Information on EC 1.3.1.86 - crotonyl-CoA reductase

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

EC NUMBER
COMMENTARY hide
1.3.1.86
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RECOMMENDED NAME
GeneOntology No.
crotonyl-CoA reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
butanoyl-CoA + NADP+ = (E)-but-2-enoyl-CoA + NADPH + H+
show the reaction diagram
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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reductive carboxylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Butanoate metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
butanoyl-CoA:NADP+ 2,3-oxidoreductase
Catalyses the reaction in the reverse direction. This enzyme from Streptomyces collinus is specific for (E)-but-2-enoyl-CoA, and is proposed to provide butanoyl-CoA as a starter unit for straight-chain fatty acid biosynthesis.
CAS REGISTRY NUMBER
COMMENTARY hide
37251-07-3
cf. EC 1.3.1.8
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(E)-but-2-enoyl-CoA + NADPH + H+
butanoyl-CoA + NADP+
show the reaction diagram
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-
?
crotonyl-CoA + NADH + ferredoxin
butyryl-CoA + ?
show the reaction diagram
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-
-
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?
crotonyl-CoA + NADPH + H+
butanoyl-CoA + NADP+
show the reaction diagram
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the enzyme exhibits a high substrate specificity for crotonyl-CoA
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-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
show the reaction diagram
trans-crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
show the reaction diagram
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the crotonyl-CoA reductase reaction requires NADPH as electron donor
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
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in the absence of ferredoxin, a remarkable stimulation of crotonyl-CoA reduction by FAD is observed
Ferredoxin
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butyryl-CoA dehydrogenase from C. difficile belongs to the subfamily of bifurcating enzymes capable of coupling the exergonic reduction of crotonyl-CoA by NAD Hwith the endergonic reduction of ferredoxin by NADH
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NADPH
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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at high concentrations beta-mercaptoethanol is inhibitory
2-methylcrotonyl-CoA
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CoA-activated enzyme shows competitive inhibition with the substrate analog 2-methylcrotonyl-CoA
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
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extremely potent inhibitor
5,5'-dithiobis(2-nitrobenzoic acid)
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extremely potent inhibitor
acetyl-CoA
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competitive inhibitor
ammonium sulfate
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enzyme activity is inhibited by ammonium sulfatehowever, this inhibition is overcome by addition of 10 mM guanidine
arachidoyl-CoA
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86% residual activity at 0.1 mM
butyryl-CoA
Ca2+
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complete inhibition at 1 mM
Co2+
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complete inhibition at 1 mM
dithiothreitol
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at high concentrations dithiothreitol is inhibitory
iodoacetamide
iodoacetate
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isomyristoyl-CoA
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78% residual activity at 0.1 mM
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isopalmitoyl-CoA
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95% residual activity at 0.1 mM
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malonyl-CoA
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noncompetitive inhibitor
Mg2+
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30% inhibition at 1 mM
Mn2+
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complete inhibition at 1 mM
myristoyl-CoA
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36% residual activity at 0.1 mM
N-ethylmaleimide
NADPH
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concentrations of NADPH above 0.2 mM lead to inhibition of enzyme activity
p-chloromercuribenzoate
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a 30-min incubation of crotonyl-CoA reductase with p-chloromercuribenzoate at 0.008 mM leads to approximately 8.5% inhibition of enzyme activity
palmitoyl-CoA
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24% residual activity at 0.1 mM
stearoyl-CoA
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92% residual activity at 0.1 mM
Zn2+
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55% inhibition at 1 mM
additional information
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no significant inhibition of the activity of crotonyl-CoA reductase is observed upon addition of either flavin adenine dinucleotide (0.018 and 0.072 mM) or flavin mononucleotide (0.013 and 0.130 mM)
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoA
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free CoA is a strong activator of the reductase reaction
L-arabinose
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about 2fold CCR activity is obtained by the addition of 0.1% (w/v) of L-arabinose
additional information
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no significant activation of the activity of crotonyl-CoA reductase is observed upon addition of either flavin adenine dinucleotide (0.018 and 0.072 mM) or flavin mononucleotide (0.013 and 0.130 mM)
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01
butyryl-CoA
