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Information on EC 1.1.1.192 - long-chain-alcohol dehydrogenase
for references in articles please use BRENDA:EC1.1.1.192
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.192 long-chain-alcohol dehydrogenase
IUBMB Comments
Hexadecanol is a good substrate.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.1.1.192
- dehydrogenases
- sls
-
zinc-dependent
- d-mannitol
-
2-dehydrogenase
- d-fructose
-
glutathione-dependent
-
hydride
- nostoc
-
beta-oxidation
-
nose
- n-alkanes
- glycerol-3-phosphate
Reaction Schemes
show+
2
+
=
+
2
+
2
Synonyms
long-chain alcohol dehydrogenase, long-chain dehydrogenase, fatty alcohol oxidoreductase, long-chain-alcohol dehydrogenase, nad+-dependent secondary alcohol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH1
ADH2
dehydrogenase, long-chain alcohol
-
-
-
-
fatty alcohol oxidoreductase
-
-
-
-
long-chain alcohol dehydrogenase
-
-
-
-
long-chain alkyl alcohol dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a long-chain alcohol + 2 NAD+ + H2O = a long-chain carboxylate + 2 NADH + 2 H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
long-chain-alcohol:NAD+ oxidoreductase
Hexadecanol is a good substrate.
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CAS REGISTRY NUMBER
COMMENTARY
76774-36-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S)-5-hydroxy-2-aminovaleric acid + NAD+ + H2O
(2S)-2-amino-5-oxopentanoate + NADH
-
Substrates: no activity with the (2R)-isomer
Products: -
Products: -
?
1-docosanol + NAD+ + H2O
behenic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
1-tetracosanol + NAD+ + H2O
lignoceric acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
10,12-dihydroxyoctadecanoic acid + NAD+ + H2O
?
-
Substrates: -
Products: -
Products: -
?
10,12-dihydroxyoctadecanoic acid + NADP+ + H2O
? + NADPH
-
Substrates: the reaction is catalyzed by mutant enzyme D37S/V39S
Products: -
Products: -
?
10-hydroxyoctadecanoic acid + NAD+ + H2O
9-(nonanoyloxy)nonanoic acid + NADH
-
Substrates: -
Products: -
Products: -
?
10-hydroxyoctadecanoic acid + NADP+ + H2O
9-(nonanoyloxy)nonanoic acid + NADPH
-
Substrates: the reaction is catalyzed by mutant enzyme D37S/A38R/V39S/T15I
Products: -
Products: -
?
12-hydroxydodecanoic acid + NAD+ + H2O
? + NADH
-
Substrates: -
Products: -
Products: -
?
12-hydroxyoctadecanoic acid + NAD+ + H2O
? + NADH
-
Substrates: -
Products: -
Products: -
?
