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Information on EC 1.1.1.71 - alcohol dehydrogenase [NAD(P)+]
for references in articles please use BRENDA:EC1.1.1.71
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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
1.1.1.71 alcohol dehydrogenase [NAD(P)+]
IUBMB Comments
Reduces aliphatic aldehydes of carbon chain length from 2 to 14, with greatest activity on C4, C6 and C8 aldehydes; also reduces retinal to retinol.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 1.1.1.71
-
retinoids
- thermoanaerobacter
- all-trans-retinaldehyde
-
retinyl
-
ethanolicus
- all-trans-retinol
-
r-1-phenylethanol
-
cyp26a1
- akr1b10
Reaction Schemes
showSynonyms
dhrs3, retinaldehyde reductase, tesadh, retsdr1, nadph-dependent alcohol dehydrogenase, adh12, nad(p)h-dependent adh, retinol-active alcohol dehydrogenase, nad(p)h-dependent aldehyde reductase, tsib_0319, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH
ADH2
Adh319
AdhA
alcohol dehydrogenase
aldehyde reductase (NADPH/NADH)
-
-
-
-
HvADH2
HVO_B0071
NAD(P)+-dependent alcohol dehydrogenase
NAD(P)H-dependent aldehyde reductase
NADPH-dependent ADHA
NADPH-dependent alcohol dehydrogenase
PH0743
PhADH
RADH
retinal reductase
-
-
-
-
TsAdh319
Tsib_0319
VNG_2617G
YqhD
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
-
-
-
-
a primary alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
enzyme is stereospecific for the pro-R hydride of NADPH
-
a primary alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
enzyme is stereospecific for the pro-R hydride of NADPH
-
a primary alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
the human pancreas protein 2 has a retinal reductase activity
a primary alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
the enzyme is an aldo-keto reductase
-
a primary alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
the defence-related alcohol dehydrogenase DRD-1 is an alcohol:NADP+ oxidoreductase with preference for various aromatic and aliphatic aldehydes
a primary alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
enzyme is stereospecific for the pro-R hydride of NADPH
-
-
a primary alcohol + NAD(P)+ = an aldehyde + NAD(P)H + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
alcohol:NAD(P)+ oxidoreductase
Reduces aliphatic aldehydes of carbon chain length from 2 to 14, with greatest activity on C4, C6 and C8 aldehydes; also reduces retinal to retinol.
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CAS REGISTRY NUMBER
COMMENTARY
37250-10-5
-
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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
(1R)-1-hydroxy-1-phenylpropan-2-one + NADPH + H+
(1R)-1-phenylpropane-1,2-diol + NADP+
-
Substrates: -
Products: -
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(2R)-2-hydroxy-1-(4-methoxyphenyl)propan-1-one + NADPH + H+
(2R)-1-(4-methoxyphenyl)propane-1,2-diol + NADP+
-
Substrates: -
Products: -
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(2S)-2-hydroxy-1-(4-methoxyphenyl)propan-1-one + NADPH + H+
(2S)-1-(4-methoxyphenyl)propane-1,2-diol + NADP+
-
Substrates: -
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(4R,6R)-6-pentyloxane-2,4-diol + NAD+
(4R,6R)-4-hydroxy-6-pentyloxan-2-one + NADH + H+
-
Substrates: -
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(4R,6S)-6-(chloromethyl)oxane-2,4-diol + NAD+
(4R,6S)-6-(chloromethyl)-4-hydroxyoxan-2-one + NADH + H+
(4R,6S)-6-(chloromethyl)oxane-2,4-diol + NADP+
(4R,6S)-6-(chloromethyl)-4-hydroxyoxan-2-one + NADPH + H+
(RS)-1-phenylethanol + NAD+
1-phenylethanone + NADH + H+
-
Substrates: 100% activity
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(RS)-1-phenylethanol + NADP+
1-phenylethanone + NADPH + H+
-
Substrates: 100% activity
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(S)-2-butanol + NADP+
butanone + NADPH + H+
Substrates: 196% of the activity with 2-propanol, 2fold preference for (S)-2-butanol over (RS)-2-butanol
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1,2-propanediol + NAD+
? + NADH + H+
Substrates: -
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r
1,3-butanediol + NADP+
? + NADPH + H+
Substrates: 91% relative activity as compared to 2-propanol
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1,3-propanediol + NAD+
? + NADH + H+
Substrates: -
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1-(2-bromophenyl)ethanol + NAD(P)+
1-(2-bromophenyl)ethanone + NAD(P)H + H+
-
Substrates: 11.3% activity compared to (RS)-1-phenylethanol
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1-(2-chlorophenyl)ethanol + NAD(P)+
1-(2-chlorophenyl)ethanone + NAD(P)H + H+
-
Substrates: 16.4% activity compared to (RS)-1-phenylethanol
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1-(3-bromophenyl)ethanol + NAD(P)+
1-(3-bromophenyl)ethanone + NAD(P)H + H+
-
Substrates: 315% activity compared to (RS)-1-phenylethanol
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1-(3-chlorophenyl)ethanol + NAD(P)+
1-(3-chlorophenyl)ethanone + NAD(P)H + H+
-
Substrates: 205% activity compared to (RS)-1-phenylethanol
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1-(4-bromophenyl)ethanol + NAD(P)+
1-(4-bromophenyl)ethanone + NAD(P)H + H+
-
Substrates: 167% activity compared to (RS)-1-phenylethanol
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1-(4-chlorophenyl)ethanone + NAD(P)+
1-(4-chlorophenyl)ethanone + NAD(P)H + H+
-
Substrates: 151% activity compared to (RS)-1-phenylethanol
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1-(4-fluorophenyl)ethanol + NAD(P)+
1-(4-fluorophenyl)ethanol + NAD(P)H + H+
-
Substrates: 119% activity compared to (RS)-1-phenylethanol
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1-(4-methylphenyl)ethanone + NAD(P)+
1-(4-methylphenyl)ethanol + NAD(P)H + H+
-
Substrates: 189% activity compared to (RS)-1-phenylethanol
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1-butanol + NAD(P)+
butanal + NAD(P)H + H+
-
Substrates: 2.3% activity compared to (RS)-1-phenylethanol
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?
1-heptanol + NAD(P)+
heptanal + NAD(P)H + H+
-
Substrates: 3.3% activity compared to (RS)-1-phenylethanol
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1-heptanol + NAD+
heptanal + NADH + H+
Substrates: -
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r
1-hexanol + NAD(P)+
hexanal + NAD(P)H + H+
-
Substrates: 2.8% activity compared to (RS)-1-phenylethanol
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1-hexanol + NAD+
hexanal + NADH + H+
Substrates: -
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r
1-octanol + NAD(P)+
octanal + NAD(P)H + H+
-
Substrates: 2.3% activity compared to (RS)-1-phenylethanol
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1-octanol + NAD+
octanal + NADH + H+
Substrates: -
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1-pentanol + NAD(P)+
pentanal + NAD(P)H + H+
-
Substrates: 2.8% activity compared to (RS)-1-phenylethanol
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1-pentanol + NAD+
pentanal + NADH + H+
Substrates: -
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1-phenyl-1,2-ethanediol + NAD(P)+
?
-
Substrates: 3.4% activity compared to (RS)-1-phenylethanol
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1-phenyl-1-propanol + NAD(P)+
1-phenylpropionaldehyde + NAD(P)H + H+
-
Substrates: 13.1% activity compared to (RS)-1-phenylethanol
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1-phenyl-2-propanol + NAD(P)+
1-phenylpropan-2-one + NAD(P)H + H+
-
Substrates: 39.1% activity compared to (RS)-1-phenylethanol
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1-phenylethanol + NADP+
1-phenylethanone + NADPH + H+
Substrates: 35% of the activtiy with 1-propanol
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1-phenylethanol + NADP+
acetophenone + NADPH + H+
Substrates: 35% compared to activity with 1-propanol
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1-phenylmethanol + NADP+
benzaldehyde + NADPH + H+
Substrates: 180% relative activity as compared to 2-propanol
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1-propanol + NAD(P)+
propionaldehyde + NAD(P)H + H+
-
Substrates: 1.2% activity compared to (RS)-1-phenylethanol
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2,2,2-trifluoroacetophenone + NAD(P)H + H+
2,2,2-trifluoro-1-phenylethan-1-ol + NAD(P)+
-
Substrates: 180% activity compared to acetoin
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2-bromoacetophenone + NAD(P)H + H+
1-(2-bromophenyl)ethanone + NAD(P)+
-
Substrates: 8.7% activity compared to acetoin
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2-bromobenzaldehyde + NADPH
2-bromobenzyl alcohol + NADP+
-
Substrates: -
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2-bromobenzaldehyde + NADPH + H+
2-bromobenzyl alcohol + NADP+
-
Substrates: -
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2-butanol + NAD(P)+
butan-2-one + NAD(P)H + H+
-
Substrates: 22.3% activity compared to (RS)-1-phenylethanol
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2-butanol + NADP+
2-butanone + NADPH + H+
Substrates: 43% of the activity compared to ethanol
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2-chloro-1-phenylethanol + NAD(P)+
2-chloro-1-phenylethan-1-one + NAD(P)H + H+
-
Substrates: 0.3% activity compared to (RS)-1-phenylethanol
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2-cyclohexenol + NADP+
2-cyclohexenone + NADH + H+
-
Substrates: -
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r
2-cyclohexenone + NADH + H+
2-cyclohexenol + NADP+
-
Substrates: -
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r
2-fluorobenzaldehyde + NADPH + H+
2-fluorobenzyl alcohol + NADP+
-
Substrates: -
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2-heptanol + NAD(P)+
heptan-2-one + NAD(P)H + H+
-
Substrates: 61.6% activity compared to (RS)-1-phenylethanol
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2-hexanol + NAD(P)+
hexan-2-one + NAD(P)H + H+
-
Substrates: 38.7% activity compared to (RS)-1-phenylethanol
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?
2-hexanone + NAD(P)H + H+
hexan-2-ol + NAD(P)+
-
Substrates: 3.6% activity compared to acetoin
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2-hydroxy-2-methyl-1-phenylpropan-1-one + NADPH + H+
2-methyl-1-phenylpropan-1,2-diol + NADP+
-
Substrates: -
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?
2-hydroxy-3-methoxybenzaldehyde + NADPH + H+
2-hydroxy-3-methoxybenzyl alcohol + NADP+
Substrates: -
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?
2-methylbenzaldehyde + NADPH + H+
2-methylbenzyl alcohol + NADP+
-
Substrates: -
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2-octanol + NAD(P)+
octan-2-one + NAD(P)H + H+
-
Substrates: 45.8% activity compared to (RS)-1-phenylethanol
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?
2-pentanol + NAD(P)+
pentan-2-one + NAD(P)H + H+
-
Substrates: 30.2% activity compared to (RS)-1-phenylethanol
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?
2-pentanol + NADP+
pentan-2-one + NADPH + H+
Substrates: 67% of the activity with 2-propanol
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2-phenylethanol + NAD(P)+
phenylacetaldehyde + NAD(P)H + H+
-
Substrates: 0.3% activity compared to (RS)-1-phenylethanol
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2-propanol + NAD(P)+
propan-2-one + NAD(P)H + H+
-
Substrates: 5.3% activity compared to (RS)-1-phenylethanol
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?
3,4-dimethoxybenzaldehyde + NADPH + H+
3,4-dimethoxybenzyl alcohol + NADP+
Substrates: -
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?
3-fluorobenzaldehyde + NADPH
3-fluorobenzyl alcohol + NADP+
-
Substrates: -
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r
3-methoxybenzaldehyde + NADPH + H+
3-methoxybenzyl alcohol + NADP+
-
Substrates: -
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?
