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Information on EC 1.1.1.54 - allyl-alcohol dehydrogenase for references in articles please use BRENDA:EC1.1.1.54
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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
ADH1, allyl-ADH, NtRed-1,
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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
-
allyl alcohol + NADP+ = acrolein + NADPH + H+
also acts on saturated primary alcohols
-
-
-
allyl alcohol + NADP+ = acrolein + NADPH + H+
3-methyl-2-buten-1-ol-dependent inducible activity
-
-
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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)-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
-
-
?
2,3-butylene glycol + NADP+
?
-
-
-
-
r
2-buten-2-ol + NADPH
but-2-enal
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
allyl alcohol + NADP+
acrolein + NADPH
allyl alcohol + NADP+
acrolein + NADPH + H+
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
?
-
(R)-carvone, (S)-carvone, (1S,5S)-verbenone, (1R,5R)-verbenone, oxalacetic acid, and (2S,4S)-carveol do not serve as substrate
-
-
-
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
-
-
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
-
-
-
-
?
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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+
-
specific for
NADP+
-
activity 4times greater than with NAD+
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additional information
-
is sensitive against metal ion chelators
additional information
-
is not sensitive against metal ion chelators
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3-methyl-2-buten-1-al
-
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
-
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
3.7
-
purified enzyme, substrate cinnamyl alcohol
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
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
38
-
purified enzyme, substrate aromatic 3-aminobenzyl alcohol
38.8
-
purified enzyme, in bis-Tris-propane-hydrazine buffer pH 9.4
additional information
-
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
brenda
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brenda
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brenda
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brenda
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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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AK1A1_BOVIN
325
0
36617
Swiss-Prot
AK1A1_CRIGR
324
0
36510
Swiss-Prot
AK1A1_HUMAN
325
0
36573
Swiss-Prot
AK1A1_MOUSE
325
0
36587
Swiss-Prot
AK1A1_PIG
325
0
36582
Swiss-Prot
AK1A1_PONAB
325
0
36390
Swiss-Prot
AK1A1_RAT
325
0
36506
Swiss-Prot
AK1BA_HUMAN
316
0
36020
Swiss-Prot
AK1BF_HUMAN
316
0
36537
Swiss-Prot
ALDR_RABIT
316
0
35763
Swiss-Prot
ALDR_RAT
316
0
35797
Swiss-Prot
ALDR_BOVIN
315
0
35919
Swiss-Prot
ALDR_HUMAN
316
0
35853
Swiss-Prot
ALDR_MOUSE
316
0
35732
Swiss-Prot
ALDR_PIG
316
0
35868
Swiss-Prot
A0A2G9HCR3_9LAMI
251
0
27057
TrEMBL
A0A251VQR8_HELAN
343
0
37822
TrEMBL
A0A2G9HSW9_9LAMI
346
0
38319
TrEMBL
DBR_TOBAC
343
0
38088
Swiss-Prot
E3UTQ9_FUSOX
353
0
37530
TrEMBL
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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
-
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
-
2 * 37000, SDS-PAGE and amino acid sequence analysis
dimer
2 * 36300, SDS-PAGE, native mass by gel filtration; 2 * 38482, recombinant protein, MALDI TOF-MS, native mass by gel filtration; 2 * 38487, recombinant protein, calculated from the deduced amino acid sequence, native mass by gel filtration
tetramer
-
4 * 37700, SDS-PAGE
tetramer
-
4 * 37700, SDS-PAGE
-
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additional information
-
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
-
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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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
brenda
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, Nicotiana tabacum (Q9SLN8)
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
brenda
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)
brenda
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1.1.1.54 allyl-alcohol dehydrogenase
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