Information on EC 2.1.1.79 - cyclopropane-fatty-acyl-phospholipid synthase

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

EC NUMBER
COMMENTARY
2.1.1.79
-
RECOMMENDED NAME
GeneOntology No.
cyclopropane-fatty-acyl-phospholipid synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
-
S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
both chemical steps of the enzymatic cyclopropanation, the methyl addition onto the double bond and the deprotonation step, are rate determining
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
cyclopropane fatty acid (CFA) biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C17:cyclopropane synthase
-
-
CFA synthase
-
-
-
-
CFA synthase
-
-
CFA synthase
Brucella abortus 2308 NalR
-
-
-
CFA synthase
-
-
CFA synthase
-
-
CFA synthase
-
-
CFA synthase
Sinorhizobium meliloti RmP110
-
-
-
cfaB
-
gene encoding the major C17:cyclopropane synthase
CFAS
-
-
-
-
CPS1
-
isoform
CPS2
-
isoform
CPS3
-
isoform
cyclopropane fatty acid synthase
-
-
-
-
cyclopropane fatty acid synthase
-
-
cyclopropane fatty acid synthase
Brucella abortus 2308 NalR
-
-
-
cyclopropane fatty acid synthase
-
-
cyclopropane fatty acid synthase
-
-
cyclopropane fatty acid synthase
Lactobacillus reuteri ATCC PTA 6475
-
-
-
cyclopropane fatty acid synthase
-
-
cyclopropane fatty acid synthetase
-
-
-
-
cyclopropane fatty acyl synthase
-
-
cyclopropane fatty acyl synthase
Sinorhizobium meliloti RmP110
-
-
-
cyclopropane synthase
-
-
-
-
SfCPA-FAS
-
-
synthetase, cyclopropane fatty acid
-
-
-
-
unsaturated-phospholipid methyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
51845-48-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Brucella abortus 2308 NalR
-
-
-
Manually annotated by BRENDA team
BL21 transformed with plasmid pAYW58
-
-
Manually annotated by BRENDA team
strains K12 and LM-5005
-
-
Manually annotated by BRENDA team
Eubacterium HX
moderately-halophilic
-
-
Manually annotated by BRENDA team
Lactobacillus reuteri ATCC PTA 6475
-
-
-
Manually annotated by BRENDA team
strain MG1363
-
-
Manually annotated by BRENDA team
Lactococcus lactis MG1363
strain MG1363
-
-
Manually annotated by BRENDA team
strain ATCC BAA-1163, formerly Oenococcus oeni strain IOB 8413
-
-
Manually annotated by BRENDA team
strain KT2440
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
strain RmP110
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti RmP110
strain RmP110
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
mutants defective in cyclopropane fatty acid synthase are unable to suppress tumor necrosis factor production
malfunction
-
enzyme deficiency does not alter the ability of Brucella abortus to multiply in RAW 264.7 macrophages and in mice
malfunction
Brucella abortus 2308 NalR
-
enzyme deficiency does not alter the ability of Brucella abortus to multiply in RAW 264.7 macrophages and in mice
-
malfunction
Lactobacillus reuteri ATCC PTA 6475
-
mutants defective in cyclopropane fatty acid synthase are unable to suppress tumor necrosis factor production
-
physiological function
-
cfa2 is required for the cyclopropanation of phospholipids and of non phosphorus-containing lipids, neither cfa1 nor cfa2 is required for symbiotic nitrogen fixation
physiological function
-
in cotton, isoform CPS1 and CPS2 gene expression correlates with the total cyclic fatty acid content in roots, stems and seeds
physiological function
-
the enzyme suppresses tumor necrosis factor production by activated THP-1 human monocytoid cells
physiological function
-
the enzyme is useful for survival extracellularly, thus facilitating persistence in contaminated materials and transmission to new hosts
physiological function
Brucella abortus 2308 NalR
-
the enzyme is useful for survival extracellularly, thus facilitating persistence in contaminated materials and transmission to new hosts
-
physiological function
Lactobacillus reuteri ATCC PTA 6475
-
the enzyme suppresses tumor necrosis factor production by activated THP-1 human monocytoid cells
-
physiological function
Sinorhizobium meliloti RmP110
-
cfa2 is required for the cyclopropanation of phospholipids and of non phosphorus-containing lipids, neither cfa1 nor cfa2 is required for symbiotic nitrogen fixation
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-homocysteine + phosphatidylcholine
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
addition of the methylene group to oleic acid occurs at the sn-1 position
-
-
-
S-adenosyl-L-homocysteine + phosphatidylcholine
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
phosphatidylcholine is not a substrate
-
-
-
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)]
show the reaction diagram
-
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 + ?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + oleate
S-adenosyl-L-homocysteine + dihydrosterculate
