Information on EC 1.3.1.95 - acrylyl-CoA reductase (NADH)

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.3.1.95
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RECOMMENDED NAME
GeneOntology No.
acrylyl-CoA reductase (NADH)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
propanoyl-CoA + NAD+ = acryloyl-CoA + NADH + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
pyruvate fermentation to propanoate II (acrylate pathway)
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alanine metabolism
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Propanoate metabolism
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Metabolic pathways
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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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha subunit
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E)-2-butenoate + methyl viologen
?
show the reaction diagram
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less than 2% activity of that with ethyl vinyl ketone
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-
?
(E)-2-butenoyl-CoA + methyl viologen
?
show the reaction diagram
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second best substrate, 45% activity compared to acryloyl-CoA
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-
?
1-penten-3-one + methyl viologen
?
show the reaction diagram
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less than 2% activity of that with ethyl vinyl ketone
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-
?
2-cyclohexen-1-one + methyl viologen
?
show the reaction diagram
-
less than 2% activity of that with ethyl vinyl ketone
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-
?
2-methylacrolein + methyl viologen
?
show the reaction diagram
-
less than 2% activity of that with ethyl vinyl ketone
-
-
?
3-buten-2-one + NADH + H+
?
show the reaction diagram
-
-
-
-
?
4-phenyl-3-buten-2-one + methyl viologen
?
show the reaction diagram
-
less than 2% activity of that with ethyl vinyl ketone
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-
?
acrolein + methyl viologen
?
show the reaction diagram
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-
-
-
?
acrylic acid + methyl viologen
?
show the reaction diagram
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less than 2% activity of that with ethyl vinyl ketone
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-
?
acryloyl-CoA + methyl viologen
?
show the reaction diagram
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best substrate
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-
?
acryloyl-CoA + NADH + H+
propanoyl-CoA + NAD+
show the reaction diagram
acryloyl-CoA + NADPH + H+
propanoyl-CoA + NADP+
show the reaction diagram
butyryl-CoA + 2,6-dichlorophenolindophenol
?
show the reaction diagram
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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
?
show the reaction diagram
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less than 2% activity of that with ethyl vinyl ketone
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?
ethyl acrylate + methyl viologen
?
show the reaction diagram
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less than 2% activity of that with ethyl vinyl ketone
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-
?
ethyl vinyl ketone + methyl viologen
?
show the reaction diagram
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-
-
-
?
methyl propenyl ketone + methyl viologen
?
show the reaction diagram
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less than 2% activity of that with ethyl vinyl ketone
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-
?
methyl vinyl ketone + methyl viologen
?
show the reaction diagram
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less than 2% activity of that with ethyl vinyl ketone
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?
N-acetyl-S-acryloylcysteamine + methyl viologen
?
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethyl acrylate
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strong inhibitor of the reduction of ethyl vinyl ketone
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
(E)-2-butenoyl-CoA
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in 0.1 M phosphate buffer pH 6.4, at 22C
1.8
3-buten-2-one
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apparent value, in 50 mM Tris/HCl, pH 7.0, at 25C
5.6
acrolein
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in 0.1 M phosphate buffer pH 6.4, at 22C
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 22C
35
N-acetyl-S-acryloylcysteamine
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in 0.1 M phosphate buffer pH 6.4, at 22C
0.008
NADH
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using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25C
0.036
NADPH
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apparent value, recombinant enzyme, at pH 7.5 and 22C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29
3-buten-2-one
Clostridium propionicum
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in 50 mM Tris/HCl, pH 7.0, at 25C
4.5 - 13
acryloyl-CoA
3.5
NADH
Clostridium propionicum
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using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17
3-buten-2-one
Clostridium propionicum
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in 50 mM Tris/HCl, pH 7.0, at 25C
2904
2300
acryloyl-CoA
Clostridium propionicum
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in 50 mM Tris/HCl, pH 7.0, at 25C
2191
440
NADH
Clostridium propionicum
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using acryloyl-CoA as cosubstrate, in 50 mM Tris/HCl, pH 7.0, at 25C
8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.014
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cell extract, at pH 7.5 and 22C
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 25C
0.79
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after purification, in 50 mM Tris/HCl, pH 7.0, at 25C
2.9
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after 210fold purification, at pH 7.5 and 22C
4.6
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cell extract, at pH 7.5 and 22C
18.7
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after 4.1fold purification, at pH 7.5 and 22C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28400
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gel filtration
36000
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calculated from amino acid sequence
43000
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gel filtration
600000
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native enzyme complex consisting of acryloyl-CoA reductase (two alpha subunits), (beta subunit), and (gamma subunit), gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
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 10C and 30C, respectively
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696519
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 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
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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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta 2 (DE3) cells
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expressed in Escherichia coli Rosetta-gami 2(DE3)pLysS (VK-23) cells
Show AA Sequence (140 entries)
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