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Literature summary extracted from

  • Ramanavicius, A.; Habermuller, K.; Csoeregi, E.; Laurinavicius, V.; Schuhmann, W.
    Polypyrrole-entrapped quinohemoprotein alcohol dehydrogenase. Evidence for direct electron transfer via conducting-polymer chains (1999), Anal. Chem., 71, 3581-3586.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.5.5 analysis construction and evaluation of an ethanol sensor based on the enzyme using direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode, overview Gluconobacter sp.

General Stability

EC Number General Stability Organism
1.1.5.5 0.1% Triton X-100 stabilizes the enzyme Gluconobacter sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.5.5 Ca2+ required, stabilizes the pyrroloquinoline quinone in the active site Gluconobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.5 Gluconobacter sp.
-
-
-
1.1.5.5 Gluconobacter sp. DSM 3504 / ATCC 15163
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.5.5 native enzyme by anion exchange and hydrophobic interaction chromatography, and dialysis against high-viscosity carboxymethyl cellulose as the absorber Gluconobacter sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.5.5 32.2
-
 purified native enzyme Gluconobacter sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.5 ethanol + acceptor direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode take place via the conducting-polymer network, mechanism modelling, overview Gluconobacter sp. acetaldehyde + reduced acceptor
-
 ?
1.1.5.5 ethanol + acceptor direct electron-transfer processes between the polypyrrole entrapped quinohemoprotein alcohol dehydrogenase and a platinum electrode take place via the conducting-polymer network, mechanism modelling, overview Gluconobacter sp. DSM 3504 / ATCC 15163 acetaldehyde + reduced acceptor
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.5.5 dimer
-
 Gluconobacter sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.5.5 QH-ADH
-
 Gluconobacter sp.
1.1.5.5 quinohemoprotein alcohol dehydrogenase
-
 Gluconobacter sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.5.5 20
-
 assay at Gluconobacter sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.5.5 6
-
 assay at Gluconobacter sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.5 heme eight molecules per enzyme molecule Gluconobacter sp.
1.1.5.5 pyrroloquinoline quinone PQQ, two molecules per enzyme molecule Gluconobacter sp.