decanal + NAD+ + H+
decanoic acid + NADH
Substrates: about 10% of the activity with 1-octanol
Products: -
Products: -
r
dodecanal + NAD+ + H+
dodecanoic acid + NADH
Substrates: about 10% of the activity with 1-octanol
Products: -
Products: -
r
glycerol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
Substrates: about 45% of the activity with ethanol
Products: -
Products: -
r
isopropanol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
Substrates: about 15% of the activity with 1-octanol
Products: -
Products: -
r
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
(4S)-5-oxo-L-leucine + NADH
-
Substrates: enzyme reaction is part of the biosynthesis of (2S,4S)-4-methylproline
Products: -
Products: -
r
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
(4S)-5-oxo-L-leucine + NADH
-
Substrates: -
Products: -
Products: -
r
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
Substrates: about 45% of the activity with ethanol
Products: -
Products: -
r
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
Substrates: about 5% of the activity with 1-octanol
Products: -
Products: -
r
1-decanol + 2 NAD+ + H2O
decanoic acid + 2 NADH + 2 H+
Substrates: about 20% of the activity with ethanol
Products: -
Products: -
r
1-decanol + 2 NAD+ + H2O
decanoic acid + 2 NADH + 2 H+
Substrates: about 50% of the activity with 1-octanol
Products: -
Products: -
r
1-decanol + 2 NAD+ + H2O
decanoic acid + 2 NADH + 2 H+
Substrates: about 20% of the activity with ethanol
Products: -
Products: -
r
1-decanol + 2 NAD+ + H2O
decanoic acid + 2 NADH + 2 H+
Substrates: about 50% of the activity with 1-octanol
Products: -
Products: -
r
1-dodecanol + 2 NAD+ + H2O
dodecanoic acid + 2 NADH + 2 H+
Substrates: about 17% of the activity with ethanol
Products: -
Products: -
r
1-dodecanol + 2 NAD+ + H2O
dodecanoic acid + 2 NADH + 2 H+
Substrates: about 30% of the activity with 1-octanol
Products: -
Products: -
r
1-dodecanol + 2 NAD+ + H2O
dodecanoic acid + 2 NADH + 2 H+
Substrates: about 17% of the activity with ethanol
Products: -
Products: -
r
1-dodecanol + 2 NAD+ + H2O
dodecanoic acid + 2 NADH + 2 H+
Substrates: about 30% of the activity with 1-octanol
Products: -
Products: -
r
1-eicosanol + 2 NAD+ + H2O
eicosanoic acid + 2 NADH + 2 H+
Substrates: about 3% of the activity with ethanol
Products: -
Products: -
r
1-eicosanol + 2 NAD+ + H2O
eicosanoic acid + 2 NADH + 2 H+
Substrates: about 25% of the activity with 1-octanol
Products: -
Products: -
r
1-hexadecanol + 2 NAD+ + H2O
hexadecanoic acid + 2 NADH + 2 H+
Substrates: about 10% of the activity with ethanol
Products: -
Products: -
r
1-hexadecanol + 2 NAD+ + H2O
hexadecanoic acid + 2 NADH + 2 H+
Substrates: about 25% of the activity with 1-octanol
Products: -
Products: -
r
1-hexadecanol + 2 NAD+ + H2O
hexadecanoic acid + 2 NADH + 2 H+
Substrates: about 10% of the activity with ethanol
Products: -
Products: -
r
1-octacosanol + 2 NAD+ + H2O
octacosanoic acid + 2 NADH + 2 H+
Substrates: about 40% of the activity with ethanol
Products: -
Products: -
r
1-octacosanol + 2 NAD+ + H2O
octacosanoic acid + 2 NADH + 2 H+
Substrates: about 5% of the activity with 1-octanol
Products: -
Products: -
r
1-octadecanol + 2 NAD+ + H2O
octadecanoic acid + 2 NADH + 2 H+
Substrates: about 5% of the activity with ethanol
Products: -
Products: -
r
1-octadecanol + 2 NAD+ + H2O
octadecanoic acid + 2 NADH + 2 H+
Substrates: about 15% of the activity with 1-octanol
Products: -
Products: -
r
1-octadecanol + 2 NAD+ + H2O
octadecanoic acid + 2 NADH + 2 H+
Substrates: about 5% of the activity with ethanol
Products: -
Products: -
r
1-octanol + 2 NAD+ + H2O
octanoic acid + 2 NADH + 2 H+
-
Substrates: -
Products: -
Products: -
r
1-octanol + 2 NAD+ + H2O
octanoic acid + 2 NADH + 2 H+
Substrates: -
Products: -
Products: -
r
1-octanol + 2 NAD+ + H2O
octanoic acid + 2 NADH + 2 H+
Substrates: -
Products: -
Products: -
r
1-octanol + 2 NADP+ + H2O
octanoic acid + 2 NADPH + 2 H+
Substrates: -
Products: -
Products: -
r
1-octanol + 2 NADP+ + H2O
octanoic acid + 2 NADPH + 2 H+
Substrates: -
Products: -
Products: -
r
1-tetracosanol + 2 NAD+ + H2O
tetracosanoic acid + 2 NADH + 2 H+
Substrates: about 30% of the activity with ethanol
Products: -
Products: -
r
1-tetracosanol + 2 NAD+ + H2O
tetracosanoic acid + 2 NADH + 2 H+
Substrates: about 10% of the activity with 1-octanol
Products: -
Products: -
r
1-tetradecanol + 2 NAD+ + H2O
tetradecanoic acid + 2 NADH + 2 H+
Substrates: about 15% of the activity with ethanol
Products: -
Products: -
r