3-methyl-2-pentanone + NADPH + H+
? + NADP+
Substrates: 13% relative activity as compared to pyruvaldehyde
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?
3-methylbenzaldehyde + NADPH + H+
3-methylbenzyl alcohol + NADP+
-
Substrates: -
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3-methylbutanal + NADP+
? + NADPH + H+
Substrates: about% of the activity with 1-butanol
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3-methylcyclohexanone + NADH + H+
3-methylcyclohexanol + NAD+
-
Substrates: -
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r
4-bromobenzaldehyde + NADPH + H+
4-bromobenzyl alcohol + NADP+
-
Substrates: -
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?
4-fluorobenzaldehyde + NADPH + H+
4-fluorobenzyl alcohol + NADP+
-
Substrates: -
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4-methylbenzaldehyde + NADPH + H+
4-methylbenzyl alcohol + NADP+
-
Substrates: -
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4-methylnitrosamino-1-(3-pyridyl)-1-butanone + NADPH + H+
?
-
Substrates: -
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4-methylpentan-2-one + NADPH + H+
4-methylpentan-2-ol + NADP+
-
Substrates: -
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4-phenyl-2-butanone + NADH + H+
4-phenyl-2-butanol + NAD+
-
Substrates: -
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acetoin + NAD(P)+
butan-2,3-dione + NAD(P)H + H+
-
Substrates: 100% activity
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acetoin + NAD(P)H + H+
2,3-butanediol + NAD(P)+
-
Substrates: 4.5% activity compared to (RS)-1-phenylethanol
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acetoin + NADPH + H+
?
-
Substrates: 1.9% activity compared to 3-hydroxypropionaldehyde
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acetone + NAD(P)H + H+
propan-2-ol + NAD(P)+
-
Substrates: 4.1% activity compared to acetoin
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acetophenone + NADH + H+
1-phenylethan-1-ol + NAD+
-
Substrates: -
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all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
Substrates: -
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all-trans-retinol + NADP+
all-trans-retinal + NADPH + H+
Substrates: -
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benzaldehyde + NAD(P)H
benzyl alcohol + NAD(P)+
-
Substrates: -
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benzaldehyde + NADPH + H+
benzyl alcohol + NADP+
Substrates: -
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benzylalcohol + NAD+
benzaldehyde + NADH + H+
Substrates: -
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butan-1,4-diol + NADP+
butandialdehyde + NADPH
-
Substrates: 29% of activity with hexan-1-ol
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butanal + NADPH + H+
1-butanol + NAD(P)+
Substrates: 44% activity compared to pentanal
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cinnamaldehyde + NADPH + H+
cinnamyl alcohol + NADP+
Substrates: -
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cis-4-cyclopentene-1,3-diol + NADP+
(R)-4-hydroxy-2-cyclopentenone + NADPH + H+
-
Substrates: -
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cis-4-heptenal + NAD(P)+
cis-4-heptenol + NAD(P)H
-
Substrates: -
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cis-hex-3-en-1-ol + NADP+
cis-hex-3-en-1-al + NADPH
-
Substrates: 18.7% of activity with hexan-1ol
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cyclohexanol + NAD(P)+
cyclohexanone + NAD(P)H + H+
-
Substrates: 52.3% activity compared to (RS)-1-phenylethanol
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cyclohexanol + NAD+
cyclohexanone + NADH + H+
Substrates: -
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cyclohexanone + NAD(P)H + H+
cyclohexanol + NAD(P)+
-
Substrates: 19.1% activity compared to acetoin
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D-arabinose + NAD(P)+
?
-
Substrates: 21.4% activity compared to (RS)-1-phenylethanol
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D-arabinose + NADP+
? + NADPH + H+
Substrates: 200% relative activity as compared to 2-propanol
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D-arabinose + NADP+
D-arabitol + NADPH + H+
Substrates: 200% of the activity with 2-propanol. D-arabinose is preferred over L-arabinose
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D-mannose + NADP+
? + NADPH + H+
Substrates: 48% relative activity as compared to 2-propanol
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D-ribose + NADP+
? + NADPH + H+
Substrates: 35% relative activity as compared to 2-propanol
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decan-1-ol + NADP+
decanal + NADPH
-
Substrates: decrease in enzyme activity with increase in chain length
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dihydroxyacetone + NAD(P)H + H+
?
-
Substrates: 34.8% activity compared to acetoin
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dodecan-1-ol + NADP+
dodecanal + NADPH
-
Substrates: decrease in enzyme activity with increase in chain length
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ethanol + NAD(P)+
acetaldehyde + NAD(P)H + H+
-
Substrates: 0.5% activity compared to (RS)-1-phenylethanol
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ethyl acetoacetate + NADPH + H+
? + NADP+
-
Substrates: -
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ethyl pyruvate + NAD(P)H + H+
?
-
Substrates: 294% activity compared to acetoin
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farnesyl aldehyde + NAD(P)H
farnesol + NAD(P)+
-
Substrates: -
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furan-2-carbaldehyde + NADPH + H+
(furan-2-yl)methanol + NADP+
-
Substrates: -
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furfural + NADPH + H+
(furan-2-yl)methanol + NAD(P)+
Substrates: 5% activity compared to pentanal
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glycerol + NADP+
glyceraldehyde + NADPH + H+
Substrates: 16% relative activity as compared to 2-propanol
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glycoaldehyde + NADPH + H+
?
Substrates: 5% activity compared to pentanal
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glyoxylic acid + NADPH + H+
? + NADP+
Substrates: 36% relative activity as compared to pyruvaldehyde
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heptan-1-ol + NADP+
heptanal + NADPH
-
Substrates: -
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heptanal + NADPH + H+
1-heptanol + NAD(P)+
Substrates: 56% activity compared to pentanal
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hexanal + NAD(P)H + H+
hexan-1-ol + NAD(P)+
-
Substrates: 12.9% activity compared to acetoin
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hexanal + NADPH + H+
1-hexanol + NAD(P)+
Substrates: 62% activity compared to pentanal
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hydrocinnamaldehyde + NADPH + H+
hydrocinnamyl alcohol + NADP+
Substrates: -
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isoamyl alcohol + NADP+
? + NADPH + H+
Substrates: about 80% of the activity with 1-butanol
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L-arabinose + NAD(P)+
?
-
Substrates: 5.2% activity compared to (RS)-1-phenylethanol
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L-arabinose + NADP+
? + NADPH + H+
Substrates: 17% relative activity as compared to 2-propanol
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linolenyl aldehyde + NAD(P)H
linolenol + NAD(P)+
-
Substrates: -
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linoleyl aldehyde + NAD(P)H
linoleol + NAD(P)+
-
Substrates: -
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mannitol + NADP+
D-mannose + NADPH
-
Substrates: 6.5% of activity with hexan-1-ol
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meso-2,3-butanediol + NAD+
?
-
Substrates: 272% activity compared to (RS)-1-phenylethanol
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meso-2,3-butanediol + NADP+
?
-
Substrates: 272% activity compared to (RS)-1-phenylethanol
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methanol + NAD(P)+
formaldehyde + NAD(P)H + H+
-
Substrates: 0.2% activity compared to (RS)-1-phenylethanol
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methyl benzoylformate + NAD(P)H + H+
?
-
Substrates: 67% activity compared to acetoin
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methylglyoxal + NADPH + H+
2-hydroxy-propanal + NADP+
-
Substrates: -
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methylglyoxal + NADPH + H+
?
Substrates: 29% activity compared to pentanal
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octan-1-ol + NADP+
octanal + NADPH
-
Substrates: decrease in enzyme activity with increase in chain length
Products: -
Products: -
r
octan-1-ol + NADP+
octanal + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
octanal + NADPH + H+
1-octanol + NAD(P)+
Substrates: 55% activity compared to pentanal
Products: -
Products: -
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pentanal + NADPH + H+
1-pentanol + NAD(P)+
Substrates: 100% activity
Products: -
Products: -
?
phenylacetaldehyde + NAD(P)H + H+
2-phenylethan-1-ol + NAD(P)+
-
Substrates: 18.6% activity compared to acetoin
Products: -
Products: -
?
pyridine-2-carbaldehyde + NADPH + H+
(pyridin-2-yl)methanol + NADP+
-
Substrates: -
Products: -
Products: -
?
pyruvaldehyde + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
pyruvic aldehyde + NAD(P)H + H+
?
-
Substrates: 328% activity compared to acetoin
Products: -
Products: -
?
rac-1-nonen-4-ol + NADP+
(S)-1-nonen-4-ol + 1-nonen-4-one + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
rac-1-phenylethanol + NAD(P)+
acetophenone + (R)-1-phenylethanol + NAD(P)H + H+
-
Substrates: -
Products: -
Products: -
?
rac-1-phenylethanol + NADP+
(R)-1-phenylethanol + (S)-1-phenylethanol + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
ribitol + NADP+
D-ribose + NADPH
-
Substrates: 4% of activity with hexan-1-ol
Products: -
Products: -
r
salicylaldehye + NADPH + H+
salicylalcohol + NADP+
Substrates: -
Products: -
Products: -
?
tetradecanal + NAD(P)H
tetradecan-1-ol + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
trans-2,cis-6-nonadienal + NAD(P)+
trans-2,cis-6-nonadienol + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-2,cis-6-nonadienal + NADPH + H+
trans-2,cis-6-nonadienol + NADP+
Substrates: -
Products: -
Products: -
?
trans-2-hexenal + NADPH + H+
trans-2-hexenol + NADP+
Substrates: -
Products: -
Products: -
?
trans-2-nonenal + NADPH + H+
trans-2-nonen-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
trans-2-nonenal + NADPH + H+
trans-2-nonenol + NADP+
Substrates: -
Products: -
Products: -
?
trans-2-octenal + NADPH + H+
trans-2-octen-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
?
trans-2-pentenol + NAD(P)+
trans-2-pentenal + NAD(P)H
-
Substrates: -
Products: -
Products: -
?
trans-trans-2,4-decadienal + NADPH + H+
trans-trans-2,4-decadienol + NADP+
-
Substrates: -
Products: -
Products: -
?
(2S,5S)-2,5-hexanediol + NADP+
? + NADPH + H+
Substrates: -
Products: -
Products: -
?
(2S,5S)-2,5-hexanediol + NADP+
? + NADPH + H+
Substrates: -
Products: -
Products: -
?
(4R,6R)-6-butyloxane-2,4-diol + NAD+
(4R,6R)-6-butyl-4-hydroxyoxan-2-one + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(4R,6R)-6-butyloxane-2,4-diol + NAD+
(4R,6R)-6-butyl-4-hydroxyoxan-2-one + NADH + H+
Starmerella magnoliae DSMZ 70638
-
Substrates: -
Products: -
Products: -
?
(4R,6R)-6-butyloxane-2,4-diol + NADP+
(4R,6R)-6-butyl-4-hydroxyoxan-2-one + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(4R,6R)-6-butyloxane-2,4-diol + NADP+
(4R,6R)-6-butyl-4-hydroxyoxan-2-one + NADPH + H+
Starmerella magnoliae DSMZ 70638
-
Substrates: -
Products: -
Products: -
?
(4R,6R)-6-pentyloxane-2,4-diol + NADP+
(4R,6R)-4-hydroxy-6-pentyloxan-2-one + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(4R,6R)-6-pentyloxane-2,4-diol + NADP+
(4R,6R)-4-hydroxy-6-pentyloxan-2-one + NADPH + H+
Starmerella magnoliae DSMZ 70638
-
Substrates: -
Products: -
Products: -
?
(4R,6S)-6-(chloromethyl)oxane-2,4-diol + NAD+
(4R,6S)-6-(chloromethyl)-4-hydroxyoxan-2-one + NADH + H+
-
Substrates: -
Products: -
Products: -
?
