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Information on EC 1.1.1.54 - allyl-alcohol dehydrogenase
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1.1.1.54 allyl-alcohol dehydrogenaseIUBMB Comments
Also acts on saturated primary alcohols.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
ADH1, allyl-ADH, NtRed-1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
allyl-alcohol:NADP+ oxidoreductase
Also acts on saturated primary alcohols.
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CAS REGISTRY NUMBER
COMMENTARY
9028-58-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(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)-pulegone + NADP+
(1S,4S)-isomenthone + (1S,4R)-menthone + NADPH + H+
recombinant enzyme
-
-
?
saturated primary alcohols + NADP+
?
-
i.e. ethyl alcohol, n-propyl alcohol, n-butyl acohol, isobutyl alcohol, propylene glycol
-
-
r
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
-
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
-
specific for the (S)-isomer of secondary allylic alcohols, several stereomers tested for activity in both reaction directions
-
-
r
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-methyl-2-buten-1-al
-
product inhibition, therefore the product must be removed via reaction with hydrazine during the enzyme assay
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
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
Show AA Sequence and Transmembrane Helices (183 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9.4
-
stability at pH 9.4, 25°C much higher than at reactions optimal pH of 10.0
287114
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, 50-65% ethylene glycol (v/v), frozen in liquid nitrogen, stable for several month
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (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
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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