1-tetradecanol + 2 NAD+ + H2O
tetradecanoic acid + 2 NADH + 2 H+
Substrates: about 30% of the activity with 1-octanol
Products: -
Products: -
r
1-tetradecanol + 2 NAD+ + H2O
tetradecanoic acid + 2 NADH + 2 H+
Substrates: about 15% of the activity with ethanol
Products: -
Products: -
r
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: enzyme also uses formaldehyde and short chain aliphatic alcohols
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: C17-C-19 alcohols do not serve as a good substrate
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: maximum activity on C14 alcohol
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: C8-C16
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: peroxisomal enzyme is participating in fatty acid degradation
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: microsomal and mitochondrial enzyme may have an indispensable role in lipid biosynthesis
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: long chain n-alcanols up to C12
Products: -
Products: -
r
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: maximal activity with decanol
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: C10-C18
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: enzyme may play an important role in regulating the cellular levels of ether-linked lipids
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: C6-C18 alcohols
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: maximal activity with decanol
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: C17-C-19 alcohols do not serve as a good substrate
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: peroxisomal enzyme is participating in fatty acid degradation
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: microsomal and mitochondrial enzyme may have an indispensable role in lipid biosynthesis
Products: -
Products: -
?
n-butanol + NAD+ + H2O
n-butanal + NADH
-
Substrates: -
Products: -
Products: -
?
n-hexanol + NAD+ + H2O
n-hexanal + NADH
-
Substrates: -
Products: -
Products: -
?
n-pentanol + NAD+ + H2O
n-pentanal + NADH
-
Substrates: -
Products: -
Products: -
?
n-propanol + NAD+ + H2O
n-propanal + NADH
-
Substrates: -
Products: -
Products: -
?
octanal + NAD+ + H2O
octanoic acid + NADH + H+
Substrates: -
Products: -
Products: -
r
octanal + NAD+ + H2O
octanoic acid + NADH + H+
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
Products: -
Products: -
?
additional information
?
-
Substrates: substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
Products: -
Products: -
?
additional information
?
-
-
Substrates: the wild type enzyme shows no activity with NADP+
Products: -
Products: -
?
additional information
?
-
-
Substrates: stereospecific abstraction of the 5pro-S hydrogen
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
(4S)-5-oxo-L-leucine + NADH
-
Substrates: enzyme reaction is part of the biosynthesis of (2S,4S)-4-methylproline
Products: -
Products: -
r
1-docosanol + NAD+ + H2O
behenic acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
1-tetracosanol + NAD+ + H2O
lignoceric acid + NADH + H+
-
Substrates: -
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: enzyme also uses formaldehyde and short chain aliphatic alcohols
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: peroxisomal enzyme is participating in fatty acid degradation
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: microsomal and mitochondrial enzyme may have an indispensable role in lipid biosynthesis
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: enzyme may play an important role in regulating the cellular levels of ether-linked lipids
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: peroxisomal enzyme is participating in fatty acid degradation
Products: -
Products: -
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
Substrates: microsomal and mitochondrial enzyme may have an indispensable role in lipid biosynthesis
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Zinc
Zn2+
additional information
additional information
enzyme contains neither Fe nor other metals, and Fe is not required for the activity, although sequence analysis reveals that ADH1 belongs to the Fe-containing/activated long-chain alcohol dehydrogenases
additional information
enzyme contains neither Fe nor other metals, and Fe is not required for the activity, although sequence analysis reveals that ADH1 belongs to the Fe-containing/activated long-chain alcohol dehydrogenases
