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Literature summary for 1.1.5.5 extracted from

  • Chavez-Pacheco, J.L.; Contreras-Zentella, M.; Membrillo-Hernandez, J.; Arreguin-Espinoza, R.; Mendoza-Hernandez, G.; Gomez-Manzo, S.; Escamilla, J.E.
    The quinohaemoprotein alcohol dehydrogenase from Gluconacetobacter xylinus: molecular and catalytic properties (2010), Arch. Microbiol., 192, 703-713.
    View publication on PubMed
Search for more literature for 1.1.5.5

Inhibitors

Inhibitors Comment Organism Structure
antimycin A powerful inhibitor of the purified ADH complex, most likely acting at the ubiquinone acceptor site in subunit II Komagataeibacter xylinus
Myxothiazol powerful inhibitor of the purified ADH complex, most likely acting at the ubiquinone acceptor site in subunit II Komagataeibacter xylinus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.047
-
 ubiquinone-1 using ethanol as cosubstrate, pH and temperature not specified in the publication Komagataeibacter xylinus
0.36
-
 n-butanol using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
0.43
-
 allylic alcohol using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
0.66
-
 ethanol using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
6.9
-
 acetaldehyde using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Komagataeibacter xylinus 16020
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41000
-
 1 * 68000 + 1 * 41000, SDS-PAGE Komagataeibacter xylinus
68000
-
 1 * 68000 + 1 * 41000, SDS-PAGE Komagataeibacter xylinus
119000
-
 gel filtration Komagataeibacter xylinus

Organism

Organism UniProt Comment Textmining
Komagataeibacter xylinus
-
-
-
Komagataeibacter xylinus IFO 13693
-
-
-

Purification (Commentary)

Purification (Comment) Organism
QAE-Toyopearl 550C column chromatography, DEAE-Toyopearl 650 M column chromatography, HA-Ultrogel column chromatography, and Sephacryl-S200 gel filtration Komagataeibacter xylinus

Storage Stability

Storage Stability Organism
4°C, purified enzyme in 10 mM potassium phosphate buffer containing 0.1% (v/v) Triton X-100, 30 days, no appreciable loss of activity Komagataeibacter xylinus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetaldehyde + 2,6-dichlorophenolindophenol 42% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high Komagataeibacter xylinus ?
-
 ?
acetaldehyde + ferricyanide 13% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high Komagataeibacter xylinus ?
-
 ?
allylic alcohol + 2,6-dichlorophenolindophenol 91% activity compared to n-butanol Komagataeibacter xylinus ?
-
 ?
allylic alcohol + ferricyanide 96% activity compared to n-butanol Komagataeibacter xylinus ?
-
 ?
ethanol + 2,6-dichlorophenolindophenol 88% activity compared to n-butanol Komagataeibacter xylinus acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
 ?
ethanol + 2,6-dichlorophenolindophenol 88% activity compared to n-butanol Komagataeibacter xylinus IFO 13693 acetaldehyde + reduced 2,6-dichlorophenolindophenol
-
 ?
ethanol + ferricyanide 91% activity compared to n-butanol Komagataeibacter xylinus acetaldehyde + ferrocyanide
-
 ?
ethanol + ferricyanide 91% activity compared to n-butanol Komagataeibacter xylinus IFO 13693 acetaldehyde + ferrocyanide
-
 ?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
-
 Komagataeibacter xylinus ?
-
 ?
ethanol + phenazine methosulfate + 2,6-dichlorophenolindophenol
-
 Komagataeibacter xylinus IFO 13693 ?
-
 ?
ethanol + ubiquinone-1 the ADH complex shows a high affinity for ubiquinone-1 with ethanol as cosubstrate Komagataeibacter xylinus acetaldehyde + ubiquinol-1
-
 ?
formaldehyde + 2,6-dichlorophenolindophenol 38% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high Komagataeibacter xylinus ?
-
 ?
formaldehyde + ferricyanide 34% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high Komagataeibacter xylinus ?
-
 ?
glutaraldehyde + 2,6-dichlorophenolindophenol 18% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high Komagataeibacter xylinus ?
-
 ?
glutaraldehyde + ferricyanide 8% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high Komagataeibacter xylinus ?
-
 ?
glutaraldehyde + ferricyanide 8% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high Komagataeibacter xylinus IFO 13693 ?
-
 ?
additional information purified ADH oxidizes primary alcohols (C2-C6) but not methanol Komagataeibacter xylinus ?
-
 ?
additional information purified ADH oxidizes primary alcohols (C2-C6) but not methanol Komagataeibacter xylinus IFO 13693 ?
-
 ?
n-butanol + 2,6-dichlorophenolindophenol 100% activity Komagataeibacter xylinus n-butanal + reduced 2,6-dichlorophenolindophenol
-
 ?
n-propanol + ferricyanide 98% activity compared to n-butanol Komagataeibacter xylinus n-propanal + ferrocyanide
-
 ?
n-propanol + oxidized 2,6-dichlorophenolindophenol 96% activity compared to n-butanol Komagataeibacter xylinus n-propanal + reduced 2,6-dichlorophenolindophenol
-
 ?
propionaldehyde + 2,6-dichlorophenolindophenol 33% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high Komagataeibacter xylinus ?
-
 ?
propionaldehyde + ferricyanide 24% activity compared to n-butanol. The enzyme also oxidizes aldehydes, however the affinity for alcohols is at least twice as high Komagataeibacter xylinus ?
-
 ?

