We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments 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.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
3-hydroxyacyl CoA reductase, acyl-CoA:NADP+ trans-2-oxidoreductase, bcd2, butanoyl-CoA:(acceptor) 2,3-oxidoreductase, butyryl coenzyme A dehydrogenase, butyryl dehydrogenase, butyryl-CoA dehydrogenase, butyryl-CoA dehydrogenase complex, CCR,
CD1054 ,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-hydroxyacyl CoA reductase
-
-
ambiguous
-
acyl-CoA:NADP+ trans-2-oxidoreductase
-
-
butanoyl-CoA:(acceptor) 2,3-oxidoreductase
-
-
-
-
butyryl coenzyme A dehydrogenase
-
-
ambiguous
-
butyryl dehydrogenase
-
-
-
-
butyryl-CoA dehydrogenase
-
-
ambiguous
-
butyryl-CoA dehydrogenase complex
crotonyl CoA reductase
-
-
crotonyl coenzyme A reductase
crotonyl-CoA reductase
-
-
crotonyl-coenzyme A reductase
enoyl-coenzyme A reductase
-
-
ambiguous
-
ethylene reductase
-
-
ambiguous
-
short-chain acyl CoA dehydrogenase
-
-
ambiguous
-
short-chain acyl-coenzyme A dehydrogenase
-
-
ambiguous
-
trans-crotonyl CoA reductase
-
-
unsaturated acyl coenzyme A reductase
-
-
ambiguous
-
unsaturated acyl-CoA reductase
-
-
-
-
bcd2
-
-
butyryl-CoA dehydrogenase complex
-
-
butyryl-CoA dehydrogenase complex
-
-
-
CCR
-
-
ambiguous
-
CD1054
-
-
crotonyl coenzyme A reductase
-
-
crotonyl coenzyme A reductase
-
-
crotonyl-coenzyme A reductase
-
-
crotonyl-coenzyme A reductase
-
-
crotonyl-coenzyme A reductase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
butanoyl-CoA + NADP+ = (E)-but-2-enoyl-CoA + NADPH + H+
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
carboxylation
-
reductive carboxylation
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
37251-07-3
cf. EC 1.3.1.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(E)-but-2-enoyl-CoA + NADPH + H+
butanoyl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + NADH + ferredoxin
butyryl-CoA + ?
-
-
-
-
?
crotonyl-CoA + NADPH + H+
butanoyl-CoA + NADP+
-
the enzyme exhibits a high substrate specificity for crotonyl-CoA
-
-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
trans-crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
the crotonyl-CoA reductase reaction requires NADPH as electron donor
-
-
?
additional information
?
-
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
-
-
-
ir
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
-
-
-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
the overall reduction of crotonyl-CoA proceeds in an anti fashion, the reaction proceeds with transfer of the hydrogen from the pro-4S position of NADPH to the Re face of the beta-carbon of crotonyl-CoA
-
-
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
-
-
-
?
additional information
?
-
-
the crotonyl-CoA reductase reaction requires NADPH as electron donor, but at a 20fold higher concentration NADH will substitute for NADPH with 50% Vmax
-
-
?
additional information
?