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Al3+
1 mM, 14.7% residual activity; 1 mM, 18.9% residual activity
Co2+
1 mM, 51.9% residual activity; 1 mM, 68.7% residual activity
Cu2+
1 mM, 14.0% residual activity; 1 mM, 44.2% residual activity
K+
1 mM, 70.3% residual activity; 1 mM, 82.3% residual activity
Mg2+
1 mM, 0.3% residual activity; 1 mM, 74.3% residual activity
Mn2+
1 mM, 14.3% residual activity; 1 mM, 23.4% residual activity
Ni2+
1 mM, 18.2% residual activity; 1 mM, 72.7% residual activity
sodium dodecylsulfate
1 mM, 3% residual activity; 1 mM, no residual activity
Zn2+
1 mM, 14.1% residual activity; 1 mM, 30.5% residual activity
additional information
-
inhibition differs for ethanol and formaldehyde as substrates
-
additional information
-
not: pyrazole, sodium azide, AMP, ATP, quinacrine, iodoacetate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Sjogren-Larsson Syndrome
Cerebral MRI and spectroscopy in Sjögren-Larsson syndrome: case report.
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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
283.1
NADP+
cosubstrate 1-octanol, pH 8.0, 60°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
117.9
NADP+
cosubstrate 1-octanol, pH 8.0, 60°C
0.0021
10,12-dihydroxyoctadecanoic acid
-
mutant enzyme D37S/A38R/V39S/T15I, with NAD+ as cosubstrate, pH and temperature not specified in the publication
0.0035
10,12-dihydroxyoctadecanoic acid
-
wild type enzyme, with NAD+ as cosubstrate, pH and temperature not specified in the publication
0.012
10,12-dihydroxyoctadecanoic acid
-
mutant enzyme D37S/V39S, with NAD+ as cosubstrate, pH and temperature not specified in the publication
0.0014
10-hydroxyoctadecanoic acid
-
wild type enzyme, with NAD+ as cosubstrate, pH and temperature not specified in the publication
0.0014
10-hydroxyoctadecanoic acid
-
mutant enzyme D37S/V39S, with NAD+ as cosubstrate, pH and temperature not specified in the publication
0.013
10-hydroxyoctadecanoic acid
-
mutant enzyme D37S/A38R/V39S/T15I, with NAD+ as cosubstrate, pH and temperature not specified in the publication
0.00061
12-hydroxyoctadecanoic acid
-
wild type enzyme, with NAD+ as cosubstrate, pH and temperature not specified in the publication
0.0015
12-hydroxyoctadecanoic acid
-
mutant enzyme D37S/V39S, with NAD+ as cosubstrate, pH and temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
50
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line Links Show AA Sequence and Transmembrane Helices (160 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
41664
8 * 45000, SDS-PAGE, 8 * 41664, calculated
45000
8 * 45000, SDS-PAGE, 8 * 41664, calculated
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
octamer
additional information
octamer
8 * 45000, SDS-PAGE, 8 * 41664, calculated
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 1.0 M trisodium citrate dihydrate at pH 6.5
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D37S/A38R/V39S
-
the mutant has preferred activity with NADP+ and shows increased catalytic efficiency compared to the wild type enzyme
D37S/V39S
-
the mutant has also activity with NADP+ and shows increased catalytic efficiency compared to the wild type enzyme
T15I/D37S/A38R/V39S
-
the mutant shows about 10fold increased catalytic efficiency with 10-hydroxyoctadecanoic acid and has 1800fold increase in catalytic efficiency for NADP+ compared to the wild type enzyme
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 58
-
the soluble enzyme has half-lives of 11.9, 7.8, 5.4 and 1.8 min at 4°C, 25°C, 40°C, and 58°C, respectively. The enzyme immobilized on 6BCL agarose beads activated with glyoxyl groups has a half-life of 136 min at 40°C. The enzyme immobilized on 6BCL agarose beads activated with glyoxyl groups and polyethylenimine 25000 has half-lives of 364 and 131 min at 40°C and 58°C, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithiothreitol, 2 mM, no stabilization, crude extract
ethylene glycol, 20% w/w, no stabilization, crude extract
solubilization with 1% Tween 80 or Triton X-100 at 4C stimulates inactivation, crude extract
solubilization with 1% Tween 80 or Triton X-100 at 4C stimulates inactivation, crude extract
-
solubilization with 1% Tween 80 or Triton X-100 at 4C stimulates inactivation, crude extract
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene nosE, overexpression in Escherichia coli BL21(DE3) as N-terminally His-tagged enzyme
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van Ophem, P.W.; Van Beeumen, J.; Duine, J.A.
