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Literature summary 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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.95 0.002
-
 acryloyl-CoA apparent value, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
1.3.1.95 0.008
-
 NADH using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
1.3.1.95 1.8
-
 3-buten-2-one apparent value, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.95 soluble
-
 Anaerotignum propionicum
-
-

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.1.95 41440
-
 2 * 41440, MALDI-TOF mass spectrometry Anaerotignum propionicum
1.3.1.95 49000
-
 2 * 49000, SDS-PAGE Anaerotignum propionicum
1.3.1.95 600000
-
 native enzyme complex consisting of acryloyl-CoA reductase (two alpha subunits), (beta subunit), and (gamma subunit), gel filtration Anaerotignum propionicum

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.95 Anaerotignum propionicum
-
-
-

Purification (Commentary)

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

Source Tissue

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.1.95 0.28
-
 cell-free extract, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
1.3.1.95 0.79
-
 after purification, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.95 3-buten-2-one + NADH + H+
-
 Anaerotignum propionicum ?
-
 ?
1.3.1.95 acryloyl-CoA + NADH + H+
-
 Anaerotignum propionicum propanoyl-CoA + NAD+
-
 ir
1.3.1.95 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

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

Synonyms

EC Number Synonyms Comment Organism
1.3.1.95 acryloyl-CoA reductase
-
 Anaerotignum propionicum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.3.1.95 3.5
-
 NADH using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
1.3.1.95 4.5
-
 acryloyl-CoA in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
1.3.1.95 29
-
 3-buten-2-one in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum

Cofactor

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

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.3.1.95 17
-
 3-buten-2-one in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
1.3.1.95 440
-
 NADH using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum
1.3.1.95 2300
-
 acryloyl-CoA in 50 mM Tris/HCl, pH 7.0, at 25°C Anaerotignum propionicum