(4R,6S)-6-(chloromethyl)oxane-2,4-diol + NAD+
(4R,6S)-6-(chloromethyl)-4-hydroxyoxan-2-one + NADH + H+
Starmerella magnoliae DSMZ 70638
-
Substrates: -
Products: -
Products: -
?
(4R,6S)-6-(chloromethyl)oxane-2,4-diol + NADP+
(4R,6S)-6-(chloromethyl)-4-hydroxyoxan-2-one + NADPH + H+
-
Substrates: -
Products: -
Products: -
?
(4R,6S)-6-(chloromethyl)oxane-2,4-diol + NADP+
(4R,6S)-6-(chloromethyl)-4-hydroxyoxan-2-one + NADPH + H+
Starmerella magnoliae DSMZ 70638
-
Substrates: -
Products: -
Products: -
?
(S)-2-butanol + NADP+
butanone + NADPH
Substrates: 196% relative activity as compared to 2-propanol
Products: -
Products: -
?
(S)-2-butanol + NADP+
butanone + NADPH
Substrates: 196% relative activity as compared to 2-propanol
Products: -
Products: -
?
1-butanol + NAD+
butanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NAD+
butanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NAD+
butanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NAD+
butanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NAD+
butanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NAD+
butanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NADP+
1-butanal + NADPH + H+
Substrates: -
Products: -
Products: -
?
1-butanol + NADP+
1-butanal + NADPH + H+
Substrates: -
Products: -
Products: -
?
1-butanol + NADP+
butanal + NADPH
Substrates: 80% relative activity as compared to 2-propanol
Products: -
Products: -
?
1-butanol + NADP+
butanal + NADPH
Substrates: 80% relative activity as compared to 2-propanol
Products: -
Products: -
?
1-butanol + NADP+
butanal + NADPH + H+
Substrates: 117% of the activity compared to ethanol
Products: -
Products: -
?
1-butanol + NADP+
butanal + NADPH + H+
Substrates: 80% compared to activity with 1-propanol
Products: -
Products: -
?
1-butanol + NADP+
butanal + NADPH + H+
Substrates: 80% compared to activity with 1-propanol
Products: -
Products: -
?
1-butanol + NADP+
butanal + NADPH + H+
Substrates: 80% of the activtiy with 1-propanol
Products: -
Products: -
?
1-butanol + NADP+
butanal + NADPH + H+
Substrates: 80% of the activtiy with 1-propanol
Products: -
Products: -
?
1-butanol + NADP+
butanal + NADPH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NADP+
butanal + NADPH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NADP+
butanal + NADPH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NADP+
butanal + NADPH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NADP+
butanal + NADPH + H+
Substrates: -
Products: -
Products: -
r
1-butanol + NADP+
butanal + NADPH + H+
Substrates: -
Products: -
Products: -
r
1-pentanol + NADP+
pentanal + NADPH + H+
Substrates: 74% of the activity compared to ethanol
Products: -
Products: -
?
1-pentanol + NADP+
pentanal + NADPH + H+
Substrates: about 75% of the activity with 1-butanol
Products: -
Products: -
?
1-pentanol + NADP+
pentanal + NADPH + H+
Substrates: about 75% of the activity with 1-butanol
Products: -
Products: -
?
1-propanol + NAD+
propanal + NADH + H+
Substrates: dual cofactor dependency, NAD+ shows 60% of the activity with NADP+
Products: -
Products: -
?
1-propanol + NAD+
propanal + NADH + H+
Substrates: dual cofactor dependency, NAD+ shows 60% of the activity with NADP+
Products: -
Products: -
?
1-propanol + NAD+
propanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-propanol + NAD+
propanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-propanol + NAD+
propanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-propanol + NAD+
propanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-propanol + NAD+
propanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-propanol + NAD+
propanal + NADH + H+
Substrates: -
Products: -
Products: -
r
1-propanol + NADP+
propanal + NADPH + H+
Substrates: 137% of the activity compared to ethanol
Products: -
Products: -
?
1-propanol + NADP+
propanal + NADPH + H+
Substrates: dual cofactor dependency, NAD+ shows 60% of the activity with NADP+
Products: -
Products: -
?
1-propanol + NADP+
propanal + NADPH + H+
Substrates: dual cofactor dependency, NAD+ shows 60% of the activity with NADP+
Products: -
Products: -
?
1-propanol + NADP+
propanal + NADPH + H+
Substrates: -
Products: -
Products: -
?
1-propanol + NADP+
propanal + NADPH + H+
Substrates: -
Products: -
Products: -
?
1-propanol + NADP+
propanal + NADPH + H+
Substrates: about 60% of the activity with 1-butanol
Products: -
Products: -
?
1-propanol + NADP+
propanal + NADPH + H+
Substrates: about 60% of the activity with 1-butanol
Products: -
Products: -
?
1-propanol + NADP+
propanal + NADPH + H+
Substrates: -
Products: -
Products: -
?
1-propanol + NADP+
propanal + NADPH + H+
Substrates: -
Products: -
Products: -
?
2,3-pentanedione + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2,3-pentanedione + NADPH + H+
? + NADP+
Substrates: -
Products: -
Products: -
?
2-butanol + NADP+
butanone + NADPH + H+
Substrates: 30% compared to activity with 1-propanol
Products: -
Products: -
?
2-butanol + NADP+
butanone + NADPH + H+
Substrates: 30% of the activtiy with 1-propanol
Products: -
Products: -
?
2-butanol + NADP+
butanone + NADPH + H+
Substrates: 30% of the activtiy with 1-propanol
Products: -
Products: -
?
2-butanol + NADP+
butanone + NADPH + H+
Substrates: about 25% of the activity with 1-butanol
Products: -
Products: -
?
2-butanol + NADP+
butanone + NADPH + H+
Substrates: about 25% of the activity with 1-butanol
Products: -
Products: -
?
2-methoxybenzaldehyde + NADPH + H+
2-methoxybenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
2-methoxybenzaldehyde + NADPH + H+
2-methoxybenzyl alcohol + NADP+
Substrates: highest activity
Products: -
Products: -
?
2-pentanol + NADP+
2-pentanone + NADPH + H+
Substrates: 67% relative activity as compared to 2-propanol
Products: -
Products: -
?
2-pentanol + NADP+
2-pentanone + NADPH + H+
Substrates: 67% relative activity as compared to 2-propanol
Products: -
Products: -
?
2-propanol + NADP+
acetone + NADPH
Substrates: -
Products: -
Products: -
?
2-propanol + NADP+
acetone + NADPH
Substrates: -
Products: -
Products: -
?
2-propanol + NADP+
acetone + NADPH + H+
Substrates: 25% compared to activity with 1-propanol
Products: -
Products: -
?
2-propanol + NADP+
acetone + NADPH + H+
Substrates: 25% compared to activity with 1-propanol
Products: -
Products: -
?
2-propanol + NADP+
acetone + NADPH + H+
Substrates: -
Products: -
Products: -
?
2-propanol + NADP+
acetone + NADPH + H+
Substrates: -
Products: -
Products: -
?
3-hydroxypropionaldehyde + NADPH + H+
propan-1,3-diol + NADP+
-
Substrates: 100% activity
Products: -
Products: -
?
3-hydroxypropionaldehyde + NADPH + H+
propan-1,3-diol + NADP+
-
Substrates: 100% activity
Products: -
Products: -
?
4-methoxybenzaldehyde + NADPH + H+
4-methoxybenzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
?
4-methoxybenzaldehyde + NADPH + H+
4-methoxybenzyl alcohol + NADP+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NADH + H+
ethanol + NAD+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NADH + H+
ethanol + NAD+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NADPH + H+
ethanol + NADP+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NADPH + H+
ethanol + NADP+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NADPH + H+
ethanol + NADP+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NADPH + H+
ethanol + NADP+
Substrates: -
Products: -
Products: -
?
acetaldehyde + NADPH + H+
ethanol + NADP+
-
Substrates: 2.2% activity compared to 3-hydroxypropionaldehyde
Products: -
Products: -
?
acetaldehyde + NADPH + H+
ethanol + NADP+
Substrates: -
Products: -
Products: -
?
acrolein + NADPH + H+
prop-2-en-1-ol + NADP+
-
Substrates: 41.8% activity compared to 3-hydroxypropionaldehyde
Products: -
Products: -
?
acrolein + NADPH + H+
prop-2-en-1-ol + NADP+
-
Substrates: 41.8% activity compared to 3-hydroxypropionaldehyde
Products: -
Products: -
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allyl alcohol + NADP+
acrylaldehyde + NADPH
-
Substrates: 28% of activity with hexan-1-ol
Products: -
Products: -
r
allyl alcohol + NADP+
acrylaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
allyl alcohol + NADP+
acrylaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
benzaldehyde + NADPH
benzyl alcohol + NADP+
-
Substrates: -
Products: -
Products: -
r
benzyl alcohol + NADP+
benzaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
benzyl alcohol + NADP+
benzaldehyde + NADPH
-
Substrates: -
Products: -
Products: -
r
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
Substrates: 20% compared to activity with 1-propanol
Products: -
Products: -
?
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
Substrates: about% of the activity with 1-butanol
Products: -
Products: -
?
benzyl alcohol + NADP+
benzaldehyde + NADPH + H+
Substrates: 180% of the activity with 2-propanol
Products: -
Products: -
?
butan-1-ol + NADP+
butanal + NADPH
-
Substrates: 36.3% of activity with hexan-1-ol
Products: -
Products: -
r
butan-1-ol + NADP+
butanal + NADPH
-
Substrates: -
Products: -
Products: -
r
butan-1-ol + NADP+
butanal + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
butan-1-ol + NADP+
butanal + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
butanal + NADPH + H+
butan-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
r
butanal + NADPH + H+
butan-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
r
butanal + NADPH + H+
butan-1-ol + NADP+
-
Substrates: -
Products: -
Products: -
r
butyraldehyde + NADPH + H+
butanol + NADP+
-
Substrates: 118.4% activity compared to 3-hydroxypropionaldehyde
Products: -
Products: -
?
butyraldehyde + NADPH + H+
butanol + NADP+
-
Substrates: 118.4% activity compared to 3-hydroxypropionaldehyde
Products: -
Products: -
?
cellobiose + NADP+
? + NADPH + H+
Substrates: 71% relative activity as compared to 2-propanol
Products: -
Products: -
?
cellobiose + NADP+
? + NADPH + H+
Substrates: 71% of the activity with 2-propanol
Products: -
Products: -
?
cis-2-butenol + NAD(P)H
trans-2-butenal + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
cis-2-butenol + NAD(P)H
trans-2-butenal + NAD(P)+
-
Substrates: -
Products: -
Products: -
?
cyclohexanol + NADP+
cyclohexanone + NADH + H+
-
Substrates: -
Products: -
Products: -
r
cyclohexanone + NADH + H+
cyclohexanol + NADP+
-
Substrates: -
Products: -
Products: -
r
D-glucose + NADP+
? + NADPH + H+
Substrates: 146% relative activity as compared to 2-propanol
Products: -
Products: -
?
D-glucose + NADP+
? + NADPH + H+
Substrates: 146% of the activity with 2-propanol
Products: -
Products: -
?
D-xylose + NADP+
? + NADPH + H+
Substrates: 246% relative activity as compared to 2-propanol
Products: -
Products: -
?
