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EC Tree
IUBMB Comments The enzyme adds a methylene group across the 9,10 position of a Delta9-olefinic acyl chain in phosphatidylethanolamine or, more slowly, phosphatidylglycerol or phosphatidylinositol, forming a cyclopropane derivative (cf. EC 2.1.1.16 methylene-fatty-acyl-phospholipid synthase).
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
cfa synthase, cyclopropane fatty acid synthase, cyclopropane synthase, sfcpa-fas, cyclopropane fatty acid synthetase, cyclopropane-fatty-acyl-phospholipid synthase, c17:cyclopropane synthase, hp0416,
more
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cyclopropane fatty acid synthetase
-
cyclopropane-fatty-acyl-phospholipid synthase
-
cyclopropane fatty acid synthase
cyclopropane fatty acid synthetase
-
-
-
-
synthetase, cyclopropane fatty acid
-
-
-
-
unsaturated-phospholipid methyltransferase
-
-
-
-
CFA synthase
-
-
-
-
CFAS
-
-
-
-
cyclopropane fatty acid synthase
-
-
-
-
cyclopropane fatty acid synthase
-
-
cyclopropane synthase
-
-
-
-
cyclopropane synthase
-
-
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S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
both chemical steps of the enzymatic cyclopropanation, the methyl addition onto the double bond and the deprotonation step, are rate determining
-
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methyl group transfer
-
-
-
-
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S-adenosyl-L-methionine:unsaturated-phospholipid methyltransferase (cyclizing)
The enzyme adds a methylene group across the 9,10 position of a Delta9-olefinic acyl chain in phosphatidylethanolamine or, more slowly, phosphatidylglycerol or phosphatidylinositol, forming a cyclopropane derivative (cf. EC 2.1.1.16 methylene-fatty-acyl-phospholipid synthase).
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S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
-
-
?
S-adenosyl-L-methionine + 1-stearoyl-2-oleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)]
S-adenosyl-L-homocysteine + 1-stearoyl-2-dihydrosterculoyl-sn-glycero-3-[phospho-rac-(1-glycerol)]
-
reaction takes place via methyl transfer followed by proton loss, rather than by processes that are initiated by proton abstraction from S-adenosyl-L-methionine. Methyl transfer takes place via a tight SN2 transition state
-
-
?
S-adenosyl-L-methionine + cardiolipin
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + phosphatidylcholine
?
-
the enzyme acts primarily on the sn-1 position of + phosphatidylcholine
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + phosphatidylglycerol
S-adenosyl-L-homocysteine + ?
-
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
S-adenosyl-L-methionine + phospholipids
S-adenosyl-L-homocysteine + phospholipid + cyclopropane fatty acid
-
-
-
-
?
S-adenosyl-L-methionine + triacylglycerol
?
-
-
-
-
?
Se-adenosyl-L-selenomethionine + 1-stearoyl-2-oleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)]
Se-adenosyl-L-selenohomocysteine + 1-stearoyl-2-dihydrosterculoyl-sn-glycero-3-[phospho-rac-(1-glycerol)]
-
-
-
-
?
Te-adenosyl-L-telluromethionine + 1-stearoyl-2-oleoyl-sn-glycero-3-[phospho-rac-(1-glycerol)]
Te-adenosyl-L-tellurohomocysteine + 1-stearoyl-2-dihydrosterculoyl-sn-glycero-3-[phospho-rac-(1-glycerol)]
-
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
-
no exchange of the cylopropane methylene protons with the solvent during catalysis. There is a significant intermolecular primary tritium kinetic isotope effect consistent with a partially rate determining deprotonation step
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
reaction is not affected by the order-disorder state of the lipid substrate
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
increased level of cyclopropane fatty acid synthase activity as bacterial cultures enter stationary phase is transient, activity quickly declines to the basal level, the loss of activity is due to proteolytic degradation dependent on expression of the heat shock regulon
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
methylation of unsaturated fatty acid moieties of phospholipids in the phospholipid bilayer
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
the enzyme acts on sn-2 of phospholipids
-
-
?