NAD-linked, factor-dependent formaldehyde dehydrogenase or trimeric, zinc-containing, long-chain alcohol dehydrogenase from Amycolatopsis methanolica
Eur. J. Biochem.
206
511-518
1992
Amycolatopsis methanolica
brenda
Lee, T.C.
Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver
J. Biol. Chem.
254
2892-2896
1979
Rattus norvegicus
brenda
Ueda, M.; Tanaka, A.
Long-chain alcohol dehydrogenase of Candida yeast
Methods Enzymol.
188
171-175
1990
Candida tropicalis, Yarrowia lipolytica
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Yamada, T.; Nawa, H.; Kawamoto, S.; Tanaka, A.; Fukui, S.
Subcellular localization of long-chain alcohol dehydrogenase and aldehyde dehydrogenase in n-alkane-grown Candida tropicalis
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Candida tropicalis
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Ribas de Pouplana, L.; Atrian, S.; Gonzalez-Duarte, R.; Fothergill-Gilmore, L.A.; Kelly, S.M.; Price, N.C.
Structural properties of long- and short-chain alcohol dehydrogenases. Contribution of NAD+ to stability
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Equus caballus
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Nagashima, H.; Inoue, J.; Sasaki, E.; Yamamoto, S.; Sasaki, Y.; Yamauchi-Inomata, Y.; Harayama, S.
Long-chain n-alkanol dehydrogenase from Pseudomonas putida
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Pseudomonas putida
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Eklund, H.; Nordstrom, B.; Zeppezauer, E.; Soderlund, G.; Ohlsson, I.; Boiwe, T.; Soderberg, B.O.; Tapia, O.; Branden, C.I.; Akeson, A.
Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution
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Equus caballus
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Luesch, H.; Hoffmann, D.; Hevel, J.M.; Becker, J.E.; Golakoti, T.; Moore, R.E.
Biosynthesis of 4-methylproline in cyanobacteria: cloning of nosE and nosF genes and biochemical characterization of the encoded dehydrogenase and reductase activities
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Nostoc sp.
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Liu, X.; Dong, Y.; Zhang, J.; Zhang, A.; Wang, L.; Feng, L.
Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2
Microbiology
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Geobacillus thermodenitrificans (A4IP64), Geobacillus thermodenitrificans (A4ISB9), Geobacillus thermodenitrificans NG80-2 (A4IP64), Geobacillus thermodenitrificans NG80-2 (A4ISB9)
brenda
Ottone, C.; Bernal, C.; Serna, N.; Illanes, A.; Wilson, L.
Enhanced long-chain fatty alcohol oxidation by immobilization of alcohol dehydrogenase from S. cerevisiae
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Saccharomyces cerevisiae
brenda
Seo, E.J.; Kim, H.J.; Kim, M.J.; Kim, J.S.; Park, J.B.
Cofactor specificity engineering of a long-chain secondary alcohol dehydrogenase from Micrococcus luteus for redox-neutral biotransformation of fatty acids
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Micrococcus luteus
brenda
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