Information on EC 1.3.1.84 - acrylyl-CoA reductase (NADPH)

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

EC NUMBER
COMMENTARY hide
1.3.1.84
-
RECOMMENDED NAME
GeneOntology No.
acrylyl-CoA reductase (NADPH)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
propanoyl-CoA + NADP+ = acryloyl-CoA + NADPH + H+
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
3-hydroxypropanoate cycle
-
-
3-hydroxypropanoate/4-hydroxybutanate cycle
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glyoxylate assimilation
-
-
CO2 fixation in Crenarchaeota
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Carbon fixation pathways in prokaryotes
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
propanoyl-CoA:NADP+ oxidoreductase
Catalyses a step in the 3-hydroxypropanoate/4-hydroxybutanoate cycle, an autotrophic CO2 fixation pathway found in some thermoacidophilic archaea [1]. The enzyme from Sulfolobus tokodaii does not act on either NADH or crotonyl-CoA [2]. Different from EC 1.3.1.8, which acts only on enoyl-CoA derivatives of carbon chain length 4 to 16. Contains Zn2+.
CAS REGISTRY NUMBER
COMMENTARY hide
150386-12-2
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acryloyl-CoA + NADPH + H+
propanoyl-CoA + NADP+
show the reaction diagram
-
-
-
?
acrylyl-CoA + NADH + H+
propanoyl-CoA + NAD+
show the reaction diagram
acrylyl-CoA + NADPH + H+
propanoyl-CoA + NADP+
show the reaction diagram
acrylyl-CoA + NADPH + H+
propionyl-CoA + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acrylyl-CoA + NADPH + H+
propanoyl-CoA + NADP+
show the reaction diagram
acrylyl-CoA + NADPH + H+
propionyl-CoA + NADP+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
-
dependent on
NADPH
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
not inhibitory: EDTA, Zn2+, other divalent cations
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003
acryloyl-CoA
pH 6.0, 65C
0.0011 - 0.0028
acrylyl-CoA
0.018 - 0.036
NADPH
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
45 - 80
acrylyl-CoA
13
NADPH
pH 6.0, 65C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
53333
acrylyl-CoA
-
pH 7.0, 30C, recombinant His-tagged enzyme
100 - 420
NADH
2700 - 6700
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.016
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enzyme activity in crude cell extract of D-glucose-grown cells, pH 7.5, temperature not specified in the publication
0.195
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enzyme activity in crude cell extract of dimethylsulphoniopropionate-grown cells, pH 7.5, temperature not specified in the publication
18.7
pH 6.0, 65C
23
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cell extract, at pH 7.0 and 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
-
broad optimum
6.5
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assay at
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
half-maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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anoxygenic phototroph Rhodobacter sphaeroides uses 3-hydroxypropionate as a sole carbon source for growth
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38600
1 * 39000, SDS-PAGE, 1 * 38600, calculated
39000
1 * 39000, SDS-PAGE, 1 * 38600, calculated
40000
-
x * 40000, SDS-PAGE
43000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
1 * 39000, SDS-PAGE, 1 * 38600, calculated
additional information
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 30% glycerol, stable for months
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by anion exchange and hydrophobic interaction chromatography, ultrafiltration, hydroxyapatatite chromatography, and again ultrafiltration. The enzyme is separated from acryloyl-CoA hydratase
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Ni-NTA column chromatography and Superose 12 gel filtration
recombinant His-tagged enzyme from Escherichia coli strain Rosetta 2(DE3) by immobilized metal affinity chromatography and gel filtration
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recombinant His10-tagged enzyme 11fold from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and gel filtration
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recombinant His10-tagged enzyme 4fold from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and gel filtration
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recombinant His10-tagged enzyme 6fold from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Rosetta2 (DE3) cells
gene Msed_1426, cloned from genomic DNA, recombinant co-expression of His-tagged enzyme with enzyme succinic semialdehyde reductase (NADPH), SSR, gene Msed_1424 from Metallosphaera sedula, in Escherichia coli strain Rosetta 2(DE3). Construction of a yeast two-hybrid assay for protein interaction analysis of ACR and SSR. ACR cannot be expressed in soluble, active form in Escherichia coli
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gene RSP_1434, recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
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gene SPO1914, the gene is adjacent to and predicted to be within the same transcriptional unit as dmdA, which encodes the enzyme for the first step of the demethylation pathway
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gene SPO_1914, recombinant expression of N-terminally His10-tagged enzyme in Escherichia coli strain Rosetta2 (DE3), recombinant expression in Rhodobacter sphaeroides mutant DELTAacuI::kan complements 3-hydroxypropionate-dependent growth of the mutant strain
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gene yhdH, cloning and expression of N-terminally His10-tagged enzyme in Escherichia coli strain Rosetta2 (DE3), recombinant expression in Rhodobacter sphaeroides mutant DELTAacuI::kan complements 3-hydroxypropionate-dependent growth of the mutant strain
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced 14fold in dimethylsulphoniopropionate-grown cells
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the enzyme is upregulated in cell extracts of Rhodobacter sphaeroides grown with 3-hydroxypropionate compared to those grown with succinate as a sole carbon source
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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