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Literature summary for 1.3.1.95 extracted from

  • Hetzel, M.; Brock, M.; Selmer, T.; Pierik, A.; Golding, B.; Buckel, W.
    Acryloyl-CoA reductase from Clostridium propionicum: An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein (2003), Eur. J. Biochem., 270, 902-910.
    View publication on PubMed
Search for more literature for 1.3.1.95

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 acryloyl-CoA apparent value, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
0.008
-
 NADH using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
1.8
-
 3-buten-2-one apparent value, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
 Anaerotignum propionicum
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information does not contain iron Anaerotignum propionicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
41440
-
 2 * 41440, MALDI-TOF mass spectrometry Anaerotignum propionicum
49000
-
 2 * 49000, SDS-PAGE Anaerotignum propionicum
600000
-
 native enzyme complex consisting of acryloyl-CoA reductase (two alpha subunits), (beta subunit), and (gamma subunit), gel filtration Anaerotignum propionicum

Organism

Organism UniProt Comment Textmining
Anaerotignum propionicum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, phenyl Sepharose column chromatography, Q-Sepharose column chromatography, and Uno Q6-Sepharose HP column chromatography Anaerotignum propionicum

Source Tissue

Source Tissue Comment Organism Textmining
culture condition:L-alanine-grown cell
-
 Anaerotignum propionicum
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.28
-
 cell-free extract, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
0.79
-
 after purification, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-buten-2-one + NADH + H+
-
 Anaerotignum propionicum ?
-
 ?
acryloyl-CoA + NADH + H+
-
 Anaerotignum propionicum propanoyl-CoA + NAD+
-
 ir
additional information the enzyme complex also exhibits acyl-CoA dehydrogenase activity with propionyl-CoA or butyryl-CoA as electron donor and ferricenium hexafluorophosphate as acceptor. The enzyme also catalyses the oxidation of NADH by iodonitrosotetrazolium chloride (diaphorase activity) or by air, which leads to the formation of H2O2 (NADH oxidase activity) Anaerotignum propionicum ?
-
 ?

Subunits

Subunits Comment Organism
homodimer 2 * 49000, SDS-PAGE Anaerotignum propionicum
homodimer 2 * 41440, MALDI-TOF mass spectrometry Anaerotignum propionicum

Synonyms

Synonyms Comment Organism
acryloyl-CoA reductase
-
 Anaerotignum propionicum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5
-
 NADH using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
4.5
-
 acryloyl-CoA in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
29
-
 3-buten-2-one in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum

Cofactor

Cofactor Comment Organism Structure
FAD contains 90% FAD (3-4 molecules) Anaerotignum propionicum
FMN contains 10% FMN Anaerotignum propionicum
NADH
-
 Anaerotignum propionicum

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
17
-
 3-buten-2-one in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
440
-
 NADH using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
2300
-
 acryloyl-CoA in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum