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Information on EC 1.3.1.95 - acrylyl-CoA reductase (NADH) for references in articles please use BRENDA:EC1.3.1.95
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IUBMB Comments Contains FAD. The reaction is catalysed in the opposite direction to that shown. The enzyme from the bacterium Clostridium propionicum is a complex that includes an electron-transfer flavoprotein (ETF). The ETF is reduced by NADH and transfers the electrons to the active site. Catalyses a step in a pathway for L-alanine fermentation to propanoate . cf. EC 1.3.1.84, acrylyl-CoA reductase (NADPH).
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
Acr, acryloyl-CoA reductase, acryloyl-CoA reductase (NADPH), acryloyl-coenzyme A reductase,
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acryloyl-CoA reductase (NADPH)
acryloyl-coenzyme A reductase
Acr
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acryloyl-CoA reductase
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acryloyl-CoA reductase
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acryloyl-CoA reductase
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acryloyl-CoA reductase
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acryloyl-CoA reductase
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acryloyl-CoA reductase (NADPH)
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acryloyl-CoA reductase (NADPH)
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acryloyl-coenzyme A reductase
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acryloyl-coenzyme A reductase
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propanoyl-CoA + NAD+ = acryloyl-CoA + NADH + H+
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propanoyl-CoA:NAD+ oxidoreductase
Contains FAD. The reaction is catalysed in the opposite direction to that shown. The enzyme from the bacterium Clostridium propionicum is a complex that includes an electron-transfer flavoprotein (ETF). The ETF is reduced by NADH and transfers the electrons to the active site. Catalyses a step in a pathway for L-alanine fermentation to propanoate [1]. cf. EC 1.3.1.84, acrylyl-CoA reductase (NADPH).
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(E)-2-butenoate + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
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-
?
(E)-2-butenoyl-CoA + methyl viologen
?
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second best substrate, 45% activity compared to acryloyl-CoA
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-
?
1-penten-3-one + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
-
-
?
2-cyclohexen-1-one + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
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-
?
2-methylacrolein + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
-
-
?
3-buten-2-one + NADH + H+
?
-
-
-
-
?
4-phenyl-3-buten-2-one + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
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-
?
acrolein + methyl viologen
?
-
-
-
-
?
acrylic acid + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
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-
?
acryloyl-CoA + methyl viologen
?
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best substrate
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-
?
acryloyl-CoA + NADH + H+
propanoyl-CoA + NAD+
acryloyl-CoA + NADPH + H+
propanoyl-CoA + NADP+
butyryl-CoA + 2,6-dichlorophenolindophenol
?
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about 1% of the reduction rate of (E)-2-butenoyl-CoA and methyl viologen
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-
?
diethyl ketone + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
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-
?
ethyl acrylate + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
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-
?
ethyl vinyl ketone + methyl viologen
?
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-
?
methyl propenyl ketone + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
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-
?
methyl vinyl ketone + methyl viologen
?
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less than 2% activity of that with ethyl vinyl ketone
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-
?
N-acetyl-S-acryloylcysteamine + methyl viologen
?
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-
-
-
?
additional information
?
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acryloyl-CoA + NADH + H+
propanoyl-CoA + NAD+
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ir
acryloyl-CoA + NADH + H+
propanoyl-CoA + NAD+
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-
-
?
acryloyl-CoA + NADH + H+
propanoyl-CoA + NAD+
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-
-
?
acryloyl-CoA + NADPH + H+
propanoyl-CoA + NADP+
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-
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ir
acryloyl-CoA + NADPH + H+
propanoyl-CoA + NADP+
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100% specificity
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ir
additional information
?
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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)
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additional information
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the enzyme shows no activity with different concentrations of NAD(P)H in 0.1 M phosphate buffer pH 7.0 and ethyl vinyl ketone as substrate
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additional information
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less than 1% specificity for crotonyl-CoA
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additional information
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he activity of the acryloyl-CoA reductase is not altered significantly by any of the following substances added in concentrations of 0.075 to 0.15 mM: FMN, FAD, AMP, ADP, ATP, NAD+, NADH, acetyl phosphate and co-enzyme A
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FAD
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contains 90% FAD (3-4 molecules)
FMN
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contains 1.5 mol FMN
NADPH
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-
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Zn2+
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contains 0.8 mol of Zn2+ per mol of enzyme monomer
Zn2+
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contains 0.8 mol of Zn2+ per mol of enzyme monomer
additional information
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does not contain iron
additional information
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does not contain iron
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ethyl acrylate
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strong inhibitor of the reduction of ethyl vinyl ketone
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0.008
(E)-2-butenoyl-CoA
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in 0.1 M phosphate buffer pH 6.4, at 22°C
1.8
3-buten-2-one
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apparent value, in 50 mM Tris/HCl, pH 7.0, at 25°C
5.6
acrolein
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in 0.1 M phosphate buffer pH 6.4, at 22°C
0.00083 - 0.036
acryloyl-CoA
0.77
ethyl vinyl ketone
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in 0.1 M phosphate buffer pH 6.4, at 22°C
