Information on EC 1.1.1.54 - allyl-alcohol dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.54
-
RECOMMENDED NAME
GeneOntology No.
allyl-alcohol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
allyl alcohol + NADP+ = acrolein + NADPH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
detoxification of reactive carbonyls in chloroplasts
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-
SYSTEMATIC NAME
IUBMB Comments
allyl-alcohol:NADP+ oxidoreductase
Also acts on saturated primary alcohols.
CAS REGISTRY NUMBER
COMMENTARY hide
9028-58-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
strain MB-1
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-
Manually annotated by BRENDA team
strain MB-1
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2S,4S)-carveol + NADP+
(S)-carvone + NADPH
show the reaction diagram
-
-
-
r
(R)-pulegone + NADP+
(1R,4R)-isomenthone + (1R,4S)-menthone + NADPH + H+
show the reaction diagram
recombinant enzyme
reaction is not stereospecific as with the native enzyme
-
?
(R)-pulegone + NADP+
(1R,4R)-isomenthone + NADPH + H+
show the reaction diagram
native enzyme
-
-
?
(S)-carvone + NADPH
(2S,4S)-carveol + NADP+
show the reaction diagram
-
-
-
r
(S)-pulegone + NADP+
(1S,4S)-isomenthone + (1S,4R)-menthone + NADPH + H+
show the reaction diagram
recombinant enzyme
-
-
?
2,3-butylene glycol + NADP+
?
show the reaction diagram
-
-
-
-
r
2-buten-2-ol + NADPH
but-2-enal
show the reaction diagram
3-chloro-2-buten-1-ol + NADP+
3-chloro-2-butenaldehyde + NADPH
show the reaction diagram
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
show the reaction diagram
allyl alcohol + NADP+
acrolein + NADPH
show the reaction diagram
allyl alcohol + NADP+
acrolein + NADPH + H+
show the reaction diagram
cinnamyl alcohol + NADP+
cinnamyl aldehyde + NADPH
show the reaction diagram
saturated primary alcohols + NADP+
?
show the reaction diagram
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i.e. ethyl alcohol, n-propyl alcohol, n-butyl acohol, isobutyl alcohol, propylene glycol
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-
r
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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-
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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
3-methyl-2-buten-1-ol + NAD+
3-methyl-2-buten-1-al + NADH
show the reaction diagram
allyl alcohol + NADP+
acrolein + NADPH
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD(P)H
NAD+
-
exhibits less than 5% of the activity with NADP+
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
cyanide
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dipyridyl
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dithiothreitol
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N-ethylmaleimide
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p-chloromercuribenzoate
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can be overcome by addition of gluthathione
additional information
-
not: monoiodoacetate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012
(R)-(+)-perillyl alcohol
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0.025 - 1.4
(R)-pulegone
8.3
(S)-pulegone
recombinant enzyme, pH 7.0, 35C
1.1
1-butanol
-
-
0.044
2-Buten-1-ol
-
-
0.011
3-aminobenzyl alcohol
-
-
0.007
3-chloro-2-buten-1-ol
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-
0.27
3-methyl-1-butanol
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-
0.04
3-methyl-2-buten-1-ol
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-
1.7
3-methyl-3-buten-1-ol
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5
allyl-alcohol
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-
0.007
benzyl alcohol
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-
0.036
cinnamyl alcohol
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0.064 - 0.118
NAD+
0.04
NADP+
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-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.3
(R)-pulegone
Nicotiana tabacum
Q9SLN8
recombinant enzyme, pH 7.0, 35C
2.8
(S)-pulegone
Nicotiana tabacum
Q9SLN8
recombinant enzyme, pH 7.0, 35C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.05
-
purified enzyme, substrate 1-butanol
0.08
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purified enzyme, substrate 3-methyl-3-buten-1-ol
0.2
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purified enzyme, substrate 3-methyl-1-butanol
3.7
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purified enzyme, substrate cinnamyl alcohol
4.6
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purified enzyme, substrate 2-buten-1-ol
7.7
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purified enzyme, substrate 3-methyl-2-buten-1-ol
8.8
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purified enzyme, substrate (R)-(+)-perillyl alcohol
16
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purified enzyme, substrate 3-chlor-2-buten-1-ol
19.3
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purified enzyme, in glycine buffer pH 9.4
22
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purified enzyme, substrate benzyl alcohol
38
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purified enzyme, substrate aromatic 3-aminobenzyl alcohol
38.8
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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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4
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for reduction
7.4
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reduction of carbonyl group of (S)-carvone
7.7
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in Tris-buffer
8
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dehydrogenation of (S)-carveol
10
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for oxidation
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
assay temperature
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36300
2 * 36300, SDS-PAGE, native mass by gel filtration
37000
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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
151000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.4
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stability at pH 9.4, 25C much higher than at reactions optimal pH of 10.0
287114
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 50-65% ethylene glycol (v/v), frozen in liquid nitrogen, stable for several month
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme, recombinant enzyme purified using GST-tag
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GST-fusion protein expressed in Escherichia coli BL21
sequence homology with other NADPH-dependent oxidoreductases from plants
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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