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S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
increased level of cyclopropane fatty acid synthase activity as bacterial cultures enter stationary phase is transient, activity quickly declines to the basal level, the loss of activity is due to proteolytic degradation dependent on expression of the heat shock regulon
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
methylation of unsaturated fatty acid moieties of phospholipids in the phospholipid bilayer
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
the enzyme acts on sn-2 of phospholipids
-
-
?
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(12aS,12bS)-7-fluoro-2,3,5,12,12a,12b-hexahydro-1H,4H-11-oxa-3a,9b-diazabenzo[a]naphtho[2,1,8-cde]azulene
-
-
(1R,7aR)-hexahydro-1H-pyrrolizin-1-ylmethyl 4-hydroxy-3,5-dimethoxybenzoate
-
-
1,2,5-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
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-
2,5,11-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
-
-
3-palmitoyl-2-(9/10-epoxyoleoyl)phosphatidylethanolamine
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-
3-palmitoyl-2-(9/10-fluorooleoyl)phosphatidyl ethanolamine
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3beta,5alpha-17a-aza-D-homoandrostan-3-ol
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5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
5,5'-dithiobis(2-nitrobenzoic acid)
5,5'-dithiobis-(2-nitrobenzoic acid)
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substrate does not protect against inactivation
9-methoxy-1,2,5-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
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N,N,N-trimethylhexadecan-1-aminium bromide
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N-decyl-N,N-dimethyldecan-1-aminium bromide
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p-hydroxymercuribenzoate
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sorbitol monolaurate ester
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sorbitol monooleate ester
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additional information
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identification of new inhibitors of Escherichia coli cyclopropane fatty acid synthase using a colorimetric assay
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5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
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5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
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this compound is also found to completely inhibit cyclopropanation of the phospholipids in growing Escherichia coli cells in vivo, at 0.15 mM
5,5'-dithiobis(2-nitrobenzoic acid)
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5,5'-dithiobis(2-nitrobenzoic acid)
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reversed by addition of dithiothreitol
S-adenosylhomocysteine
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-
S-adenosylhomocysteine
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product inhibition
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bicarbonate
-
required. CFA synthase isolated and assayed in potassium bicarbonate buffer displayes more than 3-fold higher activity than in HEPES buffer
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0.07 - 0.105
S-adenosyl-L-methionine
0.0564
Se-adenosyl-L-selenomethionine
-
-
0.74
Te-adenosyl-L-telluromethionine
-
-
additional information
additional information
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Km (phospholipids): 0.5 mg/ml. Since a mixture of phospholipids prepared from an Escherichia coli K12 strain is used, the Km constant is only an apparent constant given in mg/mL unit rather than molar unit
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0.07
S-adenosyl-L-methionine
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37°C, pH 8.0, wild-type enzyme
0.0705
S-adenosyl-L-methionine
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purification buffer/assay buffer: KHCO3/HEPES
0.0716
S-adenosyl-L-methionine
-
purification buffer/assay buffer: HEPES/KHCO3
0.073
S-adenosyl-L-methionine
-
mutant enzyme C176S
0.075
S-adenosyl-L-methionine
-
37°C, pH 8.0, mutant enzyme C139S
0.078
S-adenosyl-L-methionine
-
37°C, pH 8.0, mutant enzyme H266A
