Information on EC 1.1.99.36 - alcohol dehydrogenase (nicotinoprotein)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.99.36
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RECOMMENDED NAME
GeneOntology No.
alcohol dehydrogenase (nicotinoprotein)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ethanol + acceptor = acetaldehyde + reduced acceptor
show the reaction diagram
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-
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SYSTEMATIC NAME
IUBMB Comments
ethanol:acceptor oxidoreductase
Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DSM 1069
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-butanol + N,N-dimethyl-4-nitrosoaniline
butanal + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
1-butanol + N,N-dimethyl-4-nitrosoaniline
butanaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
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-
-
-
?
1-hexanol + N,N-dimethyl-4-nitrosoaniline
hexanal + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
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-
-
-
?
1-propanol + N,N-dimethyl-4-nitrosoaniline
propanaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
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-
-
-
?
2-butanol + N,N-dimethyl-4-nitrosoaniline
butanone + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
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-
-
-
?
2-propanol + N,N-dimethyl-4-nitrosoaniline
acetone + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
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-
-
-
?
acetate + N,N-dimethyl-4-nitrosoaniline
? + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
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?
acetophenone + 1-propanol
?
show the reaction diagram
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4.3% yield, enantiomeric excess of 0.99 for (S)-product chiral secondary alcohol
3.8% yield, enantiomeric excess of 0.99 for (S)-product
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r
acetophenone + cyclohexanol
?
show the reaction diagram
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2.8-3.7% yield, depending on the ratio of substrates, enantiomeric excess of 0.95-0.99 for (S)-product chiral secondary alcohol
3.8% yield, enantiomeric excess of 0.99 for (S)-product
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r
acetophenone + ethanol
?
show the reaction diagram
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3.8% yield, enantiomeric excess of 0.99 for (S)-product chiral secondary alcohol
3.8% yield, enantiomeric excess of 0.99 for (S)-product
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r
ethanol + N,N-dimethyl-4-nitrosoaniline
acetaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
ethanol + N,N-dimethyl-4-nitrosoaniline
formaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
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-
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?
methanol + N,N-dimethyl-4-nitrosoaniline
formaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ethanol + N,N-dimethyl-4-nitrosoaniline
acetaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
methanol + N,N-dimethyl-4-nitrosoaniline
formaldehyde + 4-(hydroxylamino)-N,N-dimethylaniline
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no cofactor: NADPH
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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takes part in catalysis
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-butanol
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substrate inhibition
1-propanol
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substrate inhibition
2-butanol
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substrate inhibition
2-propanol
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substrate inhibition
acetaldehyde
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1 mM, 40% inhibition; 40% inhibition at 1 mM, 60% at 2 mM, and 95% at 10 mM
ADP
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10% inhibition at 1 mM, 50% at 10 mM
AMP
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10% inhibition at 1 mM, 50% at 10 mM
ATP
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10% inhibition at 1 mM, 50% at 10 mM
Cu2+
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1 mM, 90% inhibition; 90% inhibition at 1 mM
ethanol
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substrate inhibition
Fe2+
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1 mM, 90% inhibition; 90% inhibition at 1 mM
Hg2+
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100% inhibition at 1 mM
Isobutyramide
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competitive to N,N-dimethyl-4-nitrosoaniline
KCN
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2 mM, 90% inhibition; 90% inhibition at 2 mM
NaN3
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25% inhibition at 2 mM; 2 mM, 25% inhibition
Ni2+
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15% inhibition at 1 mM
trans-4-(N,N-dimethylamino)-cinnamaldehyde
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inhibition through direct binding to the catalytic zinc ion in a substrate-like geometry. This binding is accompanied by a characteristic red shift of the aldehyde absorbance from 398 nm to 467 nm
trifluoroethanol
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nonreactive substrate analogue, competitive to ethanol
Zn2+
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1 mM, 40% inhibition; 40% inhibition at 1 mM
additional information
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NAD(H) and NADP(H) do neither inhibit nor stimulate NDMA-ADH activity; NAD(H) and NADP(H) neither inhibit nor stimulate NDMA-ADH activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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NAD(H) and NADP(H) neither inhibit nor stimulate NDMA-ADH activity; no activation by phosphate and ammonium chloride. NAD(H) and NADP(H) do neither inhibit nor stimulate NDMA-ADH activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025
1-butanol
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pH 7.0, 45C
0.0039
1-propanol
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pH 7.0, 45C
10.1
2-butanol
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pH 7.0, 45C
13.4
2-propanol
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pH 7.0, 45C
0.082
ethanol
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pH 7.0, 45C
additional information
additional information
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kinetics
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65
1-butanol
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pH 7.0, 45C
4
1-propanol
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pH 7.0, 45C
4.4
2-butanol
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pH 7.0, 45C
14.5
2-propanol
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pH 7.0, 45C
33
ethanol
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pH 7.0, 45C
0.046
Isobutyramide
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pH 7.0, 20C
0.0016 - 0.0033
trans-4-(N,N-dimethylamino)-cinnamaldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.003
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substrate methanol, pH 7.0, 45C, extracts of cells grown on ethanol
0.004
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substrate ethanol, pH 7.0, 45C, extracts of cells grown on ethanol
0.005
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substrate methanol, pH 7.0, 45C, extracts of cells grown in fed-batch culture on methanol
0.018
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substrate ethanol, pH 7.0, 45C, extracts of cells grown in fed-batch culture on methanol
3.1
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45C, pH 7.0, purified enzyme; purified enzyme, pH 7.0, 45C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
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native PAGE; PAGE
120000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 38970, calculated
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
docking study of trans-4-(N,N-dimethylamino)-cinnamaldehyde to the enzyme model active site. The np-ADH model accommodates the inhibitor in a substrate-like conformation without collision with inner-sphere and secondary sphere residues
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 163fold to homogeneity by ammonium sulfate fractionation, hydrophobic interaction chromatography, ultrafiltration, anion exchange and hydroxyapatite chromatography, followed by gel filtration
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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enzyme catalyzes the asymmetric reduction of ketones using cheap reductants, such as ethanol, with high stereoselectivity, but the reaction is too slow to obtain good yields. For developing biotransformations of industrial interest using nicotinoprotein alcohol dehydrogenases, the attention should be focused on enzymes with a higher reactivity towards prochiral ketones and secondary alcohols