Activating Compound | Comment | Organism | Structure |
---|---|---|---|
ethanol | ethanol does not affect the adhS gene expression but induces PQQ-ADH activity | Acetobacter pasteurianus |
Cloned (Comment) | Organism |
---|---|
gene adhS, sequence determination and analysis, encoding quinoprotein alcohol dehydrogenase subunit III | Acetobacter pasteurianus |
Protein Variants | Comment | Organism |
---|---|---|
A26V | random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
G55D | random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
L18Q | random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
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 |
T104K | random mutagenesis, the mutation leads to complpete loss of ethanol oxidizing ability | Acetobacter pasteurianus |
V107A | random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
V36I | random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
V54I | random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
V70A | random mutagenesis, the mutation has no effect on PQQ-ADH activity and ethanol oxidizing ability | Acetobacter pasteurianus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Acetobacter pasteurianus | 16020 | - |
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 | - |
- |
soluble | - |
Acetobacter pasteurianus | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ethanol + ubiquinone | Acetobacter pasteurianus | - |
acetaldehyde + ubiquinol | - |
? | |
ethanol + ubiquinone | Acetobacter pasteurianus SKU1108 | - |
acetaldehyde + ubiquinol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Acetobacter pasteurianus | - |
genes adhA, adhB, and adhS, encding subunits I , II, and III, respectively | - |
Acetobacter pasteurianus SKU1108 | - |
genes adhA, adhB, and adhS, encding subunits I , II, and III, respectively | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ethanol + ubiquinone | - |
Acetobacter pasteurianus | acetaldehyde + ubiquinol | - |
? | |
ethanol + ubiquinone | - |
Acetobacter pasteurianus SKU1108 | acetaldehyde + ubiquinol | - |
? |
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 |
---|---|---|---|
6 | - |
assay at | Acetobacter pasteurianus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Acetobacter pasteurianus | |
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 |