D-xylose + NADP+
? + NADPH + H+
Substrates: 246% of the activity with 2-propanol
Products: -
Products: -
?
dimethylglyoxal + NADPH + H+
? + NADP+
Substrates: 270% relative activity as compared to pyruvaldehyde
Products: -
Products: -
?
dimethylglyoxal + NADPH + H+
? + NADP+
Substrates: 270% of the activity with pyruvaldehyde
Products: -
Products: -
?
ethanediol + NADP+
glyoxal + NADPH
-
Substrates: 8.5% of activity with hexan-1-ol
Products: -
Products: -
r
ethanol + NAD+
acetaldehyde + NADH + H+
Substrates: enzyme appears to preferentially catalyze the reductive reaction. Activity with NAD+ is 75% less than that detected with NADP+
Products: -
Products: -
?
ethanol + NAD+
acetaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
ethanol + NAD+
acetaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
ethanol + NAD+
acetaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
ethanol + NAD+
acetaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
ethanol + NAD+
acetaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
ethanol + NAD+
acetaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: enzyme appears to preferentially catalyze the reductive reaction. Activity with NAD+ is 75% less than that detected with NADP+
Products: -
Products: -
?
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: 85% compared to activity with 1-propanol
Products: -
Products: -
?
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: 85% compared to activity with 1-propanol
Products: -
Products: -
?
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: 84% of the activtiy with 1-propanol
Products: -
Products: -
?
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: 84% of the activtiy with 1-propanol
Products: -
Products: -
?
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: about 50% of the activity with 1-butanol
Products: -
Products: -
?
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: about 50% of the activity with 1-butanol
Products: -
Products: -
?
ethanol + NADP+
acetaldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
ethanol + NADP+
acetaldehyde + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: 36% relative activity as compared to 2-propanol
Products: -
Products: -
?
ethanol + NADP+
acetaldehyde + NADPH + H+
Substrates: 36% relative activity as compared to 2-propanol
Products: -
Products: -
?
ethanol + NADP+
ethanal + NADPH + H+
-
Substrates: 8.5% of activity with hexan-1-ol
Products: -
Products: -
r
ethanol + NADP+
ethanal + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
ethanol + NADP+
ethanal + NADPH + H+
-
Substrates: oxidation rate at 5% of reduction rate
Products: -
Products: -
r
hexan-1-ol + NADP+
hexanal + NADPH
-
Substrates: -
Products: -
Products: -
r, ?
hexan-1-ol + NADP+
hexanal + NADPH
-
Substrates: -
Products: -
Products: -
?
hexan-1-ol + NADP+
hexanal + NADPH
-
Substrates: -
Products: -
Products: -
?
hexan-1-ol + NADP+
hexanal + NADPH
-
Substrates: -
Products: -
Products: -
?
hexan-1-ol + NADP+
hexanal + NADPH
-
Substrates: -
Products: -
Products: -
r
methanol + NAD+
formaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
methanol + NAD+
formaldehyde + NADH + H+
Substrates: -
Products: -
Products: -
r
methanol + NAD+
formaldehyde + NADH + H+
Substrates: -
Products: -
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r
methanol + NAD+
formaldehyde + NADH + H+
Substrates: -
Products: -
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r
methanol + NAD+
formaldehyde + NADH + H+
Substrates: -
Products: -
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r
methanol + NAD+
formaldehyde + NADH + H+
Substrates: -
Products: -
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r
pentan-1-ol + NADP+
pentanal + NADPH
-
Substrates: 4% of activity with hexan-1-ol
Products: -
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r
pentan-1-ol + NADP+
pentanal + NADPH
-
Substrates: -
Products: -
Products: -
r
pentan-1-ol + NADP+
pentanal + NADPH
-
Substrates: -
Products: -
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?
propan-1-ol + NADP+
propanal + NADPH
-
Substrates: 28% of activity with hexan-1-ol
Products: -
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r
propan-1-ol + NADP+
propanal + NADPH
-
Substrates: oxidation rate at 5% of reduction rate
Products: -
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r
propanal + NADPH + H+
1-propanol + NAD(P)+
Substrates: 14% activity compared to pentanal
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?
propanal + NADPH + H+
1-propanol + NAD(P)+
-
Substrates: 14% activity compared to pentanal
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?
propanal + NADPH + H+
1-propanol + NAD(P)+
Substrates: 14% activity compared to pentanal
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?
propionaldehyde + NADPH + H+
propanol + NADP+
-
Substrates: 37.1% activity compared to 3-hydroxypropionaldehyde
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?
propionaldehyde + NADPH + H+
propanol + NADP+
-
Substrates: 37.1% activity compared to 3-hydroxypropionaldehyde
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?
pyruvaldehyde + NADPH + H+
lactaldehyde + NADP+
Substrates: -
Products: -
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?
pyruvaldehyde + NADPH + H+
lactaldehyde + NADP+
-
Substrates: -
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?
pyruvaldehyde + NADPH + H+
lactaldehyde + NADP+
Substrates: -
Products: -
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?
retinaldehyde + NADH
retinol + NAD+
-
Substrates: the enzyme is involved in retinol and vitamin A metabolism, retinoic acid is important in intestinal epithelial cell proliferation and differentiation, the enzyme also plays a role in dietary conversion of beta-carotene to retinol via retinaldehyde
Products: -
Products: -
r
additional information
?
-
Substrates: in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. The AdhE protein of the ethanologenic strain of Clostridium thermocellum has acquired high NADPH-linked ADH activity while maintaining NADH-linked ALDH and ADH activities at wild-type levels
Products: -
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?
additional information
?
-
Substrates: the enzyme does not accept methanol, 2-propanol, glycerol or glucose as substrates
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?
additional information
?
-
-
Substrates: the enzyme does not accept methanol, 2-propanol, glycerol or glucose as substrates
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?
additional information
?
-
Substrates: preference for short-chain alcohol substrates, particularly for 1-propanol (100%) and ethanol (84%), no activity with glycerol or methanol
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?
additional information
?
-
Substrates: no substrates: methanol, glycerol
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?
additional information
?
-
Substrates: HvADH2 accepts a broad range of substrates, no activity with methanol
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?
additional information
?
-
-
Substrates: 4-nitroacetophenone, benzyl, cortisone and progesterone are no substrates
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?
additional information
?
-
-
Substrates: no activity with dihydroxyacetone, hydroxyacetone, and acetone
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?
additional information
?
-
-
Substrates: no activity with dihydroxyacetone, hydroxyacetone, and acetone
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?
additional information
?
-
Substrates: the enzyme shows no oxidative activities towards alcoholic compounds
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?
additional information
?
-
Substrates: no activity with glyoxal, methanal, and ethanal
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?
additional information
?
-
-
Substrates: the enzyme shows no oxidative activities towards alcoholic compounds
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?
additional information
?
-
Substrates: the enzyme shows no oxidative activities towards alcoholic compounds
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?
additional information
?
-
Substrates: substrate specificity of Ni-PhADH for alcohol oxidation reactions and aldehyde reduction reactions, overview. No activity with 2-butanol, tert-butanol, and 2,3-butanediol
Products: -
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?
additional information
?
-
-
Substrates: no activity with methanol and ethanol
Products: -
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?
additional information
?
-
-
Substrates: no activity with methanol and ethanol
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme plays an important role in potato defence response to Erwinia carotovora
Products: -
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?
additional information
?
-
Substrates: not: conferyl aldehyde and sinapaldehyde, the enzyme exhibits an absolute requirement for NADPH as cofactor and can not be substituted by NADH
Products: -
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?
additional information
?
-
-
Substrates: lactol substrates (4R,6S)-6-(chloromethyl)oxane-2,4-diol and (4R,6R)-6-butyloxane-2,4-diol for the biocatalytic oxidations are obtained from 2-deoxy-D-ribose 5-phosphate aldolase (DERA) catalyzed reactions of the corresponding acceptor aldehydes chloroacetaldehyde and pentanal, respectively and at least two equivalents of acetaldehyde as described previously. Development of an efficient biocatalytic process on pilot plant scale to oxidize the aliphatic hydroxylactol substrate (4R,6R)-6-butyloxane-2,4-diol to the corresponding lactone product (4R,6R)-6-butyl-4-hydroxyoxan-2-one employing the wild-type alcohol dehydrogenase ADHA
Products: -
Products: -
?
additional information
?
-
Substrates: in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. In high-ethanol-producing (ethanologen) strains of Thermoanaerobacterium saccharolyticum, both ALDH and ADH activities show increased NADPH-linked activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-arabinose, L-arabinose, acetophenone, and 4-chloroacetophenone
Products: -
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?
additional information
?
-
Substrates: no oxidation of methanol, methoxyethanol, ethylene glycol, or D-galactose. No reduction of acetone, cyclopentanone, D-arabinose, D-xylose, D-glucose or cellobiose
Products: -
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?
additional information
?
-
-
Substrates: no oxidation of methanol, methoxyethanol, ethylene glycol, or D-galactose. No reduction of acetone, cyclopentanone, D-arabinose, D-xylose, D-glucose or cellobiose
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
(RS)-1-phenylethanol + NAD+
1-phenylethanone + NADH + H+
-
Substrates: 100% activity
Products: -
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?
(RS)-1-phenylethanol + NADP+
1-phenylethanone + NADPH + H+
-
Substrates: 100% activity
Products: -
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?
1-(2-bromophenyl)ethanol + NAD(P)+
1-(2-bromophenyl)ethanone + NAD(P)H + H+
-
Substrates: 11.3% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-(2-chlorophenyl)ethanol + NAD(P)+
1-(2-chlorophenyl)ethanone + NAD(P)H + H+
-
Substrates: 16.4% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-(3-bromophenyl)ethanol + NAD(P)+
1-(3-bromophenyl)ethanone + NAD(P)H + H+
-
Substrates: 315% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-(3-chlorophenyl)ethanol + NAD(P)+
1-(3-chlorophenyl)ethanone + NAD(P)H + H+
-
Substrates: 205% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-(4-bromophenyl)ethanol + NAD(P)+
1-(4-bromophenyl)ethanone + NAD(P)H + H+
-
Substrates: 167% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-(4-chlorophenyl)ethanone + NAD(P)+
1-(4-chlorophenyl)ethanone + NAD(P)H + H+
-
Substrates: 151% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-(4-fluorophenyl)ethanol + NAD(P)+
1-(4-fluorophenyl)ethanol + NAD(P)H + H+
-
Substrates: 119% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-(4-methylphenyl)ethanone + NAD(P)+
1-(4-methylphenyl)ethanol + NAD(P)H + H+
-
Substrates: 189% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-butanol + NAD(P)+
butanal + NAD(P)H + H+
-
Substrates: 2.3% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-heptanol + NAD(P)+
heptanal + NAD(P)H + H+
-
Substrates: 3.3% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-hexanol + NAD(P)+
hexanal + NAD(P)H + H+
-
Substrates: 2.8% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-octanol + NAD(P)+
octanal + NAD(P)H + H+
-
Substrates: 2.3% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-pentanol + NAD(P)+
pentanal + NAD(P)H + H+
-
Substrates: 2.8% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-phenyl-1,2-ethanediol + NAD(P)+
?
-
Substrates: 3.4% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-phenyl-1-propanol + NAD(P)+
1-phenylpropionaldehyde + NAD(P)H + H+
-
Substrates: 13.1% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-phenyl-2-propanol + NAD(P)+
1-phenylpropan-2-one + NAD(P)H + H+
-
Substrates: 39.1% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
1-propanol + NAD(P)+
propionaldehyde + NAD(P)H + H+
-
Substrates: 1.2% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
2,2,2-trifluoroacetophenone + NAD(P)H + H+
2,2,2-trifluoro-1-phenylethan-1-ol + NAD(P)+
-
Substrates: 180% activity compared to acetoin
Products: -
Products: -
?
2-bromoacetophenone + NAD(P)H + H+
1-(2-bromophenyl)ethanone + NAD(P)+
-
Substrates: 8.7% activity compared to acetoin
Products: -
Products: -
?
