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Literature summary for 1.1.5.5 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
Search for more literature for 1.1.5.5

Application

Application Comment Organism
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

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

Metals/Ions

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
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]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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
-
 ?
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

Subunits Comment Organism
dimer
-
 Gluconobacter sp.

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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