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

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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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-
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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).
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha subunit
UniProt
Manually annotated by BRENDA team
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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
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less than 2% activity of that with ethyl vinyl ketone
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-
?
2-methylacrolein + methyl viologen
?
show the reaction diagram
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less than 2% activity of that with ethyl vinyl ketone
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-
?
3-buten-2-one + NADH + H+
?
show the reaction diagram
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-
-
-
?
4-phenyl-3-buten-2-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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-
?
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
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ethyl acrylate
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strong inhibitor of the reduction of ethyl vinyl ketone
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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 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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
29
3-buten-2-one
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in 50 mM Tris/HCl, pH 7.0, at 25°C
4.5 - 13
acryloyl-CoA
3.5
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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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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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
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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
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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isoelectric focusing
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
14200
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2 * 14200, SDS-PAGE
28400
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gel filtration
36000
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calculated from amino acid sequence
41440
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2 * 41440, MALDI-TOF mass spectrometry
43000
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gel filtration
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
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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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
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Show AA Sequence (420 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.3.1.95)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)