 7.0, 35°C
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0.05
-
purified enzyme, substrate 1-butanol
0.08
-
purified enzyme, substrate 3-methyl-3-buten-1-ol
0.2
-
purified enzyme, substrate 3-methyl-1-butanol
16
-
purified enzyme, substrate 3-chlor-2-buten-1-ol
19.3
-
purified enzyme, in glycine buffer pH 9.4
22
-
purified enzyme, substrate benzyl alcohol
3.7
-
purified enzyme, substrate cinnamyl alcohol
38
-
purified enzyme, substrate aromatic 3-aminobenzyl alcohol
38.8
-
purified enzyme, in bis-Tris-propane-hydrazine buffer pH 9.4
4.6
-
purified enzyme, substrate 2-buten-1-ol
7.7
-
purified enzyme, substrate 3-methyl-2-buten-1-ol
8.8
-
purified enzyme, substrate (R)-(+)-perillyl alcohol
additional information
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about 70,1 unit of enzyme activity defined as amount of enzyme which causes a change in optical density of 0.001 per minute
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7.4
-
reduction of carbonyl group of (S)-carvone
8
-
dehydrogenation of (S)-carveol
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brenda
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UniProt
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brenda
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UniProt
brenda
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physiological function
interruption of the coding region of the Adh1 gene causes resistance to allyl alcohol, deficiency in alcohol dehydrogenase activity, as well as alteration of different physiological parameters related to carbon and energy metabolism, including the ability to use ethanol as a carbon source under aerobic conditions, impaired growth under hypoxic conditions with glucose as the carbon source, and diminished production of ethanol in glucose-containing medium
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36300
2 * 36300, SDS-PAGE, native mass by gel filtration
37000
-
2 * 37000, SDS-PAGE and amino acid sequence analysis
37700
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4 * 37700, SDS-PAGE
38482
2 * 38482, recombinant protein, MALDI TOF-MS, native mass by gel filtration
38487
2 * 38487, recombinant protein, calculated from the deduced amino acid sequence, native mass by gel filtration
74000
-
gel filtration
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dimer
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2 * 37000, SDS-PAGE and amino acid sequence analysis
dimer
2 * 36300, SDS-PAGE, native mass by gel filtration
dimer
2 * 38482, recombinant protein, MALDI TOF-MS, native mass by gel filtration
dimer
2 * 38487, recombinant protein, calculated from the deduced amino acid sequence, native mass by gel filtration
tetramer
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4 * 37700, SDS-PAGE
tetramer
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4 * 37700, SDS-PAGE
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additional information
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isoform ADH1 oxidizes allyl alcohol to toxic acrolein. Use of the reaction to isolate mutations in the ADH1 gene that lead to decreased ADH activity. These yeast may grow more slowly due to slower reduction of acetaldehyde and a higher NADH/NAD+ ratio, which should decrease the oxidation of allyl alcohol
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9.4
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stability at pH 9.4, 25°C much higher than at reactions optimal pH of 10.0
287114
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-70°C, 50-65% ethylene glycol (v/v), frozen in liquid nitrogen, stable for several month
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native enzyme, recombinant enzyme purified using GST-tag
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-
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GST-fusion protein expressed in Escherichia coli BL21
sequence homology with other NADPH-dependent oxidoreductases from plants
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Otsuka, K.
Triphosphopyridine nucleotide-allyl and -ethyl alcohol dehydrogenases from Escherichia coli (preliminary report)
J. Gen. Appl. Microbiol.
4
211-215
1958
Escherichia coli
-
brenda
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
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Malone, V.F.; Chastian, A.J.; Ohlsson, J.T.; Poneleit, L.S.; Nemecek-Marshall, M.; Fall, R.
Characterization of a Pseudomonas putida allylic alcohol dehydrogenase induced by growth on 2-methyl-3-buten-2-ol
Appl. Environ. Microbiol.
65
2622-2630
1999
Pseudomonas putida, Pseudomonas putida MB-1
brenda
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), Nicotiana tabacum
brenda
Zhu, H.; Gonzalez, R.; Bobik, T.A.
Coproduction of acetaldehyde and hydrogen during glucose fermentation by Escherichia coli
Appl. Environ. Microbiol.
77
6441-6450
2011
Saccharomyces cerevisiae
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Corrales Escobosa, A.R.; Rangel Porras, R.A.; Meza Carmen, V.; Gonzalez Hernandez, G.A.; Torres Guzman, J.C.; Wrobel, K.; Wrobel, K.; Roncero, M.I.; Gutierrez Corona, J.F.
Fusarium oxysporum Adh1 has dual fermentative and oxidative functions and is involved in fungal virulence in tomato plants
Fungal Genet. Biol.
48
886-895
2011
Fusarium oxysporum (E3UTQ9)
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