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Literature summary for 1.1.5.5 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 ethanol does not affect the adhS gene expression but induces PQQ-ADH activity Acetobacter pasteurianus

Cloned(Commentary)

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

Protein Variants

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

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/ Products (Substrates)

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

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ethanol + ubiquinone
-
Acetobacter pasteurianus acetaldehyde + ubiquinol
-
?
ethanol + ubiquinone
-
Acetobacter pasteurianus SKU1108 acetaldehyde + ubiquinol
-
?

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
6
-
assay at Acetobacter pasteurianus

Cofactor

Cofactor Comment Organism Structure
heme
-
Acetobacter pasteurianus
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