0.08
S-adenosyl-L-methionine
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-
0.08
S-adenosyl-L-methionine
-
37°C, pH 7.4
0.088
S-adenosyl-L-methionine
-
mutant enzyme C139S
0.0887
S-adenosyl-L-methionine
-
purification buffer/assay buffer: HEPES/HEPES
0.0894
S-adenosyl-L-methionine
-
-
0.09
S-adenosyl-L-methionine
-
-
0.09
S-adenosyl-L-methionine
-
wild-type enzyme
0.0997
S-adenosyl-L-methionine
-
purification buffer/assay buffer: KHCO3/KHCO3
0.105
S-adenosyl-L-methionine
-
mutant enzyme C354S
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0.0025 - 2.7
S-adenosyl-L-methionine
0.217
Se-adenosyl-L-selenomethionine
-
-
0.06
Te-adenosyl-L-telluromethionine
-
-
0.0025
S-adenosyl-L-methionine
-
37°C, pH 8.0, mutant enzyme H266A
0.0142
S-adenosyl-L-methionine
-
37°C, pH 8.0, mutant enzyme C139S
0.042
S-adenosyl-L-methionine
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37°C, pH 8.0, wild-type enzyme
0.067
S-adenosyl-L-methionine
-
37°C, pH 7.4
0.12
S-adenosyl-L-methionine
-
-
0.3
S-adenosyl-L-methionine
-
mutant enzyme C139S
1.6
S-adenosyl-L-methionine
-
mutant enzyme C354S
2.2
S-adenosyl-L-methionine
-
wild-type enzyme
2.7
S-adenosyl-L-methionine
-
mutant enzyme C176S
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0.0011 - 0.0014
(12aS,12bS)-7-fluoro-2,3,5,12,12a,12b-hexahydro-1H,4H-11-oxa-3a,9b-diazabenzo[a]naphtho[2,1,8-cde]azulene
0.006 - 0.016
5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
0.00013 - 0.00026
dioctylamine
0.037
N,N,N-trimethylhexadecan-1-aminium bromide
-
37°C, pH 7.4
0.011
N-decyl-N,N-dimethyldecan-1-aminium bromide
-
37°C, pH 7.4
0.01
N-hexylhexan-1-amine
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37°C, pH 7.4
0.004
N-octyloctan-1-amine
-
37°C, pH 7.4
0.22
S-adenosylhomocysteine
-
-
0.0005 - 0.0072
sinefungin
0.0011
(12aS,12bS)-7-fluoro-2,3,5,12,12a,12b-hexahydro-1H,4H-11-oxa-3a,9b-diazabenzo[a]naphtho[2,1,8-cde]azulene
-
inhibits CAFS in a mixed-type fashion with respect to phospholipids
0.0014
(12aS,12bS)-7-fluoro-2,3,5,12,12a,12b-hexahydro-1H,4H-11-oxa-3a,9b-diazabenzo[a]naphtho[2,1,8-cde]azulene
-
inhibits the CFAS non-competitively with respect to AdoMet
0.006
5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
-
apparent inhibition constant when the phospholipids are the variable substrates. Noncompetitive inhibitor with respect to both substrates
0.011
5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
-
37°C, pH 7.4
0.016
5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
-
apparent inhibition constant when S-adenosyl-L-methionine is the variable substrates. Noncompetitive inhibitor with respect to both substrates
0.00013
dioctylamine
-
competitive inhibitor with respect to phospholipids
0.00026
dioctylamine
-
uncompetitive inhibitor with respect to S-adenosyl-L-methionine
0.0005
sinefungin
-
competitive inhibitor with respect to S-adenosyl-L-methionine
0.0072
sinefungin
-
non-competitive inhibitor with respect to the phospholipids
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0.007
(12aS,12bS)-7-fluoro-2,3,5,12,12a,12b-hexahydro-1H,4H-11-oxa-3a,9b-diazabenzo[a]naphtho[2,1,8-cde]azulene
Escherichia coli
-
-
0.01
(1R,7aR)-hexahydro-1H-pyrrolizin-1-ylmethyl 4-hydroxy-3,5-dimethoxybenzoate
Escherichia coli
-
-
0.004
1,2,5-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
Escherichia coli
-
-
0.005
2,5,11-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
Escherichia coli
-
-
0.009
3beta,5alpha-17a-aza-D-homoandrostan-3-ol
Escherichia coli
-
-
0.01
5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
Escherichia coli
-
-
0.001
9-methoxy-1,2,5-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
Escherichia coli
-
-
0.004
dioctylamine
Escherichia coli
-
-
0.009
sinefungin
Escherichia coli
-
-
0.01
sinefungin
Escherichia coli
-
37°C, pH 7.4
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additional information
-
-
additional information
-
-
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UniProt
brenda
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-
-
brenda
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loosely associated with the inner membrane
brenda
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43913
-
x * 43913, calculation from nucleotide sequence
90000
-
equilibrium sedimentation, gel filtration
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monomer
-
1 * 90000, SDS-PAGE
?