-
-
the enzyme is unable to catalyze the reduction of any other enoyl-CoA thioesters (acryloyl-CoA, trans-2-pentenoyl-CoA, trans-hexenoyl-CoA, trans-2-octenoyl-CoA, trans-2-dodecenoyl-CoA, trans-2-hexadecenoyl-CoA) or to utilize NADH as an electron donor. The enzyme is unable to reduce either the N-acetylcysteamine or the pantetheine thioester of crotonic acid
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
FAD
-
in the absence of ferredoxin, a remarkable stimulation of crotonyl-CoA reduction by FAD is observed
Ferredoxin
-
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
-
NADPH
-
-
NADPH
-
NADPH is the sole electron donor for the reduction catalyzed by crotonyl-CoA reductase
NADPH
-
the crotonyl-CoA reductase reaction requires NADPH as electron donor, but at a 20fold higher concentration NADH will substitute for NADPH with 50% Vmax
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2-mercaptoethanol
-
at high concentrations beta-mercaptoethanol is inhibitory
2-methylcrotonyl-CoA
-
CoA-activated enzyme shows competitive inhibition with the substrate analog 2-methylcrotonyl-CoA
4-Chloro-7-nitrobenzo-2-oxa-1,3-diazole
-
extremely potent inhibitor
5,5'-dithiobis(2-nitrobenzoic acid)
-
extremely potent inhibitor
acetyl-CoA
-
competitive inhibitor
ammonium sulfate
-
enzyme activity is inhibited by ammonium sulfate ; however, this inhibition is overcome by addition of 10 mM guanidine
arachidoyl-CoA
-
86% residual activity at 0.1 mM
Ca2+
-
complete inhibition at 1 mM
Co2+
-
complete inhibition at 1 mM
dithiothreitol
-
at high concentrations dithiothreitol is inhibitory
isomyristoyl-CoA
-
78% residual activity at 0.1 mM
isopalmitoyl-CoA
-
95% residual activity at 0.1 mM
malonyl-CoA
-
noncompetitive inhibitor
Mg2+
-
30% inhibition at 1 mM
Mn2+
-
complete inhibition at 1 mM
myristoyl-CoA
-
36% residual activity at 0.1 mM
NADPH
-
concentrations of NADPH above 0.2 mM lead to inhibition of enzyme activity
p-chloromercuribenzoate
-
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
-
24% residual activity at 0.1 mM
stearoyl-CoA
-
92% residual activity at 0.1 mM
Zn2+
-
55% inhibition at 1 mM
additional information
-
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)
-
butyryl-CoA
-
competitive inhibitor
butyryl-CoA
-
slight inhibition
iodoacetamide
-
-
iodoacetamide
-
40% inhibition at 1 mM
N-ethylmaleimide
-
extremely potent inhibitor
N-ethylmaleimide
-
80% inhibition at 1 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CoA
-
free CoA is a strong activator of the reductase reaction
L-arabinose
-
about 2fold CCR activity is obtained by the addition of 0.1% (w/v) of L-arabinose
additional information
-
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)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.01
butyryl-CoA
-
pH 7.5, temperature not specified in the publication
0.0025 - 0.018
crotonyl-CoA
0.002
Ferredoxin
-
pH 7.5, temperature not specified in the publication
-
0.145
NADH
-
pH 7.5, temperature not specified in the publication
0.0033
trans-crotonyl-CoA
-
in 200 mM potassium phosphate buffer, pH 6.8, at 26°C
0.018
crotonyl-CoA
-
in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 1 mM dithioerythritol and 10% (v/v) glycerol, at 30°C
0.0025
crotonyl-CoA
-
pH 7.5, temperature not specified in the publication
0.015
NADPH
-
in 50 mM potassium phosphate, pH 7.5, 1 mM EDTA, 1 mM dithioerythritol and 10% (v/v) glycerol, at 30°C
0.00364
NADPH
-
in 200 mM potassium phosphate buffer, pH 6.8, at 26°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 - 8
butyryl-CoA
-
pH 7.5, temperature not specified in the publication
19
crotonyl-CoA
-
pH 7.5, temperature not specified in the publication
37
Ferredoxin
-
pH 7.5, temperature not specified in the publication
-
3 - 6
NADH
-
pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2800
butyryl-CoA
-
pH 7.5, temperature not specified in the publication
7600
crotonyl-CoA
-
pH 7.5, temperature not specified in the publication
18500
Ferredoxin
-
pH 7.5, temperature not specified in the publication
-
250
NADH
-
pH 7.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0029
2-methylcrotonyl-CoA
-
pH and temperature not specified in the publication
0.006
acetyl-CoA
-
pH and temperature not specified in the publication
0.5
isomyristoyl-CoA
-
in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30°C
0.4
isopalmitoyl-CoA
-
Ki above 0.4 mM, in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30°C
0.021
malonyl-CoA
-
pH and temperature not specified in the publication
0.017
