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Information on EC 1.1.1.192 - long-chain-alcohol dehydrogenase
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1.1.1.192 long-chain-alcohol dehydrogenaseIUBMB Comments
Hexadecanol is a good substrate.
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Word Map
- 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
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
+
2
+
=
+
2
+
2
Synonyms
long-chain alcohol dehydrogenase, long-chain dehydrogenase, fatty alcohol oxidoreductase, long-chain-alcohol dehydrogenase, nad+-dependent secondary alcohol dehydrogenase, 
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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
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
(2S)-5-hydroxy-2-aminovaleric acid + NAD+ + H2O
(2S)-2-amino-5-oxopentanoate + NADH
-
no activity with the (2R)-isomer
-
-
?
1-octanol + 2 NADP+ + H2O
octanoic acid + 2 NADPH + 2 H+
-
-
-
r
10,12-dihydroxyoctadecanoic acid + NADP+ + H2O
? + NADPH
-
the reaction is catalyzed by mutant enzyme D37S/V39S
-
-
?
10-hydroxyoctadecanoic acid + NAD+ + H2O
9-(nonanoyloxy)nonanoic acid + NADH
-
-
-
-
?
10-hydroxyoctadecanoic acid + NADP+ + H2O
9-(nonanoyloxy)nonanoic acid + NADPH
-
the reaction is catalyzed by mutant enzyme D37S/A38R/V39S/T15I
-
-
?
decanal + NAD+ + H+
decanoic acid + NADH
about 10% of the activity with 1-octanol
-
-
r
dodecanal + NAD+ + H+
dodecanoic acid + NADH
about 10% of the activity with 1-octanol
-
-
r
glycerol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 45% of the activity with ethanol
-
-
r
isopropanol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 15% of the activity with 1-octanol
-
-
r
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
(4S)-5-oxo-L-leucine + NADH
-
enzyme reaction is part of the biosynthesis of (2S,4S)-4-methylproline
-
-
r
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 45% of the activity with ethanol
-
-
r
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 5% of the activity with 1-octanol
-
-
r
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 45% of the activity with ethanol
-
-
r
1,3-propanediol + 2 NAD+ + H2O
? + 2 NADH + 2 H+
about 5% of the activity with 1-octanol
-
-
r
1-decanol + 2 NAD+ + H2O
decanoic acid + 2 NADH + 2 H+
about 20% of the activity with ethanol
-
-
r
1-decanol + 2 NAD+ + H2O
decanoic acid + 2 NADH + 2 H+
about 50% of the activity with 1-octanol
-
-
r
1-decanol + 2 NAD+ + H2O
decanoic acid + 2 NADH + 2 H+
about 20% of the activity with ethanol
-
-
r
1-decanol + 2 NAD+ + H2O
decanoic acid + 2 NADH + 2 H+
about 50% of the activity with 1-octanol
-
-
r
1-dodecanol + 2 NAD+ + H2O
dodecanoic acid + 2 NADH + 2 H+
about 17% of the activity with ethanol
-
-
r
1-dodecanol + 2 NAD+ + H2O
dodecanoic acid + 2 NADH + 2 H+
about 30% of the activity with 1-octanol
-
-
r
1-dodecanol + 2 NAD+ + H2O
dodecanoic acid + 2 NADH + 2 H+
about 17% of the activity with ethanol
-
-
r
1-dodecanol + 2 NAD+ + H2O
dodecanoic acid + 2 NADH + 2 H+
about 30% of the activity with 1-octanol
-
-
r
1-eicosanol + 2 NAD+ + H2O
eicosanoic acid + 2 NADH + 2 H+
about 25% of the activity with 1-octanol
-
-
r
1-eicosanol + 2 NAD+ + H2O
eicosanoic acid + 2 NADH + 2 H+
about 3% of the activity with ethanol
-
-
r
1-eicosanol + 2 NAD+ + H2O
eicosanoic acid + 2 NADH + 2 H+
about 3% of the activity with ethanol
-
-
r
1-eicosanol + 2 NAD+ + H2O
eicosanoic acid + 2 NADH + 2 H+
about 25% of the activity with 1-octanol
-
-
r
1-hexadecanol + 2 NAD+ + H2O
hexadecanoic acid + 2 NADH + 2 H+
about 10% of the activity with ethanol
-
-
r
1-hexadecanol + 2 NAD+ + H2O
hexadecanoic acid + 2 NADH + 2 H+
about 25% of the activity with 1-octanol
-
-
r
1-octacosanol + 2 NAD+ + H2O
octacosanoic acid + 2 NADH + 2 H+
about 40% of the activity with ethanol
-
-
r
1-octacosanol + 2 NAD+ + H2O
octacosanoic acid + 2 NADH + 2 H+
about 5% of the activity with 1-octanol
-
-
r
1-octadecanol + 2 NAD+ + H2O
octadecanoic acid + 2 NADH + 2 H+
about 15% of the activity with 1-octanol
-
-
r
1-octadecanol + 2 NAD+ + H2O
