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Information on EC 1.1.1.1 - alcohol dehydrogenase and Organism(s) Geobacillus stearothermophilus and UniProt Accession P42328

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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 stearothermophilus
UNIPROT: P42328
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The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
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
-
-
-
-
ADH-A2
-
-
-
-
ADH-B2
-
-
-
-
ADH-C2
-
-
-
-
ADH-HT
-
-
-
-
ADH3
-
-
-
-
alcohol dehydrogenase (NAD)
-
-
-
-
Alcohol dehydrogenase-B2
-
-
-
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aldehyde reductase
-
-
-
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aliphatic alcohol dehydrogenase
-
-
-
-
dehydrogenase, alcohol
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-
-
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ethanol dehydrogenase
-
-
-
-
FALDH
-
-
-
-
FDH
-
-
-
-
Gastric alcohol dehydrogenase
-
-
-
-
Glutathione-dependent formaldehyde dehydrogenase
-
-
-
-
GSH-FDH
-
-
-
-
NAD-dependent alcohol dehydrogenase
-
-
-
-
NAD-specific aromatic alcohol dehydrogenase
-
-
-
-
NADH-alcohol dehydrogenase
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-
-
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NADH-aldehyde dehydrogenase
-
-
-
-
Octanol dehydrogenase
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-
-
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primary alcohol dehydrogenase
-
-
-
-
Retinol dehydrogenase
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-
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yeast alcohol dehydrogenase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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-
-
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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
-
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 + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
1-butanol + NAD+
butyraldehyde + NADH + H+
show the reaction diagram
-
-
-
?
1-propanol + NAD+
propionaldehyde + NADH + H+
show the reaction diagram
-
-
-
?
12-hydroxylauric acid methyl ester + NAD+
12-oxolauric acid methyl ester + NADH + H+
show the reaction diagram
-
product is a key intermediate for biobased polyamide 12 production
-
?
12-oxolauric acid methyl ester + NADH + H+
12-hydroxylauric acid methyl ester + NAD+
show the reaction diagram
-
-
-
?
2-butanol + NAD+
2-butanone + NADH + H+
show the reaction diagram
-
-
-
?
4-methoxybenzaldehyde + NADH + H+
4-methoxybenzyl alcohol + NAD+
show the reaction diagram
-
51% of the activity with butan-2-ol
-
?
acetaldehyde + NADH + H+
ethanol + NAD+
show the reaction diagram
benzaldehyde + NADH + H+
benzyl alcohol + NAD+
show the reaction diagram
-
93% of the activity with butan-2-ol
-
r
benzyl alcohol + NAD+
benzaldehyde + NADH + H+
show the reaction diagram
butan-2-ol + NAD+
butanone + NADH + H+
show the reaction diagram
-
83% of the activity with butan-2-ol
-
?
butyraldehyde + NAD+
n-butanol + NADH + H+
show the reaction diagram
-
-
-
r
cyclopentanol + NAD+
cyclopentanone + NADH + H+
show the reaction diagram
-
92% of the activity with butan-2-ol
-
?
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
proton and hydride equivalent transfer in the alcohol dehydrogenase enzymatic reaction are modulated by the correlated motions between NAD+ and the cofactor domain
-
-
?
ethanol + NAD+
acetaldehyde + NADH + H+
show the reaction diagram
iso-propanol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
methanol + NAD+
formaldehyde + NADH + H+
show the reaction diagram
-
-
-
?
n-butanol + NADH + H+
butyraldehyde + NAD+
show the reaction diagram
-
-
-
r
pentan-1-ol + NAD+
pentanal + NADH + H+
show the reaction diagram
-
76% of the activity with butan-2-ol
-
?
pentan-2-ol + NAD+
pentan-2-one + NADH + H+
show the reaction diagram
-
93% of the activity with butan-2-ol
-
?
prop-2-en-1-ol + NAD+
prop-2-enal + NADH + H+
show the reaction diagram
-
85% of the activity with butan-2-ol
-
?
propan-1-ol + NAD+
propanal + NADH + H+
show the reaction diagram
-
68% of the activity with butan-2-ol
-
r
propan-2-ol + NAD+
acetone + NADH + H+
show the reaction diagram
-
79% of the activity with butan-2-ol
-
?
propanal + NADH + H+
propan-1-ol + NAD+
show the reaction diagram
-
38% of the activity with butan-2-ol
-
r
tert-butanol + NAD+
butyraldehyde + NADH + H+
show the reaction diagram
-
-
-
?
