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Literature summary extracted from

  • Ashraf, R.; Rashid, N.; Basheer, S.; Aziz, I.; Akhtar, M.
    Glutathione-dependent formaldehyde dehydrogenase homolog from Bacillus subtilis strain R5 is a propanol-preferring alcohol dehydrogenase (2017), Biochemistry, 82, 13-23 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.1 expressed in Escherichia coli BL21-Codon-Plus(DE3)-RIL cells Bacillus subtilis
1.2.1.46 expressed in Escherichia coli BL21-Codon-Plus(DE3)-RIL cells Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.1 EDTA significant inhibition at 10 mM Bacillus subtilis
1.2.1.46 EDTA significant inhibition at 10 mM Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.1 1.12
-
 ethanol in the presence of 0.025 mM Cu2+, at pH 9.5 and 37°C Bacillus subtilis
1.1.1.1 2.1
-
 ethanol in the presence of 0.025 mM Zn2+, at pH 9.5 and 37°C Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.1 Cu2+ the protein contains 1.3 mol of Cu2+. The highest activity, 22fold increase, is found in the protein produced in the presence of 0.025 mM Cu2+ Bacillus subtilis
1.1.1.1 Fe2+ a 20fold increase in activity is found in the protein produced in the presence of 0.025 mM Fe2+ Bacillus subtilis
1.1.1.1 additional information the presence or absence of metal ions (0.1 mM) in the reaction mixture does not affect the enzyme activity Bacillus subtilis
1.1.1.1 Zn2+ the protein contains 1.5 mol of Zn2+. An increase in activity is found in the protein produced in the presence of 0.025 mM Zn2+ Bacillus subtilis
1.2.1.46 Cu2+ the protein contains 1.3 mol of Cu2+. The highest activity, 22fold increase, is found in the protein produced in the presence of 0.025 mM Cu2+ Bacillus subtilis
1.2.1.46 Fe2+ a 20fold increase in activity is found in the protein produced in the presence of 0.025 mM Fe2+ Bacillus subtilis
1.2.1.46 additional information the presence or absence of metal ions (0.1 mM) in the reaction mixture does not affect the enzyme activity Bacillus subtilis
1.2.1.46 Zn2+ the protein contains 1.5 mol of Zn2+. An increase in activity is found in the protein produced in the presence of 0.025 mM Zn2+ Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.1 164000
-
 gel filtration Bacillus subtilis
1.2.1.46 164000
-
 gel filtration Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.1 Bacillus subtilis
-
-
-
1.1.1.1 Bacillus subtilis R5
-
-
-
1.2.1.46 Bacillus subtilis
-
-
-
1.2.1.46 Bacillus subtilis R5
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.1 nickel chelate affinity column chromatography and Superdex 200 gel filtration Bacillus subtilis
1.2.1.46 nickel chelate affinity column chromatography and Superdex 200 gel filtration Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.1 1,2-butanediol + NAD+ 5% activity compared to 1-propanol Bacillus subtilis ? + NADH + H+
-
 ?
1.1.1.1 1-butanol + NAD+ 34% activity compared to 1-propanol Bacillus subtilis butanal + NADH + H+
-
 ?
1.1.1.1 1-butanol + NAD+ 34% activity compared to 1-propanol Bacillus subtilis R5 butanal + NADH + H+
-
 ?
1.1.1.1 1-hexanol + NAD+ 7% activity compared to 1-propanol Bacillus subtilis hexanal + NADH + H+
-
 ?
1.1.1.1 1-hexanol + NAD+ 7% activity compared to 1-propanol Bacillus subtilis R5 hexanal + NADH + H+
-
 ?
1.1.1.1 ethanol + NAD+ 63% activity compared to 1-propanol Bacillus subtilis acetaldehyde + NADH + H+
-
 ?
1.1.1.1 ethanol + NAD+ 63% activity compared to 1-propanol Bacillus subtilis R5 acetaldehyde + NADH + H+
-
 ?
1.1.1.1 methanol + NAD+ 16% activity compared to 1-propanol Bacillus subtilis formaldehyde + NADH + H+
-
 ?
1.1.1.1 methanol + NAD+ 16% activity compared to 1-propanol Bacillus subtilis R5 formaldehyde + NADH + H+
-
 ?
1.1.1.1 additional information no activity with isopropanol, 2,3-butanediol, isobutanol, isoamyl alcohol, cyclohexanol, acetone, cyclohexanone, acetophenone and alpha-tetralone Bacillus subtilis ?
-
-
1.1.1.1 additional information no activity with isopropanol, 2,3-butanediol, isobutanol, isoamyl alcohol, cyclohexanol, acetone, cyclohexanone, acetophenone and alpha-tetralone Bacillus subtilis R5 ?
-
-
1.2.1.46 acetaldehyde + NAD+ + H2O 95% activity compared to propionaldehyde Bacillus subtilis acetate + NADH + H+
-
 ?
1.2.1.46 formaldehyde + NAD+ + H2O 78% activity compared to propionaldehyde Bacillus subtilis formate + NADH + H+
-
 ?
1.2.1.46 propionaldehyde + NAD+ + H2O 95% activity compared to propionaldehyde Bacillus subtilis propionate + NADH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.1.1 homotetramer 4 * 42000, SDS-PAGE Bacillus subtilis
1.1.1.1 homotetramer 4 * 41208, calculated from amino acid sequence Bacillus subtilis
1.2.1.46 homotetramer 4 * 42000, SDS-PAGE Bacillus subtilis
1.2.1.46 homotetramer 4 * 41208, calculated from amino acid sequence Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.1.1.1 glutathione-dependent formaldehyde dehydrogenase/alcohol dehydrogenase cf. EC 1.2.1.46 Bacillus subtilis
1.1.1.1 GSH-FDH/ADH
-
 Bacillus subtilis
1.2.1.46 glutathione-dependent formaldehyde dehydrogenase/alcohol dehydrogenase cf. EC 1.1.1.1 Bacillus subtilis
1.2.1.46 GSH-FDH/ADH
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.1 60
-
 temperature optimum for oxidation reaction in glycine NaOH buffer using ethanol as the substrate Bacillus subtilis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
1.1.1.1 50 65 more than 50% activity between 50 and 65°C Bacillus subtilis
1.2.1.46 50 65 more than 50% activity between 50 and 65°C Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.1 1.78
-
 ethanol in the presence of 0.025 mM Zn2+, at pH 9.5 and 37°C Bacillus subtilis
1.1.1.1 2.47
-
 ethanol in the presence of 0.025 mM Cu2+, at pH 9.5 and 37°C Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.1 9.5
-
 pH optimum for oxidation reaction in glycine NaOH buffer using ethanol as the substrate Bacillus subtilis
1.2.1.46 6.5
-
 pH optimum for reduction reaction in sodium phosphate buffer using acetaldehyde as the substrate Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.1 glutathione dependent on Bacillus subtilis
1.1.1.1 NAD+
-
 Bacillus subtilis
1.2.1.46 glutathione dependent on Bacillus subtilis
1.2.1.46 NAD+
-
 Bacillus subtilis

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 0.85
-
 ethanol in the presence of 0.025 mM Zn2+, at pH 9.5 and 37°C Bacillus subtilis
1.1.1.1 2.2
-
 ethanol in the presence of 0.025 mM Cu2+, at pH 9.5 and 37°C Bacillus subtilis