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Literature summary for 1.2.5.2 extracted from

  • Vangnai, A.S.; Arp, D.J.
    An inducible 1-butanol dehydrogenase, a quinohaemoprotein, is involved in the oxidation of butane by Pseudomonas butanovora (2001), Microbiology, 147, 745-756.
    View publication on PubMed
Search for more literature for 1.2.5.2

Activating Compound

Activating Compound Comment Organism Structure
additional information the enzyme is induced by growth on 1-butanol and 2-butanol Thauera butanivorans
NH4+ 3fold activation at 4 mM Thauera butanivorans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.007
-
 1-butanol
-
 Thauera butanivorans

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Thauera butanivorans
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ highly activating Thauera butanivorans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
66000
-
 1 * 66000, SDS-PAGE Thauera butanivorans
69000
-
 gel filtration Thauera butanivorans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1-butanol + acceptor Thauera butanivorans the NAD+-independent inducible 1-butanol dehydrogenase, a quinohemoprotein, is responsible for 1-butanol oxidation in the butane metabolism pathway butanal + reduced acceptor
-
 ?
1-butanol + acceptor Thauera butanivorans ATCC 43655 the NAD+-independent inducible 1-butanol dehydrogenase, a quinohemoprotein, is responsible for 1-butanol oxidation in the butane metabolism pathway butanal + reduced acceptor
-
 ?

Organism

Organism UniProt Comment Textmining
Thauera butanivorans
-
 strain ATCC 43655
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme 37fold to near homogeneity by ammonium sulfate fractionation and anion exchange chromatography Thauera butanivorans

Renatured (Commentary)

Renatured (Comment) Organism
Ca2+ ions facilitate the reconstitution of inactive apoenzyme Thauera butanivorans

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:1-butanol-grown cell
-
 Thauera butanivorans
-
culture condition:2-butanol-grown cell
-
 Thauera butanivorans
-
culture condition:butane-grown cell
-
 Thauera butanivorans
-
culture condition:D-lactate-grown cell
-
 Thauera butanivorans
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0019
-
 lactate-grown cell extract Thauera butanivorans
0.0044
-
 2-butanol-grown cell extract Thauera butanivorans
0.0106
-
 1-butanol-grown cell extract Thauera butanivorans
4.8
-
 purified enzyme Thauera butanivorans

Storage Stability

Storage Stability Organism
-80°C, purified enzyme, 25 mM Tris-HCl, pH 8.0, stable for more than 6 months Thauera butanivorans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-butanol + acceptor the NAD+-independent inducible 1-butanol dehydrogenase, a quinohemoprotein, is responsible for 1-butanol oxidation in the butane metabolism pathway Thauera butanivorans butanal + reduced acceptor
-
 ?
1-butanol + acceptor the NAD+-independent inducible 1-butanol dehydrogenase, a quinohemoprotein, is responsible for 1-butanol oxidation in the butane metabolism pathway Thauera butanivorans ATCC 43655 butanal + reduced acceptor
-
 ?
acetaldehyde + 2,6-dichlorophenolindophenol
-
 Thauera butanivorans acetate + reduced 2,6-dichlorophenolindophenol
-
 ?
acetaldehyde + 2,6-dichlorophenolindophenol
-
 Thauera butanivorans ATCC 43655 acetate + reduced 2,6-dichlorophenolindophenol
-
 ?
butyraldehyde + 2,6-dichlorophenolindophenol
-
 Thauera butanivorans butanoate + reduced 2,6-dichlorophenolindophenol
-
 ?
butyraldehyde + 2,6-dichlorophenolindophenol
-
 Thauera butanivorans ATCC 43655 butanoate + reduced 2,6-dichlorophenolindophenol
-
 ?
additional information the enzyme has a broad substrate range, including primary alcohols, secondary alcohols, aldehydes, C4 diols and aromatic alcohols, BDH exhibits a marked preference towards 2-pentanol and the activity gradually decreases with longer-chain secondary alcohols, BDH exhibits ferricyanide-dependent ADH activity Thauera butanivorans ?
-
 ?
additional information the enzyme has a broad substrate range, including primary alcohols, secondary alcohols, aldehydes, C4 diols and aromatic alcohols, BDH exhibits a marked preference towards 2-pentanol and the activity gradually decreases with longer-chain secondary alcohols, BDH exhibits ferricyanide-dependent ADH activity Thauera butanivorans ATCC 43655 ?
-
 ?
propionaldehyde + 2,6-dichlorophenolindophenol
-
 Thauera butanivorans propanoate + reduced 2,6-dichlorophenolindophenol
-
 ?
propionaldehyde + 2,6-dichlorophenolindophenol
-
 Thauera butanivorans ATCC 43655 propanoate + reduced 2,6-dichlorophenolindophenol
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 66000, SDS-PAGE Thauera butanivorans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
 phenazine methosulfate/2,6-dichlorophenolindophenol-dependent activity Thauera butanivorans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25 32 purified enzyme, maximally stable within this range Thauera butanivorans
60
-
 30 min, purified enzyme, loss of 77% activity Thauera butanivorans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 phenazine methosulfate/2,6-dichlorophenolindophenol-dependent activity Thauera butanivorans

Cofactor

Cofactor Comment Organism Structure
heme c 0.25 mol of heme per mol of enzyme Thauera butanivorans
pyrroloquinoline quinone PQQ, 1.0 mol of PQQ per mol of enzyme Thauera butanivorans