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3-hydroxyacyl CoA reductase
-
-
ambiguous
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acyl-CoA:NADP+ trans-2-oxidoreductase
-
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butanoyl-CoA:(acceptor) 2,3-oxidoreductase
-
-
-
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butyryl coenzyme A dehydrogenase
-
-
ambiguous
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butyryl dehydrogenase
-
-
-
-
butyryl-CoA dehydrogenase
-
-
ambiguous
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butyryl-CoA dehydrogenase complex
crotonyl CoA reductase
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crotonyl coenzyme A reductase
crotonyl-CoA reductase
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-
crotonyl-coenzyme A reductase
enoyl-coenzyme A reductase
-
-
ambiguous
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ethylene reductase
-
-
ambiguous
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short-chain acyl CoA dehydrogenase
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-
ambiguous
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short-chain acyl-coenzyme A dehydrogenase
-
-
ambiguous
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trans-crotonyl CoA reductase
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-
unsaturated acyl coenzyme A reductase
-
-
ambiguous
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unsaturated acyl-CoA reductase
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-
-
-
bcd2
-
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butyryl-CoA dehydrogenase complex
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butyryl-CoA dehydrogenase complex
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-
-
CCR
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-
ambiguous
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CD1054
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-
crotonyl coenzyme A reductase
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crotonyl coenzyme A reductase
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crotonyl-coenzyme A reductase
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crotonyl-coenzyme A reductase
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crotonyl-coenzyme A reductase
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-
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(E)-but-2-enoyl-CoA + NADPH + H+
butanoyl-CoA + NADP+
-
Substrates: -
Products: -
?
crotonyl-CoA + NADH + ferredoxin
butyryl-CoA + ?
-
Substrates: -
Products: -
?
crotonyl-CoA + NADPH + H+
butanoyl-CoA + NADP+
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Substrates: the enzyme exhibits a high substrate specificity for crotonyl-CoA
Products: -
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
trans-crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
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Substrates: the crotonyl-CoA reductase reaction requires NADPH as electron donor
Products: -
?
additional information
?
-
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
Substrates: -
Products: -
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
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Substrates: 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
Products: -
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
Substrates: -
Products: -
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
Substrates: -
Products: -
?
crotonyl-CoA + NADPH + H+
butyryl-CoA + NADP+
-
Substrates: -
Products: -
ir
additional information
?
-
-
Substrates: the crotonyl-CoA reductase reaction requires NADPH as electron donor, but at a 20fold higher concentration NADH will substitute for NADPH with 50% Vmax
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
?
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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)
-
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
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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
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40% inhibition at 1 mM
N-ethylmaleimide
-
extremely potent inhibitor
N-ethylmaleimide
-
80% inhibition at 1 mM
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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
0.0025
crotonyl-CoA
-
pH 7.5, temperature not specified in the publication
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
0.00364
NADPH
-
in 200 mM potassium phosphate buffer, pH 6.8, at 26°C
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
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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
0.005
butyryl-CoA
-
pH and temperature not specified in the publication
0.9
butyryl-CoA
-
in 50 mM Tris/HCI pH 6.5 and 10% (v/v) glycerol, at 30°C
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malfunction
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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
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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
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
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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
-
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
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physiological function
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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
physiological function
the enzyme (EgTER1) is involved in the greening process. It is dispensable for wax ester production under anaerobic conditions
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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 collinus, Streptomyces virginiae
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 virginiae
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 virginiae
brenda
Liu, H.; Reynolds, K.A.
Precursor supply for polyketide biosynthesis: the role of crotonyl-CoA reductase
Metab. Eng.
3
40-48
2001
Streptomyces virginiae
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
Tomiyama, T.; Goto, K.; Tanaka, Y.; Maruta, T.; Ogawa, T.; Sawa, Y.; Ito, T.; Ishikawa, T.
A major isoform of mitochondrial trans-2-enoyl-CoA reductase is dispensable for wax ester production in Euglena gracilis under anaerobic conditions
PLoS ONE
14
e0210755
2019
Euglena gracilis (Q5EU90), Euglena gracilis
brenda