Subunits

Subunits Comment Organism
heterodimer 1 * 68000 + 1 * 41000, SDS-PAGE Komagataeibacter xylinus

Synonyms

Synonyms Comment Organism
ADH
-
 Komagataeibacter xylinus
quinohemoprotein alcohol dehydrogenase
-
 Komagataeibacter xylinus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
30.8
-
 acetaldehyde using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
52.3
-
 n-butanol using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
67.5
-
 allylic alcohol using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
71
-
 ethanol using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
76.3
-
 ubiquinone-1 using ethanol as cosubstrate, pH and temperature not specified in the publication Komagataeibacter xylinus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
 activity responses to pH are sharp, showing two distinct optimal pH values (pH 5.5 and 6.5) depending on the electron acceptor used (optimum pH 5.5 with ferricyanide as electron acceptor) Komagataeibacter xylinus
6.5
-
 activity responses to pH are sharp, showing two distinct optimal pH values (pH 5.5 and 6.5) depending on the electron acceptor used (optimum pH 6.5 when phenazine methosulfate plus 2,6-dichlorophenolindophenol are used as electron acceptors) Komagataeibacter xylinus

Cofactor

Cofactor Comment Organism Structure
cytochrome c the enzyme contains 4 cytochromes c per enzyme Komagataeibacter xylinus
heme the quinohaemoprotein alcohol dehydrogenase contains heme C in both subunits, the ADH complex of contains 18 nmol of heme C per mg of protein (ratio of 3.6 mol of heme C per mol of enzyme) Komagataeibacter xylinus
pyrroloquinoline quinone the ADH complex contains one mol of pyrroloquinoline quinone Komagataeibacter xylinus
pyrroloquinoline quinone one pyrroloquinoline quinone is associated with one molecule of the purified ADH complex Komagataeibacter xylinus

pI Value

Organism Comment pI Value Maximum pI Value
Komagataeibacter xylinus isoelectric focusing
-
 5.7

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
108
-
 ethanol using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
145
-
 n-butanol using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
157
-
 allylic alcohol using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus
162
-
 ubiquinone-1 using ethanol as cosubstrate, pH and temperature not specified in the publication Komagataeibacter xylinus
446
-
 acetaldehyde using 2,6-dichlorophenolindophenol as cosubstrate, pH 6.5, temperature not specified in the publication Komagataeibacter xylinus