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Literature summary extracted from

  • Elleuche, S.; Fodor, K.; Klippel, B.; von der Heyde, A.; Wilmanns, M.; Antranikian, G.
    Structural and biochemical characterisation of a NAD+-dependent alcohol dehydrogenase from Oenococcus oeni as a new model molecule for industrial biotechnology applications (2013), Appl. Microbiol. Biotechnol., 97, 8963-8975.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.1 gene adh3, sequence comparison, expression of N-terminally His-tagged enzyme in Escherichia coli strains NovaBlue Singles and M15[pREP4] Oenococcus oeni
1.1.1.202 expression in Escherichia coli Oenococcus oeni

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.1 purified recombinant N-terminally His-tagged Adh3, hanging drop vapour diffusion method, mixing of 0.002 ml of 80mg/ml protein in 50 mM Tris, pH 7.0, with 0.002 ml of reservoir solution, comprising 0.1 M MES, pH 6.5, 16% w/w PEG 20000, and 0.001 ml of 50 mM CaCl2, 20°C, X-ray diffraction structure determination and analysis Oenococcus oeni
1.1.1.202 to 3.2 A resolution. The electron density map around the active site shows no sign of a bound co-factor, but the active site metal could be located and identified as Ni2+ Oenococcus oeni

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.1 EDTA
-
 Oenococcus oeni
1.1.1.1 Zn2+ complete inhibition Oenococcus oeni
1.1.1.202 imidazole activity is reduced down to 32% in the presence of 1 mM imidazole and addition of 250 mM results in complete inactivity Oenococcus oeni

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.1 0.05
-
 NAD+ pH 9.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 0.2
-
 NADH pH 8.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 2.6
-
 acetaldehyde pH 8.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 10.4
-
 ethanol pH 9.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 11.5
-
 1,2-propanediol pH 8.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 26.7
-
 1,3-Propanediol pH 9.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.202 0.05
-
 NAD+ pH 9.0, 60°C Oenococcus oeni
1.1.1.202 0.2
-
 NADH pH 8.0, 60°C Oenococcus oeni
1.1.1.202 11.5
-
 1,2-propanediol pH 9.0, 60°C Oenococcus oeni
1.1.1.202 26.7
-
 1,3-Propanediol pH 9.0, 60°C Oenococcus oeni

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.1 Mg2+ 40% activation at 10 mM Oenococcus oeni
1.1.1.1 additional information Adh3 exhibits tolerance to several metal ions Oenococcus oeni
1.1.1.1 Na+ 40% activation at 1 mM Oenococcus oeni
1.1.1.1 Ni2+ activates, the activity using 1,3-propanediol as substrate is highly dependent on the addition of NiCl2, while no change in activity is observed using ethanol in a sample with NiCl2 Oenococcus oeni
1.1.1.202 Ni2+ located near active site, crystallization data. The activity with 1,3-propanediol is highly dependent on the presence of Ni2+ Oenococcus oeni

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.1 74000
-
 recombinant His-tagged enzyme, gel filtration Oenococcus oeni
1.1.1.202 42200
-
 2 * 42200, calculated, 2 * 43000, SDS-PAGE of recombinant His-tagged protein Oenococcus oeni
1.1.1.202 43000
-
 2 * 42200, calculated, 2 * 43000, SDS-PAGE of recombinant His-tagged protein Oenococcus oeni
1.1.1.202 74000
-
 gel filtration Oenococcus oeni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.1 ethanol + NAD+ Oenococcus oeni
-
 acetaldehyde + NADH + H+
-
 r

Organic Solvent Stability

EC Number Organic Solvent Comment Organism
1.1.1.1 additional information Adh3 exhibits tolerance to several organic solvents Oenococcus oeni

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Oenococcus oeni
-
 gene adh3
-
1.1.1.1 Oenococcus oeni DSM 20252
-
 gene adh3
-
1.1.1.202 Oenococcus oeni A0NIJ1
-
-
1.1.1.202 Oenococcus oeni ATCC BAA-1163 A0NIJ1
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.1 0.2
-
 substrates 1,3-propanediol and NAD+, pH 9.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 0.2
-
 substrates acetaldehyde and NADH, pH 8.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 0.3
-
 substrates 1,3-propanediol and NAD+, pH 9.0, 60°C, recombinant enzyme, with NiCl2 addition Oenococcus oeni
1.1.1.1 1.1
-
 substrates ethanol and NAD+, pH 9.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.202 1.1
-
 pH 9.0, 60°C Oenococcus oeni

