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 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
1.1.5.5 | gene adhS, sequence determination and analysis, encoding quinoprotein alcohol dehydrogenase subunit III | Acetobacter pasteurianus |
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 |
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 | - |
- |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.1.2.8 | Mg2+ | required | Acetobacter pasteurianus |
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 | - |
? |
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 | - |
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 | - |
? |
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 |
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 |
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 |
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 |
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 |
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 |