2-propanol + NAD+
aceton + NADH + H+
show the reaction diagram
-
-
irreversible, no measurable activity with acetone
-
ir
cinnamaldehyde + NADH + H+
cinnamyl alcohol + NAD+
show the reaction diagram
-
-
-
-
r
cinnamyl alcohol + NAD+
cinnamaldehyde + NADH + H+
show the reaction diagram
-
-
-
-
r
ethanol + NAD+
acetaldehyde + NADH
show the reaction diagram
-
-
-
-
?
propan-2-ol + NAD+
acetone + NADH + H+
show the reaction diagram
-
-
synthesis of [4R-(2)H]NADH with high yield by enzymatic oxidation of 2-propanol-d(8)
-
?
secondary alcohol + NAD+
aldehyde + NADH
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
1 catalytic zinc ion and 1 structural zinc ion per enzyme subunit
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
23.64
1,3-Propanediol
pH 7.5, 23°C
2.45
1-butanol
pH 7.5, 23°C
39.8
1-propanol
pH 7.5, 23°C
0.086 - 0.1
12-hydroxylauric acid methyl ester
0.066
12-oxolauric acid methyl ester
wild-type, pH 8.0, 60°C
23.82
2-butanol
pH 7.5, 23°C
0.364
acetaldehyde
wild-type, pH 8.0, 60°C
0.8 - 16.5
benzyl alcohol
0.108
Butyraldehyde
wild-type, pH 8.0, 60°C
0.91 - 2.95
ethanol
1.26
iso-propanol
pH 7.5, 23°C
294.23
methanol
pH 7.5, 23°C
0.611
n-butanol
wild-type, pH 8.0, 60°C
0.2 - 14.8
NAD+
0.072
NADH
wild-type, pH 8.0, 60°C
568.84
tert-butanol
pH 7.5, 23°C
57.8
2-propanol
-
pH 7.7, 60°C
0.03
cinnamaldehyde
-
pH 7.7, 60°C
0.11
cinnamyl alcohol
-
pH 7.7, 60°C
0.45
NAD+
-
pH 7.7, 60°C
0.016
NADH
-
pH 7.7, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041
1,3-Propanediol
pH 7.5, 23°C
0.004
1-butanol
pH 7.5, 23°C
0.019
1-propanol
pH 7.5, 23°C
27.6 - 34.3
12-hydroxylauric acid methyl ester
308
12-oxolauric acid methyl ester
wild-type, pH 8.0, 60°C
0.094
2-butanol
pH 7.5, 23°C
681
acetaldehyde
wild-type, pH 8.0, 60°C
5.5 - 24.9
benzyl alcohol
931
Butyraldehyde
wild-type, pH 8.0, 60°C
0.019 - 365
ethanol
0.076
iso-propanol
pH 7.5, 23°C
0.013
methanol
pH 7.5, 23°C
195
n-butanol
wild-type, pH 8.0, 60°C
1 - 34.2
NAD+
326
NADH
wild-type, pH 8.0, 60°C
0.026
tert-butanol
pH 7.5, 23°C
287
2-propanol
-
pH 7.7, 60°C
55
cinnamaldehyde
-
pH 7.7, 60°C
43
cinnamyl alcohol
-
pH 7.7, 60°C
33
NAD+
-
pH 7.7, 60°C
43
NADH
-
pH 7.7, 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00171
1,3-Propanediol
pH 7.5, 23°C
0.00167
1-butanol
pH 7.5, 23°C
0.00046
1-propanol
pH 7.5, 23°C
320 - 340
12-hydroxylauric acid methyl ester
4700
12-oxolauric acid methyl ester
wild-type, pH 8.0, 60°C
0.00396
2-butanol
pH 7.5, 23°C
1900
acetaldehyde
wild-type, pH 8.0, 60°C
8600
Butyraldehyde
wild-type, pH 8.0, 60°C
0.00626 - 340
ethanol
0.06027
iso-propanol
pH 7.5, 23°C
0.000044
methanol
pH 7.5, 23°C
320
n-butanol
wild-type, pH 8.0, 60°C
100
NAD+
wild-type, pH 8.0, 60°C
4500
NADH
wild-type, pH 8.0, 60°C
0.000046
tert-butanol
pH 7.5, 23°C
5
2-propanol
-
pH 7.7, 60°C
1835
cinnamaldehyde
-
pH 7.7, 60°C
391
cinnamyl alcohol
-
pH 7.7, 60°C
73
NAD+
-
pH 7.7, 60°C
2687
NADH
-
pH 7.7, 60°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1
Butyraldehyde
wild-type, pH 8.0, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
reduction of acetaldehyde
9
-
recombinant enzyme
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
-
recombinant enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
isoelectric focusing
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ADH3_GEOSE
339
0
36338
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
4 * 37000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with trifluoroethanol and without NAD+, X-ray diffraction structure determination and analysis at 2.35 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C257L
mutation introduced to improve stability under oxidzing conditions. Mutant exhibits prolonged stability and an elevated inactivation temperature
V260A
kinetic parameters and temperature dependencies similar to wild-type
W49F/W167Y
kinetic parameters and temperature dependencies similar to wild-type
W49F/W167Y/V260A
