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Literature summary for 1.1.2.8 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

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

Protein Variants

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

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Acetobacter pasteurianus 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Acetobacter pasteurianus

Natural Substrates/ Products (Substrates)

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

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 and Products (Substrate)

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

Synonyms Comment Organism
PQQ-ADH
-
Acetobacter pasteurianus
quinoprotein alcohol dehydrogenase
-
Acetobacter pasteurianus

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
25
-
assay at Acetobacter pasteurianus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Acetobacter pasteurianus

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone
-
Acetobacter pasteurianus

Expression

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

General 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