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 1,2-propanediol + NAD+
-
 Oenococcus oeni ?
-
 ?
1.1.1.1 1,2-propanediol + NAD+
-
 Oenococcus oeni DSM 20252 ?
-
 ?
1.1.1.1 1,3-propanediol + NAD+
-
 Oenococcus oeni ?
-
 ?
1.1.1.1 1,3-propanediol + NAD+
-
 Oenococcus oeni DSM 20252 ?
-
 ?
1.1.1.1 1-butanol + NAD+
-
 Oenococcus oeni butanal + NADH + H+
-
 r
1.1.1.1 1-butanol + NAD+
-
 Oenococcus oeni DSM 20252 butanal + NADH + H+
-
 r
1.1.1.1 1-propanol + NAD+
-
 Oenococcus oeni propanaldehyde + NADH + H+
-
 r
1.1.1.1 2-mercaptoethanol + NAD+
-
 Oenococcus oeni ?
-
 ?
1.1.1.1 acetaldehyde + NADH + H+
-
 Oenococcus oeni ethanol + NAD+
-
 r
1.1.1.1 acetaldehyde + NADH + H+
-
 Oenococcus oeni DSM 20252 ethanol + NAD+
-
 r
1.1.1.1 ethanol + NAD+
-
 Oenococcus oeni acetaldehyde + NADH + H+
-
 r
1.1.1.1 ethanol + NAD+ best substrate Oenococcus oeni acetaldehyde + NADH + H+
-
 r
1.1.1.1 additional information no activity with methanol, 1-butanol, glycerol or 2-propanol Oenococcus oeni ?
-
 ?
1.1.1.1 additional information no activity with methanol, 1-butanol, glycerol or 2-propanol Oenococcus oeni DSM 20252 ?
-
 ?
1.1.1.202 1,2-propanediol + NAD+
-
 Oenococcus oeni 2-hydroxypropanal + NADH
-
 ?
1.1.1.202 1,2-propanediol + NAD+
-
 Oenococcus oeni ATCC BAA-1163 2-hydroxypropanal + NADH
-
 ?
1.1.1.202 1,3-propanediol + NAD+ activity with 1,3-propanediol is highly dependent on the presence of Ni2+ Oenococcus oeni 3-hydroxypropanal + NADH
-
 ?
1.1.1.202 1,3-propanediol + NAD+ activity with 1,3-propanediol is highly dependent on the presence of Ni2+ Oenococcus oeni ATCC BAA-1163 3-hydroxypropanal + NADH
-
 ?
1.1.1.202 additional information enzyme additionally accepts ethanol, 1-propanol, 2-mercaptoethanol and their reduces their corresponding aldehydes. No substrates: methanol, 1-butanol, glycerol or 2-propanol Oenococcus oeni ?
-
 ?
1.1.1.202 additional information enzyme additionally accepts ethanol, 1-propanol, 2-mercaptoethanol and their reduces their corresponding aldehydes. No substrates: methanol, 1-butanol, glycerol or 2-propanol Oenococcus oeni ATCC BAA-1163 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.1 homodimer 2 * 42200-43000, recombinant His-tagged enzyme, SDS-PAGE Oenococcus oeni
1.1.1.1 More Adh3 forms a Ni2+-containing homodimer in its active form, crystal structure analysis, larger aggregates are inactive Oenococcus oeni
1.1.1.202 dimer 2 * 42200, calculated, 2 * 43000, SDS-PAGE of recombinant His-tagged protein Oenococcus oeni

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 NAD+-dependent alcohol dehydrogenase
-
 Oenococcus oeni
1.1.1.202 ADH3
-
 Oenococcus oeni
1.1.1.202 DhaT
-
 Oenococcus oeni

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.1 50 60
-
 Oenococcus oeni
1.1.1.202 50 60
-
 Oenococcus oeni

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.1 10 80 more than 40% of activity between 40°C and 70°C with all substrates. The enzyme is not capable of reducing acetaldehyde at 80°C, while remaining activity for alcohol oxidation, temperature optimum lies between 50°C to 60°C Oenococcus oeni

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.202 50
-
 60 min, inactivation Oenococcus oeni

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.1 8
-
 aldehyde reduction Oenococcus oeni
1.1.1.1 9
-
 ethanol oxidation Oenococcus oeni
1.1.1.202 8
-
 reduction of aldehydes Oenococcus oeni
1.1.1.202 9
-
 oxidation of alcohols Oenococcus oeni

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.1.202 6 7 most stable within this range Oenococcus oeni

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 NAD+ Adh3 is strictly dependent on NAD+/NADH, and shows no activity with NADP+/NADPH as cofactor Oenococcus oeni
1.1.1.1 NADH Adh3 is strictly dependent on NAD+/NADH, and shows no activity with NADP+/NADPH as cofactor Oenococcus oeni
1.1.1.202 additional information no cofactor: NADPH Oenococcus oeni
1.1.1.202 NAD+
-
 Oenococcus oeni
1.1.1.202 NADH
-
 Oenococcus oeni

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.1.1.1 Oenococcus oeni sequence calculation
-
 5.23
1.1.1.202 Oenococcus oeni calculated
-
 5.2

General Information

EC Number General Information Comment Organism
1.1.1.1 evolution the enzyme ADH3 belongs to the group III alcohol dehydrogenases Oenococcus oeni

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.1.1.1 0.01
-
 1,2-propanediol pH 8.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 0.01
-
 1,3-Propanediol pH 9.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 0.5
-
 ethanol pH 9.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 0.9
-
 acetaldehyde pH 8.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 4.9
-
 NAD+ pH 9.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.1 12.9
-
 NADH pH 8.0, 60°C, recombinant enzyme Oenococcus oeni
1.1.1.202 0.01
-
 1,2-propanediol pH 9.0, 60°C Oenococcus oeni
1.1.1.202 0.01
-
 1,3-Propanediol pH 9.0, 60°C Oenococcus oeni
1.1.1.202 4.9
-
 NAD+ pH 9.0, 60°C Oenococcus oeni
1.1.1.202 12.9
-
 NADH pH 8.0, 60°C Oenococcus oeni