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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Geobacillus thermodenitrificans and UniProt Accession A4ISB9

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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
                1.1.1.1 alcohol dehydrogenase
IUBMB Comments
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
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This record set is specific for:
Geobacillus thermodenitrificans
UNIPROT: A4ISB9
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The taxonomic range for the selected organisms is: Geobacillus thermodenitrificans
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
adh, alcohol dehydrogenase, aldehyde dehydrogenase, adh1b, short-chain dehydrogenase/reductase, ssadh, adh1c, yeast alcohol dehydrogenase, retinol dehydrogenase, faldh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 kDa allergen
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-
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ADH
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-
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ADH-A2
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-
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ADH-B2
-
-
-
-
ADH-C2
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-
-
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ADH-HT
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-
-
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ADH3
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-
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alcohol dehydrogenase (NAD)
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-
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Alcohol dehydrogenase-B2
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aldehyde reductase
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aliphatic alcohol dehydrogenase
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dehydrogenase, alcohol
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ethanol dehydrogenase
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FALDH
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-
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FDH
-
-
-
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Gastric alcohol dehydrogenase
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-
-
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Glutathione-dependent formaldehyde dehydrogenase
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-
-
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GSH-FDH
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-
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NAD-dependent alcohol dehydrogenase
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-
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NAD-specific aromatic alcohol dehydrogenase
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-
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NADH-alcohol dehydrogenase
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-
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NADH-aldehyde dehydrogenase
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-
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Octanol dehydrogenase
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-
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primary alcohol dehydrogenase
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-
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Retinol dehydrogenase
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yeast alcohol dehydrogenase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
alcohol:NAD+ oxidoreductase
A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-72-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-propanediol + 2 NAD+ + H2O
propanedial + 2 NADH + 2 H+
show the reaction diagram
-
-
-
r
acetaldehyde + NADH + H+
ethanol + NAD+
show the reaction diagram
-
-
-
r
butan-1-ol + NAD+
butanal + NADH + H+
show the reaction diagram
-
-
-
r
decan-1-ol + NAD+
decanal + NADH + H+
show the reaction diagram
-
-
-
r
dodecan-1-ol + NAD+
dodecanal + NADH + H+
show the reaction diagram
-
-
-
r
eicosan-1-ol + NAD+
n-eicosanal + NADH + H+
show the reaction diagram
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH + H+
show the reaction diagram
ethanol is the best substrate
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-
r
ethanol + NADP+
acetaldehyde + NADPH + H+
show the reaction diagram
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-
-
r
formaldehyde + NADH + H+
methanol + NAD+
show the reaction diagram
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-
-
r
glycerol + NAD+
dihydroxyacetone + NADH + H+
show the reaction diagram
-
-
-
r
hexadecan-1-ol + NAD+
hexadecanal + NADH + H+
show the reaction diagram
-
-
-
r
hexan-1-ol + NAD+
hexanal + NADH + H+
show the reaction diagram
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-
-
r
isoamylalcohol + NAD+
3-methylbutanal + NADH + H+
show the reaction diagram
-
-
-
r
isopropanol + NAD+
propan-2-one + NADH + H+
show the reaction diagram
-
-
-
r
methanol + NAD+
formaldehyde + NADH + H+
show the reaction diagram
-
-
-
r
octacosan-1-ol + NAD+
octacosanal + NADH + H+
show the reaction diagram
-
-
-
r
octadecan-1-ol + NAD+
octadecanal + NADH + H+
show the reaction diagram
-
-
-
r
octan-1-ol + NAD+
octanal + NADH + H+
show the reaction diagram
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-
-
r
tetracosanol-1-ol + NAD+
tetracosanal + NADH + H+
show the reaction diagram
-
-
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r
tetradecan-1-ol + NAD+
tetradecanal + NADH + H+
show the reaction diagram
-
-
-
r
triacontan-1-ol + NAD+
triacontanal + NADH + H+
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
NAD+ is about 2fold preferred over NADP+
NADP+
NAD+ is about 2fold preferred over NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
1 mM, 136.1% of initial activity
Na+
1 mM, 110.5% of initial activity
additional information
purified enzyme does not contain a significant amount of Fe, Ca, Co, Cu, Mg, Mn or Zn
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Al3+
1 mM, 18.9% of initial activity
Ca2+
1 mM, 98.4% of initial activity
Co2+
1 mM, 51.9% of initial activity
Cu2+
1 mM, 44.2% of initial activity
K+
1 mM, 70.3% of initial activity
Mg2+
1 mM, 74.35% of initial activity
Mn2+
1 mM, 14.3% of initial activity
Ni2+
1 mM, 72.7% of initial activity
SDS
1 mM, 2.9% of initial activity
Zn2+
1 mM, 30.5% of initial activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
1 mM, 105.7% of initial activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.71
acetaldehyde
pH 8, 60°C
7.55
ethanol
pH 8, 60°C
1.51
NAD+
cosubstrate ethanol, pH 8, 60°C
1.4
NADH
cosubstrate acetaldehyde, pH 8, 60°C
0.28
NADP+
cosubstrate ethanol, pH 8, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
404.8
acetaldehyde
pH 8, 60°C
638.7
ethanol
pH 8, 60°C
443.1
NAD+
cosubstrate ethanol, pH 8, 60°C
1645.7
NADH
cosubstrate acetaldehyde, pH 8, 60°C
43.9
NADP+
cosubstrate ethanol, pH 8, 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
85.9
acetaldehyde
pH 8, 60°C
84.6
ethanol
pH 8, 60°C
293.4
NAD+
cosubstrate ethanol, pH 8, 60°C
1175.5
NADH
cosubstrate acetaldehyde, pH 8, 60°C
156.9
NADP+
cosubstrate ethanol, pH 8, 60°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
447.6
substrate ethanol, pH 8, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
8 * 45000, SDS-PAGE, 8 * 41664, calculated from sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
14 h, more than 50% of initial activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, purification by nickel ion affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, X.; Dong, Y.; Zhang, J.; Zhang, A.; Wang, L.; Feng, L.
Two novel metal-independent long-chain alkyl alcohol dehydrogenases from Geobacillus thermodenitrificans NG80-2
Microbiology
155
2078-2085
2009
Geobacillus thermodenitrificans (A4IP64), Geobacillus thermodenitrificans NG80-2 (A4IP64), Geobacillus thermodenitrificans NG80-2
Manually annotated by BRENDA team