kinetic parameters and temperature dependencies similar to wild-type
W49F/W87F
kinetic parameters and temperature dependencies similar to wild-type
W49F/W87F/V260A
kinetic parameters and temperature dependencies similar to wild-type
W87A
mutation results in a loss of the Arrhenius break seen at 30°C for the wild-type enzyme and an increase in cold lability due to destabilization of the active tetrameric form. Kinetic isotope effects are nearly temperature-independent over the experimental temperature range, and similar in magnitude to those measured above 30°C for the wild-type enzyme
W87F
investigation on protein dynamics on the microsecond time scale. Mutant exhibits a fast, temperature-independent microsecond decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results rule out an ionizing histidine as the origin of the fluorescence quenching. A Trp49-containing dimer interface may act as a conduit for thermally activated structural change within the protein interior
W87F/H43A
investigation on protein dynamics on the microsecond time scale. Mutant exhibits a fast, temperature-independent microsecond decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results rule out an ionizing histidine as the origin of the fluorescence quenching. A Trp49-containing dimer interface may act as a conduit for thermally activated structural change within the protein interior
Y25A/W49F/W167Y
kinetic parameters and temperature dependencies similar to wild-type
Y25A/W49F/W167Y/V260A
kinetic parameters and temperature dependencies similar to wild-type
Y25A/W49F/W87F
kinetic parameters and temperature dependencies similar to wild-type
Y25A/W49F/W87F/V260A
kinetic parameters and temperature dependencies similar to wild-type
additional information
mutations Y25A (at the dimer interface) and V260A (at the cofactor-binding domain) exhibit opposing low-temperature effects on the hydride tunneling step. The distal Y25A increases active-site flexibility, V260A introduces a temperature-dependent equilibration process, and the double mutant (Y25A/V260A) eliminates the temperature-dependent transition sensed by the active-site tryptophan in the presence of V260A. V260A displays a structural change in the active-site environment/solvation
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62.6
wild-type, thermal denaturation midpoint
65.3
mutant C257L, thermal denaturation midpoint
68
-
purified recombinant enzyme, most stable at
85
-
remaining activity
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly stable against 0.1 M urea and 0.05% SDS
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1-butanol
10%, 29% residual activity
1-propanol
10%, 38% residual activity
Ethanol
10%, 86% residual activity
Methanol
10%, 100% residual activity
urea
0.1 M, 40% residual activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
15°C, 50 mM sodium phosphate buffer, pH 8.0, half-life of wild-type 7 h, half-life of mutant C257L 17 h
4°C, 50 mM sodium phosphate buffer, pH 7.0, 10 mM 2-mercaptoethanol, 10% glycerol, both wild-type and mutant C357L stable for several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
reombinant fusion enzyme by glutathione affinity chromatography, cleavage of GST fusion tag by thrombin, further purification of the active enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression as GST-fusion protein in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
semi-preparative biocatalysis at 60°C using the stabilized mutant C257L, employing butyraldehyde for in situ cofactor regeneration with only catalytic amounts of NAD+, yields up to 23% conversion of omega-hydroxy lauric acid methyl ester to omega-oxo lauric acid methyl ester after 30 min
biotechnology
-
possible usage of the enzyme in bioindustrial processes and as biosensor
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ceccarelli, C.; Liang, Z.X.; Strickler, M.; Prehna, G.; Goldstein, B.M.; Klinman, J.P.; Bahnson, B.J.