2-butanol + NAD(P)+
butan-2-one + NAD(P)H + H+
-
Substrates: 22.3% activity compared to (RS)-1-phenylethanol
Products: -
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?
2-chloro-1-phenylethanol + NAD(P)+
2-chloro-1-phenylethan-1-one + NAD(P)H + H+
-
Substrates: 0.3% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
2-heptanol + NAD(P)+
heptan-2-one + NAD(P)H + H+
-
Substrates: 61.6% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
2-hexanol + NAD(P)+
hexan-2-one + NAD(P)H + H+
-
Substrates: 38.7% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
2-hexanone + NAD(P)H + H+
hexan-2-ol + NAD(P)+
-
Substrates: 3.6% activity compared to acetoin
Products: -
Products: -
?
2-octanol + NAD(P)+
octan-2-one + NAD(P)H + H+
-
Substrates: 45.8% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
2-pentanol + NAD(P)+
pentan-2-one + NAD(P)H + H+
-
Substrates: 30.2% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
2-phenylethanol + NAD(P)+
phenylacetaldehyde + NAD(P)H + H+
-
Substrates: 0.3% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
2-propanol + NAD(P)+
propan-2-one + NAD(P)H + H+
-
Substrates: 5.3% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
acetoin + NAD(P)+
butan-2,3-dione + NAD(P)H + H+
-
Substrates: 100% activity
Products: -
Products: -
?
acetoin + NAD(P)H + H+
2,3-butanediol + NAD(P)+
-
Substrates: 4.5% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
acetone + NAD(P)H + H+
propan-2-ol + NAD(P)+
-
Substrates: 4.1% activity compared to acetoin
Products: -
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?
all-trans-retinal + NADPH + H+
all-trans-retinol + NADP+
-
Substrates: -
Products: -
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?
cyclohexanol + NAD(P)+
cyclohexanone + NAD(P)H + H+
-
Substrates: 52.3% activity compared to (RS)-1-phenylethanol
Products: -
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?
cyclohexanone + NAD(P)H + H+
cyclohexanol + NAD(P)+
-
Substrates: 19.1% activity compared to acetoin
Products: -
Products: -
?
D-arabinose + NAD(P)+
?
-
Substrates: 21.4% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
dihydroxyacetone + NAD(P)H + H+
?
-
Substrates: 34.8% activity compared to acetoin
Products: -
Products: -
?
ethanol + NAD(P)+
acetaldehyde + NAD(P)H + H+
-
Substrates: 0.5% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
ethyl pyruvate + NAD(P)H + H+
?
-
Substrates: 294% activity compared to acetoin
Products: -
Products: -
?
hexanal + NAD(P)H + H+
hexan-1-ol + NAD(P)+
-
Substrates: 12.9% activity compared to acetoin
Products: -
Products: -
?
L-arabinose + NAD(P)+
?
-
Substrates: 5.2% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
meso-2,3-butanediol + NAD+
?
-
Substrates: 272% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
meso-2,3-butanediol + NADP+
?
-
Substrates: 272% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
methanol + NAD(P)+
formaldehyde + NAD(P)H + H+
-
Substrates: 0.2% activity compared to (RS)-1-phenylethanol
Products: -
Products: -
?
methyl benzoylformate + NAD(P)H + H+
?
-
Substrates: 67% activity compared to acetoin
Products: -
Products: -
?
phenylacetaldehyde + NAD(P)H + H+
2-phenylethan-1-ol + NAD(P)+
-
Substrates: 18.6% activity compared to acetoin
Products: -
Products: -
?
pyruvic aldehyde + NAD(P)H + H+
?
-
Substrates: 328% activity compared to acetoin
Products: -
Products: -
?
retinaldehyde + NADH
retinol + NAD+
-
Substrates: the enzyme is involved in retinol and vitamin A metabolism, retinoic acid is important in intestinal epithelial cell proliferation and differentiation, the enzyme also plays a role in dietary conversion of beta-carotene to retinol via retinaldehyde
Products: -
Products: -
r
additional information
?
-
Substrates: the enzyme plays an important role in potato defence response to Erwinia carotovora
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with D-arabinose, L-arabinose, acetophenone, and 4-chloroacetophenone
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD(P)H
-
strains B592 and B593, higher activities with NADP(H) than with NAD(H)
NAD+
dual cofactor dependency, NAD+ shows 60% of the activity with NADP+
NAD+
dual cofactor specificity, activity with NAD+ is 14% compared to the activity with NADP+ at pH 11.0 with 4 M KCl
NADH
in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. The AdhE protein of the ethanologenic strain of Clostridium thermocellum has acquired high NADPH-linked ADH activity while maintaining NADH-linked ALDH and ADH activities at wild-type levels
NADH
in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. In high-ethanol-producing (ethanologen) strains of Thermoanaerobacterium saccharolyticum, both ALDH and ADH activities show increased NADPH-linked activity
NADP+
preferred cofactor. Activity with NAD+ is 75% less than that detected with NADP+
NADP+
dual cofactor dependency, NAD+ shows 60% of the activity with NADP+
NADP+
dual cofactor specificity, activity with NAD+ is 14% compared to the activity with NADP+ at pH 11.0 with 4 M KCl
NADPH
-
the specificity towards NADP(H) is determined by residues Gly198, Ser199, Arg200 and Tyr218
NADPH
-
the specificity towards NADP(H) is determined by residues Gly198, Ser199, Arg200 and Tyr218
NADPH
in wild-type strains, NADH is the preferred cofactor for both aldehyde dehydrogenase ALDH and alcohol dehydrogenase ADH activities. In high-ethanol-producing (ethanologen) strains of Thermoanaerobacterium saccharolyticum, both ALDH and ADH activities show increased NADPH-linked activity
NADPH
the ethanol tolerant phenotype of Clostridium thermocellum is primarily due to a mutated bifunctional acetaldehyde-CoA/alcohol dehydrogenase gene (adhE). The mutant displays a complete loss of NADH-dependent activity with concomitant acquisition of NADPH-dependent activity
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
Ca2+ has an stabilizing effect. With 1.0 mM CaCl2, the enzyme is completely stable at 0°C for 2 h and after 3.5 h almost 90% of the initial activity is retained
Co2+
Fe2+
moderately activating the reduction of butanal, but only very weak activation of oxidation of 1-butanol
Fe3+
moderately activating the reduction of butanal, but no activation of oxidation of 1-butanol
KCl
Mn2+
moderately activating the reduction of butanal, but only very weak activation of oxidation of 1-butanol
NaCl
Ni2+
required for reduction of butanal, activates, but only slightly in oxidation of 1-butanol
additional information
Co2+
moderately activating the reduction of butanal, but no activation of oxidation of 1-butanol
KCl
a preference for KCl over NaCl is observed, with best activity at 4 M KCl
KCl
maximally active with ethanol with 4 M KCl. It is maximally active with 1-propanol with 2 M KCl and with 1-butanol and 1-pentanol with 1 M KCl. Optimum activity with the secondary alcohols, 2-propanol and 2-butanol, is observed with 3 M KCl and 2 M KCl, respectively, and with isoamyl alcohol in the presence of 1 M KCl. Maximum activity with benzyl alcohol is detected with 2 M KCl. Catalyzed the reductive reaction optimally at pH 6.0 with 1 M KCl
KCl
activity increases in the presence of KCl is maintained even at concentration of 3 M
NaCl
the enzyme requires high salt concentrations for its activity, a preference for KCl over NaCl is observed
NaCl
activity is increased in the presence of NaCl and remains at the elevated level up to 4 M of NaCl. The rates of 2-propanol and 2,5-hexanediol oxidation are increased by more than 2fold after the addition of NaCl up to 1 M to the assay mixture and is retained at the increased level up to 4 M of NaCl
NaCl
activity increases in the presence of NaCl is maintained even at concentration of 4 M
additional information
no activity with Ca2+, Mg2+, Zn2+, and Cu2+. The Fe2+-reconstituted Ni-PhADH is sensitively and rapidly inactivated by dioxygen gas. The activity of apoform o-PhADH is significantly lower than that of Ni2+-bound PhADH. The enzyme is inactivated by the replacement of the ferrous ion in the active site with another metal ion such as a zinc ion, which has been considered an inhibitor of iron-activating group III ADHs
additional information
metal independency is supported by the absence of a significant effect of TsAdh319 preincubation with 10 mM Me2+ for 30 min before measuring the activity in the presence of 1 mM Me2+ or EDTA
additional information
-
metal independency is supported by the absence of a significant effect of TsAdh319 preincubation with 10 mM Me2+ for 30 min before measuring the activity in the presence of 1 mM Me2+ or EDTA
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8-hydroxyquinoline
-
1 mM, 100% inhibition with NAD+ as cofactor, 40% with NADP+ as cofactor
acetonitrile
complete inhibition in buffer without NaCl and in buffer with 600 mM NaCl
chloroform
21% inhibition in buffer without NaCl, 19% inhibition in buffer with 600 mM NaCl
CuSO4
-
1 mM, 75% inhibition with NAD+ as cofactor, 56% with NADP+ as cofactor
Dimethyl formamide
87% inhibition in buffer without NaCl, 59% inhibition in buffer with 600 mM NaCl
dimethyl sulfoxide
complete inhibition in buffer without NaCl, 60% inhibition in buffer with 600 mM NaCl
ethyl acetate
complete inhibition in buffer without NaCl, 67% inhibition in buffer with 600 mM NaCl
iodoacetic acid
-
1 mM, 29% inhibition with NAD+ as cofactor, 80% with NADP+ as cofactor
methanol
75% inhibition in buffer without NaCl, 81% inhibition in buffer with 600 mM NaCl
n-decane
9% inhibition in buffer without NaCl, slight activation in buffer with 600 mM NaCl
n-hexane
40% inhibition in buffer without NaCl, slight activation in buffer with 600 mM NaCl
4-chloromercuribenzoate
-
0.01 mM, complete inhibition; some protection of partial inhibition resulting from 0.001 mM 4-chloromercuribenzoate in the presence of 1 mM NADP+, almost complete protection with 10 mM hexan-1-ol
FeSO4
-
1 mM, 75% inhibition with NAD+ as cofactor, 46% with NADP+ as cofactor
o-phenanthroline
-
1 mM, 100% inhibition with NAD+ as cofactor, 40% with NADP+ as cofactor
additional information
the Fe2+-reconstituted Ni-PhADH was sensitively and rapidly inactivated by dioxygen gas. The enzyme is inactivated by the replacement of the ferrous ion in the active site with another metal ion such as a zinc ion, which has been considered an inhibitor of iron-activating group III ADHs
-
additional information
-
dithiothreitol and EDTA have no effect on either oxidative or reductive activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
hexane
-
in asymmetric reduction by TeSADH in pure hexane, the organic solvent makes the process more efficient by allowing high concentrations of substrates to be used
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinogenesis
Hypermethylation of DHRS3 as a Novel Tumor Suppressor Involved in Tumor Growth and Prognosis in Gastric Cancer.
Lymphatic Metastasis
Gene expression profiling of papillary thyroid carcinoma identifies transcripts correlated with BRAF mutational status and lymph node metastasis.
Melanoma
Silencing of Peroxiredoxin 2 and aberrant methylation of 33 CpG islands in putative promoter regions in human malignant melanomas.
Neoplasm Metastasis
Gene expression profiling of papillary thyroid carcinoma identifies transcripts correlated with BRAF mutational status and lymph node metastasis.
Neoplasm Metastasis
Induction of cell cycle arrest and inflammatory genes by combined treatment with epigenetic, differentiating, and chemotherapeutic agents in triple-negative breast cancer.