35
N-acetyl-S-acryloylcysteamine
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in 0.1 M phosphate buffer pH 6.4, at 22°C
0.008
NADH
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using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C
0.036
NADPH
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apparent value, recombinant enzyme, at pH 7.5 and 22°C
0.00083
acryloyl-CoA
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in 0.1 M phosphate buffer pH 6.4, at 22°C
0.002
acryloyl-CoA
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apparent value, in 50 mM Tris/HCl, pH 7.0, at 25°C
0.01
acryloyl-CoA
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apparent value, Km less than 0.01 mM, recombinant enzyme, at pH 7.5 and 22°C
0.01
acryloyl-CoA
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apparent value, Km less than 0.01 mM, recombinant enzyme, at pH 7.5 and 22°C
0.036
acryloyl-CoA
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apparent value, recombinant enzyme, at pH 7.5 and 22°C
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29
3-buten-2-one
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in 50 mM Tris/HCl, pH 7.0, at 25°C
3.5
NADH
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using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C
4.5
acryloyl-CoA
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in 50 mM Tris/HCl, pH 7.0, at 25°C
13
acryloyl-CoA
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apparent value, recombinant enzyme, at pH 7.5 and 22°C
13
acryloyl-CoA
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apparent value, recombinant enzyme, at pH 7.5 and 22°C
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17
3-buten-2-one
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in 50 mM Tris/HCl, pH 7.0, at 25°C
2300
acryloyl-CoA
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in 50 mM Tris/HCl, pH 7.0, at 25°C
440
NADH
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using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C
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0.014
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cell extract, at pH 7.5 and 22°C
0.02
recombinant enzyme, in 0.1 M Tris pH 7.0, temperature not specified in the publication
0.28
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cell-free extract, in 50 mM Tris/HCl, pH 7.0, at 25°C
0.79
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after purification, in 50 mM Tris/HCl, pH 7.0, at 25°C
2.9
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after 210fold purification, at pH 7.5 and 22°C
4.6
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cell extract, at pH 7.5 and 22°C
18.7
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after 4.1fold purification, at pH 7.5 and 22°C
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5.9
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two optima at pH 5.9 and 6.4
6.4
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two optima at pH 5.9 and 6.4
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3.9 - 8.3
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the activity of the acryloyl-CoA reductase decreases to about 30% at pH 3.9 or pH 8.3, respectively
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7.5
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isoelectric focusing
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alpha subunit
UniProt
brenda
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brenda
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brenda
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brenda
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brenda
alpha subunit
UniProt
brenda
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brenda
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brenda
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14200
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2 * 14200, SDS-PAGE
36000
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calculated from amino acid sequence
41440
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2 * 41440, MALDI-TOF mass spectrometry
49000
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2 * 49000, SDS-PAGE
600000
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native enzyme complex consisting of acryloyl-CoA reductase (two alpha subunits), (beta subunit), and (gamma subunit), gel filtration
40000
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1 * 40000, SDS-PAGE
40000
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1 * 40000, SDS-PAGE
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homodimer
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2 * 41440, MALDI-TOF mass spectrometry; 2 * 49000, SDS-PAGE
homodimer
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2 * 14200, SDS-PAGE
monomer
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1 * 40000, SDS-PAGE
monomer
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1 * 40000, SDS-PAGE
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the enzyme exhibits up to 11% and up to 16% residual activity after 19 days of exposure to air at pH 8.0 and 10°C and 30°C, respectively
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696519
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-18°C, 30% (w/v) ethylene glycol in 15 mM phosphate buffer pH 8.0, 1 year, 20% loss of activity
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ammonium sulfate precipitation, phenyl Sepharose column chromatography, Q-Sepharose column chromatography, and Uno Q6-Sepharose HP column chromatography
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DEAE-Sepharose CL-6B column chromatography, phenyl-Sepharose CL-4B column chromatography, CM-Sephadex A-25 gel filtration, and Sephacryl S-200 gel filtration
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heat precipitation and Ni2+-chelating Sepharose column chromatography
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heat precipitation, Q Sepharose column chromatography, carboxymethylcellulose column chromatography, ammonium sulfate precipitation, phenyl-Sepharose column chromatography, and Resource-S gel filtration
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expressed in Escherichia coli Rosetta 2 (DE3) cells
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expressed in Escherichia coli Rosetta-gami 2(DE3)pLysS (VK-23) cells
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Sedlmeier, H.; Simon, H.
Purification and some properties of an acryloyl-CoA reductase of Clostridium kluyveri
Biol. Chem. Hoppe-Seyler
366
953-961
1985
Clostridium kluyveri
brenda
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
Eur. J. Biochem.
270
902-910
2003
Anaerotignum propionicum
brenda
Teufel, R.; Kung, J.; Kockelkorn, D.; Alber, B.; Fuchs, G.
3-Hydroxypropionyl-coenzyme A dehydratase and acryloyl-coenzyme A reductase, enzymes of the autotrophic 3-hydroxypropionate/4-hydroxybutyrate cycle in the Sulfolobales
J. Bacteriol.
191
4572-4581
2009
Metallosphaera sedula, Sulfurisphaera tokodaii
brenda
Kandasamy, V.; Vaidyanathan, H.; Djurdjevic, I.; Jayamani, E.; Ramachandran, K.; Buckel, W.; Jayaraman, G.; Ramalingam, S.
Engineering Escherichia coli with acrylate pathway genes for propionic acid synthesis and its impact on mixed-acid fermentation
Appl. Microbiol. Biotechnol.
97
1191-1200
2013
Anaerotignum propionicum (G3KIM6), Anaerotignum propionicum DSM 1682 (G3KIM6)
brenda
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