Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ethanol | does not affect the adhS gene expression but induces PQQ-ADH activity | Acetobacter pasteurianus |
Protein Variants | Comment | Organism |
---|---|---|
A26V | site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
G55D | site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
L18Q | site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
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 |
T104K | site-directed mutagenesis, the mutation leads to a complete loss of ethanol oxidizing ability | Acetobacter pasteurianus |
V107A | site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
V36I | site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
V54I | site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
V70A | site-directed mutagenesis, the mutation does not affect the PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Acetobacter pasteurianus | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Acetobacter pasteurianus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ethanol + 2 ferricytochrome c | Acetobacter pasteurianus | - |
ethanal + 2 ferrocytochrome c | - |
? | |
ethanol + 2 ferricytochrome c | Acetobacter pasteurianus SKU1108 | - |
ethanal + 2 ferrocytochrome c | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acetobacter pasteurianus | - |
gene adhS encoding the smallest subunit, subunit III, genes adhA and adhB encode subunits I and II | - |
Acetobacter pasteurianus SKU1108 | - |
gene adhS encoding the smallest subunit, subunit III, genes adhA and adhB encode subunits I and II | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ethanol + 2 ferricytochrome c | - |
Acetobacter pasteurianus | ethanal + 2 ferrocytochrome c | - |
? | |
ethanol + 2 ferricytochrome c | - |
Acetobacter pasteurianus SKU1108 | ethanal + 2 ferrocytochrome c | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PQQ-ADH | - |
Acetobacter pasteurianus |
quinoprotein alcohol dehydrogenase | - |
Acetobacter pasteurianus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Acetobacter pasteurianus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Acetobacter pasteurianus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
pyrroloquinoline quinone | - |
Acetobacter pasteurianus |
Organism | Comment | Expression |
---|---|---|
Acetobacter pasteurianus | ethanol does not affect the adhS gene expression but induces PQQ-ADH activity | additional information |
General Information | Comment | Organism |
---|---|---|
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 |