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Information on EC 1.3.1.95 - acrylyl-CoA reductase (NADH)
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1.3.1.95 acrylyl-CoA reductase (NADH)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).
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Word Map
- 1.3.1.95
-
dehydratase
- acrylate
-
3-hydroxypropionate/4-hydroxybutyrate
- sedula
- 3-hydroxypropionate
- 3-hydroxypropionyl-coa
- metallosphaera
-
ferredoxin
- propionyl-coa
- fmn
- aurantiacus
-
dmdas
- dimethylsulfoniopropionate
- ketone
- propionicum
-
vinyl
- succinyl-coa
-
lyases
- demethylase
-
semialdehyde
-
acuis
- roseobacters
- chloroflexus
- sulfide
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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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Acr
acryloyl-CoA reductase
acryloyl-CoA reductase (NADPH)
acryloyl-coenzyme A reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
propanoyl-CoA + NAD+ = acryloyl-CoA + NADH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(E)-2-butenoate + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
(E)-2-butenoyl-CoA + methyl viologen
?
-
second best substrate, 45% activity compared to acryloyl-CoA
-
-
?
1-penten-3-one + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
2-cyclohexen-1-one + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
2-methylacrolein + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
4-phenyl-3-buten-2-one + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
acrylic acid + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
butyryl-CoA + 2,6-dichlorophenolindophenol
?
-
about 1% of the reduction rate of (E)-2-butenoyl-CoA and methyl viologen
-
-
?
diethyl ketone + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
ethyl acrylate + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
methyl propenyl ketone + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
methyl vinyl ketone + methyl viologen
?
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
acryloyl-CoA + NADH + H+
propanoyl-CoA + NAD+
-
-
-
?
acryloyl-CoA + NADPH + H+
propanoyl-CoA + NADP+
-
100% specificity
-
-
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)
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
less than 1% specificity for crotonyl-CoA
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ethyl acrylate
-
strong inhibitor of the reduction of ethyl vinyl ketone
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.8
3-buten-2-one
-
apparent value, in 50 mM Tris/HCl, pH 7.0, at 25°C
35
N-acetyl-S-acryloylcysteamine
-
in 0.1 M phosphate buffer pH 6.4, at 22°C
0.008
NADH
-
using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C
0.002
acryloyl-CoA
-
apparent value, in 50 mM Tris/HCl, pH 7.0, at 25°C
0.01
acryloyl-CoA
-
apparent value, Km less than 0.01 mM, recombinant enzyme, at pH 7.5 and 22°C
0.01
acryloyl-CoA
-
apparent value, Km less than 0.01 mM, recombinant enzyme, at pH 7.5 and 22°C
0.036
acryloyl-CoA
-
apparent value, recombinant enzyme, at pH 7.5 and 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.5
NADH
-
using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C
13
acryloyl-CoA
-
apparent value, recombinant enzyme, at pH 7.5 and 22°C
13
acryloyl-CoA
-
apparent value, recombinant enzyme, at pH 7.5 and 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
440
NADH
-
using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.02
recombinant enzyme, in 0.1 M Tris pH 7.0, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.9 - 8.3
-
the activity of the acryloyl-CoA reductase decreases to about 30% at pH 3.9 or pH 8.3, respectively
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (2244 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40000
600000
-
native enzyme complex consisting of acryloyl-CoA reductase (two alpha subunits), (beta subunit), and (gamma subunit), gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
696519
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phenyl Sepharose column chromatography, Q-Sepharose column chromatography, and Uno Q6-Sepharose HP column chromatography
-
DEAE-Sepharose CL-6B column chromatography, phenyl-Sepharose CL-4B column chromatography, CM-Sephadex A-25 gel filtration, and Sephacryl S-200 gel filtration
-
heat precipitation and Ni2+-chelating Sepharose column chromatography
-
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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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta-gami 2(DE3)pLysS (VK-23) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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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