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + oleate
S-adenosyl-L-homocysteine + dihydrosterculate
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + oleic acid
S-adenosyl-L-homocysteine + dihydrosterculic acid
show the reaction diagram
Lactobacillus reuteri, Lactobacillus reuteri ATCC PTA 6475
-
-
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + phosphatidylethanolamine
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
-
-
S-adenosyl-L-methionine + phosphatidylglycerol
S-adenosyl-L-homocysteine + ?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
Eubacterium HX
-
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
phosphatidylethanolamine which contains cyclopropane fatty acids
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
-
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
show the reaction diagram
-
addition of a methylene group from S-adenosylmethionine to the cis-double bond of monoenoic phospholipid-bound fatty acids
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
Serratia marcescens contains endogenous lipid substrates which cannot be removed or replaced by simple manipulations
phosphatidylethanolamine which contains cyclopropane fatty acids
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
S-adenosylmethionine levels in conjugation with cyclopropane fatty acid synthase activities regulates cyclopropane fatty acid synthesis in Lactobacillus plantarum
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
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
show the reaction diagram
-
increase in expression of CFA synthase at early stationary phase is due to the alternative sigma factor RpoS
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
the cfa locus is an essential component of the acid stress response of Lactococcus lactis MG1363
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
Brucella abortus 2308 NalR
-
-
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
Lactococcus lactis MG1363
-
the cfa locus is an essential component of the acid stress response of Lactococcus lactis MG1363
-
-
?
S-adenosyl-L-methionine + phospholipids
S-adenosyl-L-homocysteine + phospholipid + cyclopropane fatty acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + vaccenic acid
S-adenosyl-L-homocysteine + lactobacillic acid
show the reaction diagram
Lactobacillus reuteri, Lactobacillus reuteri ATCC PTA 6475
-
-
-
-
?
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)]
show the reaction diagram
-
-
-
-
?
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)]
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
growth conditions that result in an increase in the relative amount of C17:cyclopropane fatty acid yield better survival after lyophilization
-
-
-
additional information
?
-
Sinorhizobium meliloti, Sinorhizobium meliloti RmP110
-
cyclopropanation occurs in the sn-1 and sn-2 positions in lipids, cyclopropanation of phosphatidylcholines and sulfoquinovosyldiacylglycerols occurs more extensively with acidity than with phosphate starvation
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
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
show the reaction diagram
-
S-adenosylmethionine levels in conjugation with cyclopropane fatty acid synthase activities regulates cyclopropane fatty acid synthesis in Lactobacillus plantarum
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
-
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
show the reaction diagram
-
increase in expression of CFA synthase at early stationary phase is due to the alternative sigma factor RpoS
-
-
?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
Lactococcus lactis, Lactococcus lactis MG1363
-
the cfa locus is an essential component of the acid stress response of Lactococcus lactis MG1363
-
-
?
additional information
?
-
-
growth conditions that result in an increase in the relative amount of C17:cyclopropane fatty acid yield better survival after lyophilization
-
-
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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
-
-
2,5,11-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
-
-
3-palmitoyl-2-(9/10-epoxyoleoyl)phosphatidylethanolamine
-
-
3-palmitoyl-2-(9/10-fluorooleoyl)phosphatidyl ethanolamine
-
-
3beta,5alpha-17a-aza-D-homoandrostan-3-ol
-
-
5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
-
-
5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
-
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)
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
reversed by addition of dithiothreitol
5,5'-dithiobis-(2-nitrobenzoic acid)
-
substrate does not protect against inactivation
9-methoxy-1,2,5-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
-
-
A9145C
-
linear competitive
Borate
-
competitive
dioctylamine
-
-
N,N,N-trimethylhexadecan-1-aminium bromide
-
-
N-Butylmaleimide