Neoplasms
Biological role of aldo-keto reductases in retinoic Acid biosynthesis and signaling.
Neoplasms
Evaluation of genes identified by microarray analysis in favorable neuroblastoma.
Neoplasms
Hypermethylation of DHRS3 as a Novel Tumor Suppressor Involved in Tumor Growth and Prognosis in Gastric Cancer.
Neoplasms
Identification of allelic expression imbalance genes in human hepatocellular carcinoma through massively parallel DNA and RNA sequencing.
Neoplasms
Induction of cell cycle arrest and inflammatory genes by combined treatment with epigenetic, differentiating, and chemotherapeutic agents in triple-negative breast cancer.
Neoplasms
p53-inducible DHRS3 Is an Endoplasmic Reticulum Protein Associated with Lipid Droplet Accumulation.
Neoplasms
retSDR1, a short-chain retinol dehydrogenase/reductase, is retinoic acid-inducible and frequently deleted in human neuroblastoma cell lines.
Neoplasms
Substrate Specificity, Inhibitor Selectivity and Structure-Function Relationships of Aldo-Keto Reductase 1B15: A Novel Human Retinaldehyde Reductase.
Neoplasms
The retinal dehydrogenase/reductase retSDR1/DHRS3 gene is activated by p53 and p63 but not by mutants derived from tumors or EEC/ADULT malformation syndromes.
Neuroblastoma
retSDR1, a short-chain retinol dehydrogenase/reductase, is retinoic acid-inducible and frequently deleted in human neuroblastoma cell lines.
Non-alcoholic Fatty Liver Disease
Genetic analysis of expression profile involved in retinoid metabolism in non-alcoholic fatty liver disease.
Obesity
p53-inducible DHRS3 Is an Endoplasmic Reticulum Protein Associated with Lipid Droplet Accumulation.
Stomach Neoplasms
Hypermethylation of DHRS3 as a Novel Tumor Suppressor Involved in Tumor Growth and Prognosis in Gastric Cancer.
Triple Negative Breast Neoplasms
Inhibition of retinoic acid receptor ? phosphorylation represses the progression of triple-negative breast cancer via transactivating miR-3074-5p to target DHRS3.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
244
(RS)-1-phenylethanol
-
with NAD+ as cosubstrate, at pH 6.0 and 70°C
61.3
meso-2,3-butanediol
-
with NAD+ as cosubstrate, at pH 6.0 and 70°C
additional information
additional information
Michaelis-Menten kinetics
-
6.7
1-butanol
pH 10.0, temperature not specified in the publication
1.4
acetaldehyde
cosubstrate NADH, moderately ethanol producing strain, pH 7.0, 55°C
1.4
acetaldehyde
cosubstrate NADPH, moderately ethanol producing strain, pH 7.0, 55°C
9.2
acetaldehyde
pH 6.0, temperature not specified in the publication
0.089
NAD+
-
with (RS)-1-phenylethanol as cosubstrate, at pH 6.0 and 70°C
0.127
NAD+
-
with meso-2,3-butanediol as cosubstrate, at pH 6.0 and 70°C
0.17
NADH
moderately ethanol producing strain, pH 7.0, 55°C
0.066
NADP+
-
with (RS)-1-phenylethanol as cosubstrate, at pH 6.0 and 70°C
0.113
NADP+
-
with meso-2,3-butanediol as cosubstrate, at pH 6.0 and 70°C
0.2 - 1
NADP+
pH 10.0, temperature not specified in the publication
0.075
NADPH
moderately ethanol producing strain, pH 7.0, 55°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
35.7
(RS)-1-phenylethanol
-
with NAD+ as cosubstrate, at pH 6.0 and 70°C
43.8
meso-2,3-butanediol
-
with NAD+ as cosubstrate, at pH 6.0 and 70°C
210
acetaldehyde
cosubstrate NADPH, moderately ethanol producing strain, pH 7.0, 55°C
220
acetaldehyde
cosubstrate NADH, moderately ethanol producing strain, pH 7.0, 55°C
10.4
NAD+
-
with (RS)-1-phenylethanol as cosubstrate, at pH 6.0 and 70°C
30.8
NAD+
-
with meso-2,3-butanediol as cosubstrate, at pH 6.0 and 70°C
220
NADH
moderately ethanol producing strain, pH 7.0, 55°C
10.5
NADP+
-
with (RS)-1-phenylethanol as cosubstrate, at pH 6.0 and 70°C
30
NADP+
-
with meso-2,3-butanediol as cosubstrate, at pH 6.0 and 70°C
280
NADPH
moderately ethanol producing strain, pH 7.0, 55°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.15
(RS)-1-phenylethanol
-
with NAD+ as cosubstrate, at pH 6.0 and 70°C
0.71
meso-2,3-butanediol
-
with NAD+ as cosubstrate, at pH 6.0 and 70°C
0.479
1-butanol
pH 10.0, temperature not specified in the publication
0.744
acetaldehyde
pH 6.0, temperature not specified in the publication
150
acetaldehyde
cosubstrate NADH, moderately ethanol producing strain, pH 7.0, 55°C
150
acetaldehyde
cosubstrate NADPH, moderately ethanol producing strain, pH 7.0, 55°C
117
NAD+
-
with (RS)-1-phenylethanol as cosubstrate, at pH 6.0 and 70°C
243
NAD+
-
with meso-2,3-butanediol as cosubstrate, at pH 6.0 and 70°C
1300
NADH
moderately ethanol producing strain, pH 7.0, 55°C
159
NADP+
-
with (RS)-1-phenylethanol as cosubstrate, at pH 6.0 and 70°C
265
NADP+
-
with meso-2,3-butanediol as cosubstrate, at pH 6.0 and 70°C
3700
NADPH
moderately ethanol producing strain, pH 7.0, 55°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.33
-
wild-type enzyme, pH 6.5, 28°C, substrate (4R,6S)-6-(chloromethyl)oxane-2,4-diol
12.9
-
wild-type enzyme, pH 7.0, 28°C, substrate (4R,6R)-6-butyloxane-2,4-diol
4.11
additional information
-
specific activities of enzyme mutants with the different substrates, overview
4.11
-
wild-type enzyme, pH 7.5, 28°C, substrate (4R,6S)-6-(chloromethyl)oxane-2,4-diol
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
10.2
6.8
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
aldehyde reduction, cofactor NADH, NADP dependent activity occurs only at pHs below 7
6 - 8
the enzyme shows around 50% of activity at pH 6.0, pH 6.5, and pH 8.0
6.4 - 7.15
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
70
oxidation of (2S,5S)-2,5-hexanediol, in presence of 1 M NaCl
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 50
30 to 60% of activity is observed between 20° and 30°C and 20% activity at 10 and 50°C, respectively
40 - 80
40°C: about 50% of maximal activity, 80°C: about 70% of maximal activity
50 - 75
50°C: about 50% of maximal activity, 75°C: about 60% of maximal activity, oxidation of (2S,5S)-2,5-hexanediol, in presence of 1 M NaCl
65 - 86
65°C: about 50% of maximal activity, 86°C: about 50% of maximal activity, oxidation of (2S,5S)-2,5-hexanediol, no addition of NaCl
70 - 95
70°C: 60% of maximal activity, 95°C: 70% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional enzyme, C-terminal section belongs to the iron-containing alcohol dehydrogenase family, N-terminal section belongs to the aldehyde dehydrogenase family
UniProt
brenda
bifunctional enzyme, C-terminal section belongs to the iron-containing alcohol dehydrogenase family, N-terminal section belongs to the aldehyde dehydrogenase family
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
no or very low expression in lungs, spleen, pancreas, large intestine and eye
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
evolution
NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes
evolution
-
ADHs structure and function comparisons, SDR family enzymes structure-function comparisons, overview
evolution
-
NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes
-
evolution
-
NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes
-
evolution
-
NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes
-
evolution
-
NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes
-
evolution
-
NAD(P)-dependent group III alcohol dehydrogenases (ADHs), well known as iron-activated enzymes
-
malfunction
-
the optimized ADHA variant shows a 7fold higher oxidative activity, a 26°C increased stability, and is applied to develop an efficient chlorolactol oxidation process
malfunction
Starmerella magnoliae DSMZ 70638
-
the optimized ADHA variant shows a 7fold higher oxidative activity, a 26°C increased stability, and is applied to develop an efficient chlorolactol oxidation process
-
physiological function
-
enzyme ADHA from Candida magnoliae strain DSMZ 70638 is identified to efficiently catalyze the regioselective hydroxy-lactone oxidations to hydroxy-lactones. Hydroxy-lactones are common intermediates in industrial processes to cholesterol lowering (va)statin drugs. ADH catalyzed oxidations can be developed to efficient and safe processes, but the ADHA wild-type enzyme is not productive enough in chlorolactol oxidation
physiological function
Starmerella magnoliae DSMZ 70638
-
enzyme ADHA from Candida magnoliae strain DSMZ 70638 is identified to efficiently catalyze the regioselective hydroxy-lactone oxidations to hydroxy-lactones. Hydroxy-lactones are common intermediates in industrial processes to cholesterol lowering (va)statin drugs. ADH catalyzed oxidations can be developed to efficient and safe processes, but the ADHA wild-type enzyme is not productive enough in chlorolactol oxidation
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A341CHQ2_NEOAA
356
0
39027
TrEMBL
-
A0A4W2G7Z6_BOBOX
356
0
39261
TrEMBL
other Location (Reliability: 1)
A0A5E4BZG8_MARMO
137
0
15317
TrEMBL
other Location (Reliability: 1)
A0A5E4DB41_MARMO
143
0
15892
TrEMBL
Secretory Pathway (Reliability: 1)
A0A5F7ZH47_MACMU
412
0
44437
TrEMBL
other Location (Reliability: 2)
A0A5N3WKD3_MUNMU
223
0
24362
TrEMBL
other Location (Reliability: 3)
A0A7J8A5I6_PIPKU
167
0
18422
TrEMBL
other Location (Reliability: 4)
A0A8C0PNZ8_CANLF
454
0
50510
TrEMBL
other Location (Reliability: 2)
A0A8C2VCT8_CHILA
197
0
21556
TrEMBL
other Location (Reliability: 5)
A0A8C5KGG0_JACJA
180
0
20288
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8C5W2R8_MICMU
248
0
27530
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8C8Y136_PANLE
277
0
31035
TrEMBL
Secretory Pathway (Reliability: 1)
A0A8C9PN18_SPEDA
266
0
29400
TrEMBL
Secretory Pathway (Reliability: 3)
A0AAX6STU6_HETGA
136
0
15079
TrEMBL
Secretory Pathway (Reliability: 1)
A0AB34HMY7_ESCRO
320
0
34797
TrEMBL
Secretory Pathway (Reliability: 1)
G1TIW6_RABIT
378
0
41247
TrEMBL
other Location (Reliability: 3)
G5AM12_HETGA
369
0
41039
TrEMBL
other Location (Reliability: 2)
S7P3A1_MYOBR
609
0
67784
TrEMBL
other Location (Reliability: 2)
A0A0H3W5U9_ACETH
873
0
96010
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0H3W5V0_THESA
859
0
94862
TrEMBL
-
C6A190_THESM
Thermococcus sibiricus (strain DSM 12597 / MM 739)
234
0
26151
TrEMBL
-
D4GP73_HALVD
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
349
0
36992
TrEMBL
other Location (Reliability: 2)
O58517_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
375
0
41389
TrEMBL
-
Q5V676_HALMA
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
384
0
40611
TrEMBL
other Location (Reliability: 1)
Q8H0L8_SOLTU
359
0
39388
TrEMBL
Secretory Pathway (Reliability: 3)
Q9HMB6_HALSA
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
347
0
36203
TrEMBL
Secretory Pathway (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41600
x * 41600, His-tagged protein, SDS-PAGE, mass spectrometry
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.15 A resolution, tetramer of 222 symmetry, the monomer is composed of a cofactor-binding domain and a catalytic domain, it contains a single zinc atom in the putative active side, the tetramer is composed of two dimers
-
2.05 A resolution, tetramer of 222 symmetry, the monomer is composed of a cofactor-binding domain and a catalytic domain, it contains a single zinc atom in the putative active side, the tetramer is composed of two dimers
-
hanging-drop vapour-diffusion method using 25% (w/v) polyethylene glycol 3350 pH 7.5 as precipitant
to 1.68 A resolution, crystals belong to space group I222, with unit-cell parameters a = 55.63, b = 83.25, c = 120.75 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