-
x * 43913, calculation from nucleotide sequence
?
-
x * 80000-100000, SDS-PAGE
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G236E
active site mutant, replacing the strictly conserved G236 by a glutamate residue, which corresponds to E146 of the homologous mycolic acid methyltransferase. Mutant has less than 1% of the in vitro activity of the wild-type enzyme and leads to the formation of cyclopropanated fatty acid methyl esters and of new C17 methyl-branched unsaturated fatty acid methyl esters. The double bond of the latters is located at different positions 8, 9 or 10, and the methyl group at position 10 or 9. The reaction catalyzed by G236E mutant thus starts by the methylation of the unsaturated acyl chain at position 10 or 9 yielding a carbocation at position 9 or 10 respectively. It follows then two competing steps, a normal cyclopropanation or hydride shift/elimination events giving different combinations of alkenes
C176S
-
150% of wild-type activity
C354S
-
63% of wild-type activity
E239D
-
mutant shows 0.96% of wild-type activity
E239Q
-
catalytic efficiency is less than 0.02% of wild-type value
G236E
the mutant has less than 1% of the in vitro activity of the wild type enzyme. The reaction catalyzed by this G236E mutant starts by the methylation of the unsaturated acyl chain at position 10 or 9 yielding a carbocation at position 9 or 10 respectively
C139S
-
15% of wild-type activity
C139S
-
mutant retains 31% of the activity of the wild-type enzyme. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 85% of wild-type activity
E239A
-
catalytic efficiency is 0.2% of wild-type value
E239A
-
mutant shows 0.57% of wild-type activity
H266A
-
catalytic efficiency is 5.3% of wild-type value. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 16% of wild-type activity
H266A
-
mutant shows 2.1% of wild-type activity
Y317F
-
catalytic efficiency is 0.7% of wild-type value. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 14% of wild-type activity
Y317F
-
mutant shows 0.45% of wild-type activity
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37
-
30 min, complete loss of activity in absence of lipid
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sorbitol monolaurate ester stabilizes
-
sorbitol monooleate ester stabilizes
-
the enzyme is a short-lived protein in vivo and its degradation is dependent on expression of the heat shock regulon
-
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-20°C, in presence of phospholipid, stable for 2 months
-
-20°C, pH 7.4, 20 mM phosphate buffer, 50% v/v glycerol, best storage conditions
-
-78°C, 25% glycerol, less than 10% loss of activity after 6 months
-
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recombinant His6-tagged protein
-
wild-type and six-histidine-tagged mutant enzymes H266A, Y317F, E239A, and E239Q
-
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expressed in Saccharomyces cerevisiae strain BY4741
expressed in Arabidopsis thaliana
-
His-tagged recombinant protein
-
mutant enzyme G236E oís expressed in Escherichia coli BL21(DE3) cells
overproduced as a His6-tagged protein
-
overproduction of the enzyme via multicopy cfa plasmids
-
recombinantly expressed in Escherichia coli
-
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cfa transcription is strongly induced by neutral acetate, whereas 250 mM acetate is stimulatory no chloride concentration over this range activates transcription, cfa P2 promoter is not stimulated by acetate when transcribed by sigma70
-
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Taylor, F.R.; Grogan, D.W.; Cronan, J.E.
Cyclopropane fatty acid synthase from Escherichia coli
Methods Enzymol.
71
133-139
1981
Escherichia coli, Escherichia coli B / ATCC 11303
brenda
Wang, A.Y.; Grogan, D.W.; Cronan, J.E.
Cyclopropane fatty acid synthase of Escherichia coli: deduced amino acid sequence, purification, and studies of the enzyme active site
Biochemistry
31
11020-11028
1992
Escherichia coli
brenda
Grogan, D.W.; Cronan, J.E.
