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Literature summary extracted from

  • Masud, U.; Matsushita, K.; Theeragool, G.
    Cloning and functional analysis of adhS gene encoding quinoprotein alcohol dehydrogenase subunit III from Acetobacter pasteurianus SKU1108 (2010), Int. J. Food Microbiol., 138, 39-49.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.2.8 ethanol does not affect the adhS gene expression but induces PQQ-ADH activity Acetobacter pasteurianus
1.1.5.5 ethanol ethanol does not affect the adhS gene expression but induces PQQ-ADH activity Acetobacter pasteurianus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.5.5 gene adhS, sequence determination and analysis, encoding quinoprotein alcohol dehydrogenase subunit III Acetobacter pasteurianus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.2.8 A26V site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.2.8 G55D site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.2.8 L18Q site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.2.8 additional information construction of adhS gene disruptant and mutants. The adhS gene disruptant completely loses its PQQ-ADH activity and acetate-producing ability but retains acetic acid toleration. In contrast, this disruptant grows well, even better than the wild-type, in the ethanol containing medium even though its PQQ-ADH activity and ethanol oxidizing ability is completely lost, while NAD+-dependent ADH is induced. Random mutagenesis of adhS gene reveal that complete loss of PQQ-ADH activity and ethanol oxidizing ability are observed in the mutants lacking the 140 and 73 amino acid residues at the C-terminal, whereas the lack of 22 amino acid residues at the C-terminal affects neither the PQQ-ADH activity nor ethanol oxidizing ability, overview Acetobacter pasteurianus
1.1.2.8 T104K site-directed mutagenesis, the mutation leads to a complete loss of ethanol oxidizing ability Acetobacter pasteurianus
1.1.2.8 V107A site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.2.8 V36I site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.2.8 V54I site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.2.8 V70A site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.5.5 A26V random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.5.5 G55D random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.5.5 L18Q random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.5.5 additional information random mutagenesis of adhS gene, complete loss of PQQ-ADH activity and ethanol oxidizing ability are observed in the mutants lacking of the 140 and 73 amino acid residues at the C-terminal, whereas the lack of 22 amino acid residues at the C-terminal affected neither the PQQ-ADH activity nor ethanol oxidizing ability Acetobacter pasteurianus
1.1.5.5 T104K random mutagenesis, the mutation leads to complpete loss of ethanol oxidizing ability Acetobacter pasteurianus
1.1.5.5 V107A random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.5.5 V36I random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.5.5 V54I random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus
1.1.5.5 V70A random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability Acetobacter pasteurianus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.2.8 membrane
-
 Acetobacter pasteurianus 16020
-
1.1.5.5 membrane
-
 Acetobacter pasteurianus 16020
-
1.1.5.5 additional information the nucleotide sequence of adhS indicates that the 22 kDa protein is synthesized as a preprotein with NH2-terminal 28 amino acids probably acting as a signal sequence for secretion from cytoplasm to periplasm Acetobacter pasteurianus
-
-
1.1.5.5 soluble
-
 Acetobacter pasteurianus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.2.8 Mg2+ required Acetobacter pasteurianus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.2.8 ethanol + 2 ferricytochrome c Acetobacter pasteurianus
-
 ethanal + 2 ferrocytochrome c
-
 ?
1.1.2.8 ethanol + 2 ferricytochrome c Acetobacter pasteurianus SKU1108
-
 ethanal + 2 ferrocytochrome c
-
 ?
1.1.5.5 ethanol + ubiquinone Acetobacter pasteurianus
-
 acetaldehyde + ubiquinol
-
 ?
1.1.5.5 ethanol + ubiquinone Acetobacter pasteurianus SKU1108
-
 acetaldehyde + ubiquinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.2.8 Acetobacter pasteurianus
-
 gene adhS encoding the smallest subunit, subunit III, genes adhA and adhB encode subunits I and II
-
1.1.2.8 Acetobacter pasteurianus SKU1108
-
 gene adhS encoding the smallest subunit, subunit III, genes adhA and adhB encode subunits I and II
-
1.1.5.5 Acetobacter pasteurianus
-
 genes adhA, adhB, and adhS, encding subunits I , II, and III, respectively
-
1.1.5.5 Acetobacter pasteurianus SKU1108
-
 genes adhA, adhB, and adhS, encding subunits I , II, and III, respectively
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.2.8 ethanol + 2 ferricytochrome c
-
 Acetobacter pasteurianus ethanal + 2 ferrocytochrome c
-
 ?
1.1.2.8 ethanol + 2 ferricytochrome c
-
 Acetobacter pasteurianus SKU1108 ethanal + 2 ferrocytochrome c
-
 ?
1.1.5.5 ethanol + ubiquinone
-
 Acetobacter pasteurianus acetaldehyde + ubiquinol
-
 ?
1.1.5.5 ethanol + ubiquinone
-
 Acetobacter pasteurianus SKU1108 acetaldehyde + ubiquinol
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.2.8 PQQ-ADH
-
 Acetobacter pasteurianus
1.1.2.8 quinoprotein alcohol dehydrogenase
-
 Acetobacter pasteurianus
1.1.5.5 PQQ-ADH
-
 Acetobacter pasteurianus
1.1.5.5 quinoprotein alcohol dehydrogenase
-
 Acetobacter pasteurianus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.2.8 25
-
 assay at Acetobacter pasteurianus
1.1.5.5 25
-
 assay at Acetobacter pasteurianus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.2.8 7.5
-
 assay at Acetobacter pasteurianus
1.1.5.5 6
-
 assay at Acetobacter pasteurianus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.2.8 pyrroloquinoline quinone
-
 Acetobacter pasteurianus
1.1.5.5 heme
-
 Acetobacter pasteurianus
1.1.5.5 pyrroloquinoline quinone
-
 Acetobacter pasteurianus

Expression

EC Number Organism Comment Expression
1.1.2.8 Acetobacter pasteurianus ethanol does not affect the adhS gene expression but induces PQQ-ADH activity additional information
1.1.5.5 Acetobacter pasteurianus ethanol does not affect the adhS gene expression but induces PQQ-ADH activity additional information

General Information

EC Number General Information Comment Organism
1.1.2.8 additional information Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity Acetobacter pasteurianus
1.1.5.5 additional information Thr104 might be involved in molecular coupling with subunit I in order to construct active ADH complex, whereas 22 amino acid residues at C-terminal may be not necessary for PQQ-ADH activity Acetobacter pasteurianus