myristoyl-CoA
-
in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30°C
0.63
NADP+
-
in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30°C
0.0095
palmitoyl-CoA
-
in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30°C
0.9
butyryl-CoA
-
in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30°C
0.005
butyryl-CoA
-
pH and temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0008
-
native enzyme, pH and temperature not specified in the publication
0.00091
-
native enzyme from crude extract, pH 7.5 at 30°C
0.0061
-
crude extract, pH 6.8, at 26°C
0.0156
-
recombinant enzyme, pH and temperature not specified in the publication
0.0501
-
after 11.2fold purification, pH 6.8, at 26°C
0.333
-
recombinant enzyme from crude extract, pH 7.5 at 30°C
2.889
-
native enzyme after 3068fold purification, pH 7.5 at 30°C
3.316
-
recombinant enzyme after 10fold purification, pH 7.5 at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
-
-
brenda
strain C730.1
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
physiological function
-
CCR and the butyryl-CoA pathway provide the majority of methylmalonyl-CoA and ethylmalonyl-CoA for monensin A biosynthesis
physiological function
-
CCR plays a significant role in providing methylmalonyl-CoA for monensin biosynthesis in oil-based 10-day fermentations of Streptomyces cinnamonensis
physiological function
-
CCR plays a significant role in providing methylmalonyl-CoA for monensin biosynthesis in oil-based 10-day fermentations of Streptomyces cinnamonensis
physiological function
-
CCR provides butyryl-CoA precursor for monensin A biosynthesis
physiological function
-
in streptomycetes, Ccr catalyzes the last step in the reductive biosynthesis of butyryl-CoA from two molecules of acetyl-CoA
physiological function
-
the ccr gene is involved in a novel butytryl-CoA pathway for the growth of Streptomyces collinus when acetate is its sole carbon source
physiological function
-
the enzyme plays a role in providing butyryl-CoA as a starter unit for straight-chain fatty acid biosynthesis
malfunction
-
loss of ccr leads to lower levels of the monensin precursor methymalonyl-CoA, relative to coenzyme A
malfunction
-
loss of ccr leads to lower levels of the monensin precursor methymalonyl-CoA, relative to coenzyme A
malfunction
-
the ability of the ccr deletion mutant of Streptomyces collinus to grow on acetate is dramatically reduced
metabolism
-
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
metabolism
-
the genes necessary for butyrate formation from the genome of Clostridium difficile are expressed in Escherichia coli. The individual genes are assembled in a single plasmid vector into an artificial operon , which allows functional coexpression of the required genes and confers butyrate-forming capability to the host
metabolism
-
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
-
metabolism
-
the genes necessary for butyrate formation from the genome of Clostridium difficile are expressed in Escherichia coli. The individual genes are assembled in a single plasmid vector into an artificial operon , which allows functional coexpression of the required genes and confers butyrate-forming capability to the host
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
48000
-
2 * 48000, SDS-PAGE
49400
-
2 * 49400, calculated from amino acid sequence
85000
-
native protein, gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homodimer
-
2 * 48000, SDS-PAGE
homodimer
-
2 * 49400, calculated from amino acid sequence
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
40
-
at 40°C the enzyme retains 47% of its activity after 30 min
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
the crotonyl-CoA reductase activity is influenced by preincubation. 0.25 M Tris-HCl buffer diminishes the crotonyl-CoA reductase activity by approximately 30%
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ammonium sulfate precipitation, calcium phosphate gel treatment, alumina gel Cgamma extract filtration, Sephadex G-200 gel filtration
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3)/pZYB3 cells
-
expressed in Ralstonia eutropha strain PHB-4
-
expressed in Streptomyces cinnamonensis strain L1
-
expressed in Streptomyces erythraea strain EAT4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Strom, K.A.; Kumar, S.
Activation and inhibition of crotonyl-coenzyme A reductase activity of bovine mammary fatty acid synthetase
J. Biol. Chem.
254
8159-8162
1979
Bos taurus
-
brenda
Maitra, S.K.; Kumar, S.