Crystal structure and amide H/D exchange of binary complexes of alcohol dehydrogenase from Bacillus stearothermophilus: insight into thermostability and cofactor binding
Biochemistry
43
5266-5277
2004
Geobacillus stearothermophilus (P42328), Geobacillus stearothermophilus, Geobacillus stearothermophilus LLD-R (P42328)
Manually annotated by BRENDA team
Shim, E.J.; Jeon, S.H.; Kong, K.H.
Overexpression, purification, and biochemical characterization of the thermostable NAD-dependent alcohol dehydrogenase from Bacillus stearothermophilus
J. Microbiol. Biotechnol.
13
738-744
2003
Geobacillus stearothermophilus
-
Manually annotated by BRENDA team
Zhang, X.; Bruice, T.C.
Temperature-dependent structure of the E x S complex of Bacillus stearothermophilus alcohol dehydrogenase
Biochemistry
46
837-843
2007
Geobacillus stearothermophilus (P42328), Geobacillus stearothermophilus
Manually annotated by BRENDA team
Pennacchio, A.; Rossi, M.; Raia, C.A.
Synthesis of cinnamyl alcohol from cinnamaldehyde with Bacillus stearothermophilus alcohol dehydrogenase as the isolated enzyme and in recombinant E. coli cells
Appl. Biochem. Biotechnol.
170
1482-1490
2013
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Kirmair, L.; Seiler, D.L.; Skerra, A.
Stability engineering of the Geobacillus stearothermophilus alcohol dehydrogenase and application for the synthesis of a polyamide 12 precursor
Appl. Microbiol. Biotechnol.
99
10501-10513
2015
Geobacillus stearothermophilus (P42328), Geobacillus stearothermophilus
Manually annotated by BRENDA team
Guagliardi, A.; Martino, M.; Iaccarino, I.; De Rosa, M.; Rossi, M.; Bartolucci, S.
Purification and characterization of the alcohol dehydrogenase from a novel strain of Bacillus stearothermophilus growing at 70C
Int. J. Biochem. Cell Biol.
28
239-246
1996
Geobacillus stearothermophilus (P42328), Geobacillus stearothermophilus
Manually annotated by BRENDA team
Meadows, C.W.; Tsang, J.E.; Klinman, J.P.
Picosecond-resolved fluorescence studies of substrate and cofactor-binding domain mutants in a thermophilic alcohol dehydrogenase uncover an extended network of communication
J. Am. Chem. Soc.
136
14821-14833
2014
Geobacillus stearothermophilus (P42328)
Manually annotated by BRENDA team
Meadows, C.W.; Balakrishnan, G.; Kier, B.L.; Spiro, T.G.; Klinman, J.P.
Temperature-jump fluorescence provides evidence for fully reversible microsecond dynamics in a thermophilic alcohol dehydrogenase
J. Am. Chem. Soc.
137
10060-10063
2015
Geobacillus stearothermophilus (P42328)
Manually annotated by BRENDA team
Nagel, Z.D.; Cun, S.; Klinman, J.P.
Identification of a long-range protein network that modulates active site dynamics in extremophilic alcohol dehydrogenases
J. Biol. Chem.
288
14087-14097
2013
Geobacillus stearothermophilus (P42328), Moraxella sp. (Q8GIX7), Moraxella sp. TAE123 (Q8GIX7)
Manually annotated by BRENDA team
Pennacchio, A.; Giordano, A.; Esposito, L.; Langella, E.; Rossi, M.; Raia, C.A.
Insight into the stereospecificity of short-chain thermus thermophilus alcohol dehydrogenase showing pro-S hydride transfer and prelog enantioselectivity
Protein Pept. Lett.
17
437-443
2010
Geobacillus stearothermophilus, Thermus thermophilus, Thermus thermophilus BH27
Manually annotated by BRENDA team
Guo, X.; Feng, Y.; Wang, X.; Liu, Y.; Liu, W.; Li, Q.; Wang, J.; Xue, S.; Zhao, Z.K.
Characterization of the substrate scope of an alcohol dehydrogenase commonly used as methanol dehydrogenase
Bioorg. Med. Chem. Lett.
29
1446-1449
2019
Geobacillus stearothermophilus (P42328), Geobacillus stearothermophilus DSM 2334 (P42328), Geobacillus stearothermophilus DSM 2334
Manually annotated by BRENDA team