P704L/H734R
the ethanol tolerant phenotype of Clostridium thermocellum is primarily due to a mutated bifunctional acetaldehyde-CoA/alcohol dehydrogenase gene (adhE). The mutant displays a complete loss of NADH-dependent activity with concomitant acquisition of NADPH-dependent activity. The reduction in specific activity with respect to NADH is far greater (about 25fold less activity) than the increase with respect to NADPH. Although total ADH activity dropps by 25fold, ethanol production does not drop significantly between strains under these conditions
D194A
the mutation results in substantial catalytic deficiency (2.8% compared to the wild type enzyme)
H363A
the mutant with full activity is not able to grow on butanal-containing medium
E43K/S97C/T148S/A155H/P210C/L227V/Y244F
-
site-directed mutagenesis, mutant ADHA-0381, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
E43K/S97C/T148S/T194V/M206D/P210C/L227V
-
site-directed mutagenesis, mutant ADHA-0398, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
S97C/M206D
-
site-directed mutagenesis, mutant ADHA-0279, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
S97C/M206D/P210C
-
site-directed mutagenesis, mutant ADHA-0278, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
S97C/T148S/A155H/P210C/L227V
-
site-directed mutagenesis, mutant ADHA-0391, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
S97C/T148S/A155H/P210C/L227V/Y244F
-
site-directed mutagenesis, mutant ADHA-0384, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
E43K/S97C/T148S/T194V/M206D/P210C/L227V
Starmerella magnoliae DSMZ 70638
-
site-directed mutagenesis, mutant ADHA-0398, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
-
S97C/M206D
Starmerella magnoliae DSMZ 70638
-
site-directed mutagenesis, mutant ADHA-0279, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
-
S97C/M206D/P210C
Starmerella magnoliae DSMZ 70638
-
site-directed mutagenesis, mutant ADHA-0278, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
-
S97C/T148S/A155H/P210C/L227V
Starmerella magnoliae DSMZ 70638
-
site-directed mutagenesis, mutant ADHA-0391, the mutant shows increased thermostability and altered pH conditions compared to the wild-type enzyme
-
G198D
-
site-directed mutagenesis, the variant of the NAD(P)H-dependent ADH, TeSADH, shows a significant switch of cofactor dependence from NADPH towards NADH compared to the wild-type enzyme
W110A
-
site-directed mutagenesis, the mutant is able not only to reduce phenyl-ring-containing ketones with high enantioselectivity, but it can also racemize the corresponding enantiopure alcohols
W110A/I86A
-
site-directed mutagenesis, the mutant of TeSADH reduces phenyl-ring-containing ketones with high enantioselectivity and racemizes the corresponding enantiopure alcohols, and it expands substrate specificity to accommodate ketones bearing two sterically demanding groups
additional information
additional information
-
development of improved enzyme variants ADHA-0398 and -0381 shows +26°C improved melting temperature and 17fold higher oxidative activity at pH 6.5 towards (4R,6S)-6-(chloromethyl)oxane-2,4-diol but only 6fold at pH 7.5, method development, overview
additional information
Starmerella magnoliae DSMZ 70638
-
development of improved enzyme variants ADHA-0398 and -0381 shows +26°C improved melting temperature and 17fold higher oxidative activity at pH 6.5 towards (4R,6S)-6-(chloromethyl)oxane-2,4-diol but only 6fold at pH 7.5, method development, overview
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 8
-
the enzyme shows half-lives of 60-70 h between pH 5.5 and 8.0 at room temperature
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
30
-
no loss of activity after 15 min, complete loss of activity at 60°C
4 - 60
the enzyme is thermally stable when incubated for 30 min between 4 and 40°C. Incubation for 30 min at temperatures between 10 and 30 °C slightly increases the catalytic activity. Recombinant enzyme is completely inactivated at 50 and 60°C
67
-
melting temperature T1/2 of mutant ADHA-0398 and of mutant ADHA-0381
70
70 - 95
the enzyme activity is slightly decreased by 1 h incubation at 70°C (2.6%), 80°C (4.7%), 90°C (7.9%), and 95°C (18.8%), 50% loss of activity after approximately 6 h at 95°C
8 - 25
-
the enzyme has a half-life of 80 h at 25°C and stability optimum between 8 and 15°C in the presence of 0.8 mM CaCl2 (half-life of 130 h)
80
90
95
-
the highly thermostable enzyme has a half-life of 4.5 h at 95°C and 16.2 h at 85°C
additional information
thermal denaturation is fully irreversible and follows first-order kinetics
80
activity begins to decrease after 2 h preincubation. The rate of 2-propanol oxidation is decreased 34% and 58% over 24 h incubation at 80°C in the presence or absence of 1 M NaCl, respectively. Calculated half-life values of the enzyme in buffer with or without 1 M NaCl are 37 vs. 20 h at 80°C, respectively
90
activity begins to decrease after 30 min preincubation. The incubation at 90°C provokes 31% and 40% reduction of 2-propanol oxidation rate in the presence or absence of 1 M NaCl, respectively. Calculated half-life values of the enzyme in buffer with or without 1 M NaCl are 8 vs. 6 h at 90 °C, respectively
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2-propanol
-
high activity (90% of the activity without solvents) is observed in the presence of 20% (v/v)
Acetone
-
high activity (90% of the activity without solvents) is observed in the presence of 20% (v/v)
acetonitrile
dimethyl sulfoxide
dimethylfluoride
-
high activity (90% of the activity without solvents) is observed in the presence of 20% (v/v)
DMSO
Ethanol
-
high activity (90% of the activity without solvents) is observed in the presence of 20% (v/v)
ethylacetate
-
high activity (90% of the activity without solvents) is observed in the presence of 50% (v/v)
Glycerol
hexane
Methanol
octane
-
high activity (90% of the activity without solvents) is observed in the presence of 50% (v/v)
octanol
-
high activity (90% of the activity without solvents) is observed in the presence of 50% (v/v)
tetrahydrofuran
acetonitrile
10%, enzyme retains 69% of activity following incubation
acetonitrile
24 h at 4°C, 13% loss of activity at 5% (v/v), 10% loss of activity at 10% (v/v), complete loss of activity at 30% (v/v)
acetonitrile
-
24 h at 4°C, 13% loss of activity at 5% (v/v), 10% loss of activity at 10% (v/v), complete loss of activity at 30% (v/v)
-
acetonitrile
4°C, 72 h, retains 65% of its original activity following incubation with 5% (v/v) acetonitrile, retains 63% of its original activity following incubation with 10 (v/v) acetonitrile, complete inactivation following incubation with 30 (v/v) dimethyl sulfoxide
acetonitrile
-
4°C, 72 h, retains 65% of its original activity following incubation with 5% (v/v) acetonitrile, retains 63% of its original activity following incubation with 10 (v/v) acetonitrile, complete inactivation following incubation with 30 (v/v) dimethyl sulfoxide
-
dimethyl sulfoxide
10%, enzyme retains 78% of activity following incubation
dimethyl sulfoxide
24 h at 4°C, 11% loss of activity at 5% (v/v), 9% loss of activity at 10% (v/v), 59% loss of activity at 30% (v/v)
dimethyl sulfoxide
-
24 h at 4°C, 11% loss of activity at 5% (v/v), 9% loss of activity at 10% (v/v), 59% loss of activity at 30% (v/v)
-
dimethyl sulfoxide
4°C, 72 h, retains 74% of its original activity following incubation with 5% (v/v) dimethyl sulfoxide, retains 69% of its original activity following incubation with 10 (v/v) dimethyl sulfoxide, retains 47% of its original activity following incubation with 30 (v/v) dimethyl sulfoxide
dimethyl sulfoxide
-
4°C, 72 h, retains 74% of its original activity following incubation with 5% (v/v) dimethyl sulfoxide, retains 69% of its original activity following incubation with 10 (v/v) dimethyl sulfoxide, retains 47% of its original activity following incubation with 30 (v/v) dimethyl sulfoxide
-
DMSO
-
high activity (90% of the activity without solvents) is observed in the presence of 20% (v/v)
Glycerol
stabilizing and cryoprotecting additive for the preservation of the enzyme over a short-time period, 10 days
Glycerol
-
stabilizing and cryoprotecting additive for the preservation of the enzyme over a short-time period, 10 days
-
hexane
-
in asymmetric reduction by TeSADH in pure hexane, the organic solvent makes the process more efficient by allowing high concentrations of substrates to be used
hexane
-
high activity (90% of the activity without solvents) is observed in the presence of 50% (v/v)
Methanol
24 h at 4°C, 8% loss of activity at 5% (v/v), 15% loss of activity at 10% (v/v), 94% loss of activity at 30% (v/v)
Methanol
-
24 h at 4°C, 8% loss of activity at 5% (v/v), 15% loss of activity at 10% (v/v), 94% loss of activity at 30% (v/v)
-
Methanol
4°C, 72 h, retains 70% of its original activity following incubation with 5% (v/v) acetonitrile, retains 67% of its original activity following incubation with 10 (v/v) acetonitrile, retains 39% of its original activity following incubation with 30 (v/v) dimethyl sulfoxide
Methanol
-
4°C, 72 h, retains 70% of its original activity following incubation with 5% (v/v) acetonitrile, retains 67% of its original activity following incubation with 10 (v/v) acetonitrile, retains 39% of its original activity following incubation with 30 (v/v) dimethyl sulfoxide
-
Methanol
-
high activity (90% of the activity without solvents) is observed in the presence of 20% (v/v)
tetrahydrofuran
24 h at 4°C, 37% loss of activity at 5% (v/v), 57% loss of activity at 10% (v/v), complete loss of activity at 30% (v/v)
tetrahydrofuran
-
24 h at 4°C, 37% loss of activity at 5% (v/v), 57% loss of activity at 10% (v/v), complete loss of activity at 30% (v/v)
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, crude enzyme retains half of its original activity following incubation at -20°C for 75 days and almost one third of its original activity following incubation for 42 days
-20°C, retains approximately 80% of its original activity after 10 days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, DEAE-Sephadex A-50, hydroxyapatite, Sephadex G-200
-
DEAE-Sephacel, ammonium sulfate, Sephacryl S300HR, Phenyl-Sepharose, Red A
-
DEAE-Sephacel, CM-cellulose, Sephacryl S300HR, Phenyl-Sepharose, Blue A/DEAE-Sephacel
-
isolation of a gene, that is induced after culture filtrate treatment from Erwinia carotovora
Ni-NTA column chromatography and Superdex 200 pg gel filtration
purified in one step by immobilised Ni-affinity chromatography
recombinant StrepII-tagged enzyme from Escherichia coli strain BL21(DE3) by affinity chromatography, ultrafiltration, and gel filtration
strain B592, DEAE-cellulose, hydroxyapatite, Sephacryl S-300, Matrex Gel Red A
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a hexahistidine-tagged recombinant version of the enzyme is heterologously overexpressed in Haloferax volcanii
expressed in Escherichia coli as a fusion protein with (His)6-tag and 13 amino acid linker at the N-terminal
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
gene PH0743, recombinant expression of StrepII-tagged enzyme in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirschberg, D.; Cederlund, E.; Crosas, B.; Jonsson, A.; Tryggvason, S.; Farres, J.; Pares, X.; Bergmann, T.; Jrnvall, H.