Cloning and manipulation of the Escherichia coli cyclopropane fatty acid synthase gene: physiological aspects of enzyme overproduction
J. Bacteriol.
158
286-295
1984
Escherichia coli
brenda
Taylor, F.R.; Cronan, J.E.
Cyclopropane fatty acid synthase of Escherichia coli. Stabilization, purification, and interaction with phospholipid vesicles
Biochemistry
18
3292-3300
1979
Escherichia coli
brenda
Chang, Y.Y.; Eichel, J.; Cronan, J.E., Jr.
Metabolic instability of Escherichia coli cyclopropane fatty acid synthase is due to RpoH-dependent proteolysis
J. Bacteriol.
182
4288-4294
2000
Escherichia coli
brenda
Iwig, D.F.; Grippe, A.T.; McIntyre, T.A.; Booker, S.J.
Isotope and elemental effects indicate a rate-limiting methyl transfer as the initial step in the reaction catalyzed by Escherichia coli cyclopropane fatty acid synthase
Biochemistry
43
13510-13524
2004
Escherichia coli
brenda
Molitor, E.J.; Paschal, B.M.; Liu, H.w.
Cyclopropane fatty acid synthase from Escherichia coli: Enzyme purification and inhibition by vinylfluorine and epoxide-containing substrate analogues
ChemBioChem
4
1352-1356
2003
Escherichia coli
brenda
Courtois, F.; Guerard, C.; Thomas, X.; Ploux, O.
Escherichia coli cyclopropane fatty acid synthase
Eur. J. Biochem.
271
4769-4778
2004
Escherichia coli
brenda
Courtois, F.; Ploux, O.
Escherichia coli cyclopropane fatty acid synthase: is a bound bicarbonate ion the active-site base?
Biochemistry
44
13583-13590
2005
Escherichia coli
brenda
Guianvarch, D.; Drujon, T.; Leang, T.E.; Courtois, F.; Ploux, O.
Identification of new inhibitors of E. coli cyclopropane fatty acid synthase using a colorimetric assay
Biochim. Biophys. Acta
1764
1381-1388
2006
Escherichia coli
brenda
Iwig, D.F.; Uchida, A.; Stromberg, J.A.; Booker, S.J.
The activity of Escherichia coli cyclopropane fatty acid synthase depends on the presence of bicarbonate
J. Am. Chem. Soc.
127
11612-11613
2005
Escherichia coli
brenda
Guianvarch, D.; Guangqi E, D.; Drujon, T.; Rey, C.; Wang, Q.; Ploux, O.
Identification of inhibitors of the E. coli cyclopropane fatty acid synthase from the screening of a chemical library: In vitro and in vivo studies
Biochim. Biophys. Acta
1784
1652-1658
2008
Escherichia coli
brenda
Rosenthal, A.Z.; Kim, Y.; Gralla, J.D.
Regulation of transcription by acetate in Escherichia coli: in vivo and in vitro comparisons
Mol. Microbiol.
68
907-917
2008
Escherichia coli
brenda
Guangqi, E.; Lesage, D.; Ploux, O.
Insight into the reaction mechanism of the Escherichia coli cyclopropane fatty acid synthase: isotope exchange and kinetic isotope effects
Biochimie
92
1454-1457
2010
Escherichia coli
brenda
E, G.; Drujon, T.; Correia, I.; Ploux, O.; Guianvarch, D.
An active site mutant of Escherichia coli cyclopropane fatty acid synthase forms new non-natural fatty acids providing insights on the mechanism of the enzymatic reaction
Biochimie
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Escherichia coli, Escherichia coli (P0A9H7)
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Yu, X.H.; Prakash, R.R.; Sweet, M.; Shanklin, J.
Coexpressing Escherichia coli cyclopropane synthase with Sterculia foetida lysophosphatidic acid acyltransferase enhances cyclopropane fatty acid accumulation
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455-465
2014
Escherichia coli
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Peng, H.; He, L.; Haritos, V.S.
Enhanced production of high-value cyclopropane fatty acid in yeast engineered for increased lipid synthesis and accumulation
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e1800487
2019
Escherichia coli (P0A9H7), Escherichia coli
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