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pH 7.5, temperature not specified in the publication
0.0025 - 0.018
crotonyl-CoA
0.002
Ferredoxin
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pH 7.5, temperature not specified in the publication
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0.145
NADH
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pH 7.5, temperature not specified in the publication
0.00364 - 0.015
NADPH
0.0033
trans-crotonyl-CoA
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in 200 mM potassium phosphate buffer, pH 6.8, at 26C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 8
butyryl-CoA
Clostridioides difficile
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pH 7.5, temperature not specified in the publication
19
crotonyl-CoA
Clostridioides difficile
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pH 7.5, temperature not specified in the publication
37
Ferredoxin
Clostridioides difficile
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pH 7.5, temperature not specified in the publication
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3 - 6
NADH
Clostridioides difficile
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pH 7.5, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2800
butyryl-CoA
Clostridioides difficile
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pH 7.5, temperature not specified in the publication
270
7600
crotonyl-CoA
Clostridioides difficile
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pH 7.5, temperature not specified in the publication
406
18500
Ferredoxin
Clostridioides difficile
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pH 7.5, temperature not specified in the publication
169
250
NADH
Clostridioides difficile
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pH 7.5, temperature not specified in the publication
8
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0029
2-methylcrotonyl-CoA
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pH and temperature not specified in the publication
0.006
acetyl-CoA
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pH and temperature not specified in the publication
0.005 - 0.9
butyryl-CoA
0.5
isomyristoyl-CoA
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in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30C
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0.4
isopalmitoyl-CoA
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Ki above 0.4 mM, in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30C
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0.021
malonyl-CoA
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pH and temperature not specified in the publication
0.017
myristoyl-CoA
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in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30C
0.63
NADP+
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in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30C
0.0095
palmitoyl-CoA
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in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0008
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native enzyme, pH and temperature not specified in the publication
0.00091
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native enzyme from crude extract, pH 7.5 at 30C
0.0061
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crude extract, pH 6.8, at 26C
0.0156
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recombinant enzyme, pH and temperature not specified in the publication
0.0501
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after 11.2fold purification, pH 6.8, at 26C
0.333
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recombinant enzyme from crude extract, pH 7.5 at 30C
2.889
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native enzyme after 3068fold purification, pH 7.5 at 30C
3.316
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recombinant enzyme after 10fold purification, pH 7.5 at 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
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2 * 48000, SDS-PAGE
49400
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2 * 49400, calculated from amino acid sequence
85000
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native protein, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 48000, SDS-PAGE; 2 * 49400, calculated from amino acid sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
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at 40C the enzyme retains 47% of its activity after 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the crotonyl-CoA reductase activity is influenced by preincubation. 0.25 M Tris-HCl buffer diminishes the crotonyl-CoA reductase activity by approximately 30%
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, calcium phosphate gel treatment, alumina gel Cgamma extract filtration, Sephadex G-200 gel filtration
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ammonium sulfate precipitation, DEAE-cellulose column chromatography, phenyl-Sepharose column chromatography, Mono Q column chromatography, Sephadex G-100 gel filtration, and phenyl-Superose gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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expressed in Escherichia coli BL21 (DE3)/pZYB3 cells
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expressed in Ralstonia eutropha strain PHB-4
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expressed in Streptomyces cinnamonensis strain L1
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expressed in Streptomyces erythraea strain EAT4
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the addition of 1.0 g/l L-lysine induces expression of the ccr gene in Streptomyces cinnamonensis strain C730.1 in chemically defined medium containing mainly D-glucose (12 g/l), L-tyrosine (3.3 g/l), and either L-valine (6.7 g/l) or L-leucine (7.5 g/l) as carbon and nitrogen sources
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