N-terminal acetylation in a third protein family of vertebrate alcohol dehydrogenase/retinal reductase found through a proteomics approach in enzyme characterization
Cell. Mol. Life Sci.
58
1323-1326
2001
Gallus gallus
brenda
Korkhin, Y.; Kalb(Giloa), A.J.; Peretz, M.; Bogin, O.; Burstein, Y.; Frolow, F.
NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii
J. Mol. Biol.
278
967-981
1998
Clostridium beijerinckii, Thermoanaerobacter brockii
brenda
Wales, M.R.; Fewson, C.A.
NADP-dependent alcohol dehydrogenases in bacteria and yeast: purification and partial characterization of the enzymes from Acinetobacter calcoaceticus and Saccharomyces cerevisiae
Microbiology
140
173-183
1994
Acinetobacter calcoaceticus, Bacillus subtilis, Bacillus subtilis NCIMB 3610, Escherichia coli, Escherichia coli ML30, Mycobacterium tuberculosis, Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas putida NCIMB 9494, Rhodococcus rhodochrous, Rhodococcus rhodochrous NCIMB 13259, Rhodotorula graminis, Rhodotorula graminis KGX 39, Saccharomyces cerevisiae, Saccharomyces cerevisiae D273-10B, Streptomyces rimosus, Streptomyces rimosus 4018
brenda
Brophy, P.M.; Crowley, P.; Barrett, J.
A novel NADPH/NADH-dependent aldehyde reduction enzyme isolated from the tapeworm Moniezia expansa
FEBS Lett.
263
305-307
1990
Moniezia expansa
brenda
Hiu, S.F.; Zhu, C.X.; Yan R.T.; Chen, J.S.
Butanol-ethanol dehydrogenase and butanol-ethanol-isopropanol dehydrogenase: different alcohol dehydrogenases in two strains of Clostridium beijerinckii (Clostridium butylicium)
Appl. Environ. Microbiol.
53
697-703
1987
Clostridium beijerinckii
brenda
Hatanaka, A.; Kajiwara, T.; Tomohiro, S.
Purification and properties of alcohol dehydrogenase from Leuconostoc mesenteroides
Agric. Biol. Chem.
38
1819-1833
1974
Leuconostoc mesenteroides, Leuconostoc mesenteroides IFO 3426
-
brenda
Rhodes, M.J.C.
Co-factor specificity of plant alcohol dehydrogenase
Phytochemistry
12
307-314
1973
Cucumis melo
-
brenda
Fidge, N.H.; Goodman, D.S.
The enzymatic reduction of retinal to retinol in rat intestine
J. Biol. Chem.
243
4372-4379
1968
Rattus norvegicus
brenda
Belyaeva, O.V.; Kedishvili, N.Y.
Human pancreas protein 2 (PAN2) has a retinal reductase activity and is ubiquitously expressed in human tissues
FEBS Lett.
531
489-493
2002
Homo sapiens (Q9HBH5)
brenda
Montesano, M.; Hyytiainen, H.; Wettstein, R.; Palva, E.T.
A novel potato defence-related alcohol:NADP+ oxidoreductase induced in response to Erwinia carotovora
Plant Mol. Biol.
52
177-189
2003
Solanum tuberosum (Q8H0L8)
brenda
Thomas, S.; Prabhu, R.; Balasubramanian, K.A.
Retinoid metabolism in the rat small intestine
Br. J. Nutr.
93
59-63
2005
Rattus norvegicus
brenda
Timpson, L.M.; Alsafadi, D.; Mac Donnchadha, C.; Liddell, S.; Sharkey, M.A.; Paradisi, F.
Characterization of alcohol dehydrogenase (ADH12) from Haloarcula marismortui, an extreme halophile from the Dead Sea
Extremophiles
16
57-66
2012
Haloarcula marismortui (Q5V676), Haloarcula marismortui
brenda
Lyashenko, A.V.; Bezsudnova, E.Y.; Gumerov, V.M.; Lashkov, A.A.; Mardanov, A.V.; Mikhailov, A.M.; Polyakov, K.M.; Popov, V.O.; Ravin, N.V.; Skryabin, K.G.; Zabolotniy, V.K.; Stekhanova, T.N.; Kovalchuk, M.V.
Expression, purification and crystallization of a thermostable short-chain alcohol dehydrogenase from the archaeon Thermococcus sibiricus
Acta Crystallogr. Sect. F
66
655-657
2010
Thermococcus sibiricus (C6A190), Thermococcus sibiricus DSM 12597 (C6A190)
brenda
Stekhanova, T.N.; Bezsudnova, E.Y.; Mardanov, A.V.; Gumerov, V.M.; Artemova, N.; Kleymenov, S.Y.; Popov, V.O.
Sodium chloride-induced modulation of the activity and thermal stability of short-chain oxidoreductase from the archaeon Thermococcus sibiricus
Appl. Biochem. Biotechnol.
171
1877-1889
2013
Thermococcus sibiricus (C6A190), Thermococcus sibiricus DSM 12597 (C6A190)
brenda
Stekhanova, T.N.; Mardanov, A.V.; Bezsudnova, E.Y.; Gumerov, V.M.; Ravin, N.V.; Skryabin, K.G.; Popov, V.O.
Characterization of a thermostable short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Thermococcus sibiricus
Appl. Environ. Microbiol.
76
4096-4098
2010
Thermococcus sibiricus (C6A190), Thermococcus sibiricus, Thermococcus sibiricus DSM 12597 (C6A190)
brenda
Timpson, L.M.; Liliensiek, A.K.; Alsafadi, D.; Cassidy, J.; Sharkeym M.A.; Liddell, S.; Allers, T.; Paradisi, F.
A comparison of two novel alcohol dehydrogenase enzymes (ADH1 and ADH2) from the extreme halophile Haloferax volcanii
Appl. Microbiol. Biotechnol.
97
195-203
2012
Haloferax volcanii (D4GP73), Haloferax volcanii DSM 3757 (D4GP73)
brenda
Liliensiek, A.K.; Cassidy, J.; Gucciardo, G.; Whitely, C.; Paradisi, F.
Heterologous overexpression, purification and characterisation of an alcohol dehydrogenase (ADH2) from Halobacterium sp. NRC-1
Mol. Biotechnol.
55
143-149
2013
Halobacterium salinarum (Q9HMB6), Halobacterium salinarum NRC 1 (Q9HMB6), Halobacterium sp. (Q9HMB6), Halobacterium sp. NRC-1 (Q9HMB6)
brenda
Wu, X.; Zhang, C.; Orita, I.; Imanaka, T.; Fukui, T.; Xing, X.H.
Thermostable alcohol dehydrogenase from Thermococcus kodakarensis KOD1 for enantioselective bioconversion of aromatic secondary alcohols
Appl. Environ. Microbiol.
79
2209-2217
2013
Thermococcus kodakarensis
brenda
Brown, S.; Guss, A.; Karpinets, T.; Parks, J.; Smolin, N.; Yang, S.; Land, M.; Klingeman, D.; Bhandiwad, A.; Rodriguez Jr., M.; Raman, B.; Shao, X.; Mielenz, J.; Smith, J.; Keller, M.; Lynd, L.
Mutant alcohol dehydrogenase leads to improved ethanol tolerance in Clostridium thermocellum
Proc. Natl. Acad. Sci. USA
108
13752-13757
2011
Acetivibrio thermocellus (A0A0H3W5U9)
brenda
Elleuche, S.; Fodor, K.; von der Heyde, A.; Klippel, B.; Wilmanns, M.; Antranikian, G.
Group III alcohol dehydrogenase from Pectobacterium atrosepticum: insights into enzymatic activity and organization of the metal ion-containing region
Appl. Microbiol. Biotechnol.
98
4041-4051
2014
Pectobacterium atrosepticum (U6CL97), Pectobacterium atrosepticum DSM18077 (U6CL97)
brenda
Zheng, T.; Olson, D.G.; Tian, L.; Bomble, Y.J.; Himmel, M.E.; Lo, J.; Hon, S.; Shaw, A.J.; van Dijken, J.P.; Lynd, L.R.
Cofactor specificity of the bifunctional alcohol and aldehyde dehydrogenase (AdhE) in wild-type and mutant Clostridium thermocellum and Thermoanaerobacterium saccharolyticum
J. Bacteriol.
197
2610-2619
2015
Acetivibrio thermocellus (A0A0H3W5U9), Thermoanaerobacterium saccharolyticum (A0A0H3W5V0)
brenda
Holec, C.; Neufeld, K.; Pietruszka, J.
P450 BM3 monooxygenase as an efficient NAD(P)H-oxidase for regeneration of nicotinamide cofactors in ADH-catalysed preparative scale biotransformations
Adv. Synth. Catal.
358
1810-1819
2016
Equus caballus, Thermoanaerobacter brockii, Ralstonia sp.
-
brenda
Kulig, J.; Frese, A.; Kroutil, W.; Pohl, M.; Rother, D.
Biochemical characterization of an alcohol dehydrogenase from Ralstonia sp.
Biotechnol. Bioeng.
110
1838-1848
2013
Ralstonia sp., Ralstonia sp. DSM 6428
brenda
Lundova, T.; Zemanova, L.; Malcekova, B.; Skarka, A.; Stambergova, H.; Havrankova, J.; Safr, M.; Wsol, V.
Molecular and biochemical characterisation of human short-chain dehydrogenase/reductase member 3 (DHRS3)
Chem. Biol. Interact.
234
178-187
2015
Homo sapiens
brenda
Ma, C.W.; Zhang, L.; Dai, J.Y;, Xiu, Z.L.
Characterization and cofactor binding mechanism of a novel NAD(P)H-dependent aldehyde reductase from Klebsiella pneumoniae DSM2026
J. Microbiol. Biotechnol.
23
1699-1707
2013
Klebsiella pneumoniae, Klebsiella pneumoniae DSM2026
brenda
Brummund, J.; Sonke, T.; Mueller, M.
Process Development for biocatalytic oxidations applying alcohol dehydrogenases
Org. Process Res. Dev.
19
1590-1595
2015
Rhodococcus ruber
-
brenda
Bartsch, S.; Brummund, J.; Koepke, S.; Straatman, H.; Vogel, A.; Schuermann, M.
Optimization of alcohol dehydrogenase for industrial scale oxidation of lactols
Biotechnol. J.
15
e2000171
2020
Starmerella magnoliae, Starmerella magnoliae DSMZ 70638
brenda
An, J.; Nie, Y.; Xu, Y.
Structural insights into alcohol dehydrogenases catalyzing asymmetric reductions
Crit. Rev. Biotechnol.
39
366-379
2019
Thermoanaerobacter ethanolicus
brenda
Sugimoto, C.; Takeda, K.; Kariya, Y.; Matsumura, H.; Yohda, M.; Ohno, H.; Nakamura, N.
A method of expression for an oxygen-tolerant group III alcohol dehydrogenase from Pyrococcus horikoshii OT3
J. Biol. Inorg. Chem.
22
527-534
2017
Pyrococcus horikoshii (O58517), Pyrococcus horikoshii ATCC 700860 (O58517), Pyrococcus horikoshii DSM 12428 (O58517), Pyrococcus horikoshii JCM 9974 (O58517), Pyrococcus horikoshii NBRC 100139 (O58517), Pyrococcus horikoshii OT-3 (O58517)
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.1.71)
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