octadecanoic acid + 2 NADH + 2 H+
about 5% of the activity with ethanol
-
-
r
1-octanol + 2 NAD+ + H2O
octanoic acid + 2 NADH + 2 H+
-
-
-
r
1-tetracosanol + 2 NAD+ + H2O
tetracosanoic acid + 2 NADH + 2 H+
about 10% of the activity with 1-octanol
-
-
r
1-tetracosanol + 2 NAD+ + H2O
tetracosanoic acid + 2 NADH + 2 H+
about 30% of the activity with ethanol
-
-
r
1-tetradecanol + 2 NAD+ + H2O
tetradecanoic acid + 2 NADH + 2 H+
about 15% of the activity with ethanol
-
-
r
1-tetradecanol + 2 NAD+ + H2O
tetradecanoic acid + 2 NADH + 2 H+
about 30% of the activity with 1-octanol
-
-
r
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
enzyme also uses formaldehyde and short chain aliphatic alcohols
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
C17-C-19 alcohols do not serve as a good substrate
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
maximum activity on C14 alcohol
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
C8-C16
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
peroxisomal enzyme is participating in fatty acid degradation
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
microsomal and mitochondrial enzyme may have an indispensable role in lipid biosynthesis
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
long chain n-alcanols up to C12
-
-
r
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
maximal activity with decanol
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
C10-C18
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
enzyme may play an important role in regulating the cellular levels of ether-linked lipids
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
C6-C18 alcohols
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
maximal activity with decanol
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
C17-C-19 alcohols do not serve as a good substrate
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
peroxisomal enzyme is participating in fatty acid degradation
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
microsomal and mitochondrial enzyme may have an indispensable role in lipid biosynthesis
-
-
?
octanal + NAD+ + H2O
octanoic acid + NADH + H+
-
-
-
r
octanal + NAD+ + H2O
octanoic acid + NADH + H+
-
-
-
r
additional information
?
-
substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
-
-
?
additional information
?
-
substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
-
-
?
additional information
?
-
substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
-
-
?
additional information
?
-
substrates are a broad range of alkyl alcohols from ethanol to 1-triacontanol
-
-
?
additional information
?
-
-
the wild type enzyme shows no activity with NADP+
-
-
-
additional information
?
-
-
stereospecific abstraction of the 5pro-S hydrogen
-
-
?
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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
(2S,4S)-5-hydroxyleucine + NAD+ + H2O
(4S)-5-oxo-L-leucine + NADH
-
enzyme reaction is part of the biosynthesis of (2S,4S)-4-methylproline
-
-
r
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
enzyme also uses formaldehyde and short chain aliphatic alcohols
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
peroxisomal enzyme is participating in fatty acid degradation
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
microsomal and mitochondrial enzyme may have an indispensable role in lipid biosynthesis
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
enzyme may play an important role in regulating the cellular levels of ether-linked lipids
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
peroxisomal enzyme is participating in fatty acid degradation
-
-
?
long-chain alcohol + NAD+ + H2O
long-chain carboxylate + NADH
-
microsomal and mitochondrial enzyme may have an indispensable role in lipid biosynthesis
-
-
?
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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
-
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
0.013
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