Crotonyl coenzyme A reductase activity of bovine mammary fatty acid synthetase
J. Biol. Chem.
249
111-117
1974
Bos taurus
brenda
Li, C.; Florova, G.; Akopiants, K.; Reynolds, K.A.
Crotonyl-coenzyme A reductase provides methylmalonyl-CoA precursors for monensin biosynthesis by Streptomyces cinnamonensis in an oil-based extended fermentation
Microbiology
150
3463-3472
2004
Streptomyces cinnamonensis, Streptomyces collinus
brenda
Dodds, P.F.; Kumar, S.
Effects of coenzyme A and pH on the reactions catalyzed by lactating bovine mammary-gland fatty acid synthase
Biochem. Soc. Trans.
9
556-557
1981
Bos taurus
-
brenda
Fukui, T.; Abe, H.; Doi, Y.
Engineering of Ralstonia eutropha for production of poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) from fructose and solid-state properties of the copolymer
Biomacromolecules
3
618-624
2002
Streptomyces cinnamonensis
brenda
Wallace, K.K.; Bao, Z.Y.; Dai, H.; Digate, R.; Schuler, G.; Speedie, M.K.; Reynolds, K.A.
Purification of crotonyl-CoA reductase from Streptomyces collinus and cloning, sequencing and expression of the corresponding gene in Escherichia coli
Eur. J. Biochem.
233
954-962
1995
Streptomyces collinus
brenda
Liu, H.; Wallace, K.K.; Reynolds, K.A.
Linking diversity in evolutionary origin and stereospecificity for enoyl thioester reductases: determination and interpretation of the novel stereochemical course of reaction catalyzed by crotonyl CoA reductase from Streptomyces collinus
J. Am. Chem. Soc.
119
2973-2979
1997
Streptomyces collinus
-
brenda
Liu, Y.; Hazzard, C.; Eustaquio, A.S.; Reynolds, K.A.; Moore, B.S.
Biosynthesis of salinosporamides from alpha,beta-unsaturated fatty acids: implications for extending polyketide synthase diversity
J. Am. Chem. Soc.
131
10376-10377
2009
Salinispora tropica
brenda
Han, L.; Reynolds, K.A.
A novel alternate anaplerotic pathway to the glyoxylate cycle in streptomycetes
J. Bacteriol.
179
5157-5164
1997
Streptomyces collinus
brenda
Sun, W.-J.; Salmon, P.; Wilson, J.; Connors, N.
Crotonic acid-directed biosynthesis of the immunosuppressants produced by Streptomyces hygroscopicus var. ascomyceticus
J. Ferment. Bioeng.
86
261-265
1998
Streptomyces hygroscopicus subsp. ascomyceticus
-
brenda
Akopiants, K.; Florova, G.; Li, C.; Reynolds, K.A.
Multiple pathways for acetate assimilation in Streptomyces cinnamonensis
J. Ind. Microbiol. Biotechnol.
33
141-150
2006
Streptomyces cinnamonensis
brenda
Liu, H.; Reynolds, K.A.
Precursor supply for polyketide biosynthesis: the role of crotonyl-CoA reductase
Metab. Eng.
3
40-48
2001
Streptomyces cinnamonensis
brenda
Stassi, D.L.; Kakavas, S.J.; Reynolds, K.A.; Gunawardana, G.; Swanson, S.; Zeidner, D.; Jackson, M.; Liu, H.; Buko, A.; Katz, L.
Ethyl-substituted erythromycin derivatives produced by directed metabolic engineering
Proc. Natl. Acad. Sci. USA
95
7305-7309
1998
Streptomyces collinus
brenda
Aboulnaga, e.l.-.H.; Pinkenburg, O.; Schiffels, J.; El-Refai, A.; Buckel, W.; Selmer, T.
Effect of an Oxygen-Tolerant Bifurcating Butyryl Coenzyme A Dehydrogenase/Electron-Transferring Flavoprotein Complex from Clostridium difficile on Butyrate Production in Escherichia coli
J. Bacteriol.
195
3704-3713
2013
Clostridioides difficile
brenda
Select items on the left to see more content.
html completed