-
-
N-decyl-N,N-dimethyldecan-1-aminium bromide
-
-
N-Heptylmaleimide
-
-
N-hexylhexan-1-amine
-
-
N-Hexylmaleimide
-
-
N-octyloctan-1-amine
-
-
N-Pentylmaleimide
-
-
NaCl
Eubacterium HX
-
1 M, 97% inhibition
oleoyl-CoA
-
above 0.05 M
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
phosphatidylcholine
-
-
S-adenosylhomocysteine
-
product inhibition
S-adenosylhomocysteine
-
-
Sinefungin
-
linear competitiove
sorbitol monolaurate ester
-
-
sorbitol monooleate ester
-
-
vinylfluorine
-
-
Hexadecyltrimethylammonium bromide
-
-
additional information
-
identification of new inhibitors of Escherichia coli cyclopropane fatty acid synthase using a colorimetric assay
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
bicarbonate
-
required. CFA synthase isolated and assayed in potassium bicarbonate buffer displayes more than 3-fold higher activity than in HEPES buffer
glycinebetaine
Eubacterium HX
-
activity is extremely low in vitro in 100 mM buffers, 100fold stimulation by exogenous addition of 2-3 M glycinebetaine
oleoyl-CoA
-
0.02-0.05 mM, enhances activity about 2fold
sodium lauryl sulfate
-
stimulates
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.53
-
phosphatidylethanolamine
-
-
0.057
-
S-adenosyl-L-methionine
-
-
0.07
-
S-adenosyl-L-methionine
-
37C, pH 8.0, wild-type enzyme
0.0705
-
S-adenosyl-L-methionine
-
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
-
37C, pH 8.0, mutant enzyme C139S
0.078
-
S-adenosyl-L-methionine
-
37C, pH 8.0, mutant enzyme H266A
0.08
-
S-adenosyl-L-methionine
-
37C, pH 7.4
0.08
-
S-adenosyl-L-methionine
-
-
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
0.02
-
S-adenosylmethionine
-
in cell-free extract
0.0564
-
Se-adenosyl-L-selenomethionine
-
-
0.74
-
Te-adenosyl-L-telluromethionine
-
-
additional information
-
additional information
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0025
-
S-adenosyl-L-methionine
-
37C, pH 8.0, mutant enzyme H266A
0.0142
-
S-adenosyl-L-methionine
-
37C, pH 8.0, mutant enzyme C139S
0.042
-
S-adenosyl-L-methionine
-
37C, pH 8.0, wild-type enzyme
0.067
-
S-adenosyl-L-methionine
-
37C, 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
0.217
-
Se-adenosyl-L-selenomethionine
-
-
0.06
-
Te-adenosyl-L-telluromethionine
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
-
37C, 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
1.1e-05
-
A9145C
-
-
0.001
-
A9145C
-
-
2.02
-
Borate
-
-
0.00013
-
dioctylamine
-
competitive inhibitor with respect to phospholipids
0.00026
-
dioctylamine
-
uncompetitive inhibitor with respect to S-adenosyl-L-methionine
0.037
-
N,N,N-trimethylhexadecan-1-aminium bromide
-
37C, pH 7.4
0.011
-
N-decyl-N,N-dimethyldecan-1-aminium bromide
-
37C, pH 7.4
0.01
-
N-hexylhexan-1-amine
-
37C, pH 7.4
0.004
-
N-octyloctan-1-amine
-
37C, pH 7.4
0.22
-
S-adenosylhomocysteine
-
-
0.0005
-
sinefugin
-
competitive inhibitor with respect to S-adenosyl-L-methionine
-
0.0072
-
sinefugin
-
non-competitive inhibitor with respect to the phospholipids
-
0.00022
-
Sinefungin
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
-
-
0.01
-
(1R,7aR)-hexahydro-1H-pyrrolizin-1-ylmethyl 4-hydroxy-3,5-dimethoxybenzoate
-
-
0.004
-
1,2,5-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
-
-
0.005
-
2,5,11-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
-
-
0.009
-
3beta,5alpha-17a-aza-D-homoandrostan-3-ol
-
-
0.01
-
5'-S-[2-(decylamino)ethyl]-5'-thioadenosine
-
-
0.001
-
9-methoxy-1,2,5-trimethyl-2,3,4,6-tetrahydro-1H-pyrido[4,3-b]carbazole
-
-
0.004
-
dioctylamine
-
-
0.009
-
Sinefungin
-
-
0.01
-
Sinefungin
-
37C, pH 7.4
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1.13e-06
-
-
-
additional information
-
-
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
8.5
-
about 50% of activity maximum at pH 5.5 and 8.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
increase in expression of CFA synthase at early stationary phase is due to the alternative sigma factor RpoS
Manually annotated by BRENDA team
-
isoform CPS3 shows highest transcription in leaf and flower
Manually annotated by BRENDA team
-
isoforms CPS1, 2 and 3 show high, intermediate and low levels, respectively, of transcripts in root
Manually annotated by BRENDA team
-
isoforms CPS1 and 2 are both expressed at low levels in seeds
Manually annotated by BRENDA team
-
isoforms CPS1, 2 and 3 show high, intermediate and low levels, respectively, of transcripts in stem
Manually annotated by BRENDA team
-
isoform CPS3 shows highest transcription in leaf and flower
Manually annotated by BRENDA team
additional information
-
no activity in leaves
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
loosely associated with the inner membrane
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
90000
-
-
equilibrium sedimentation, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 80000-100000, SDS-PAGE
?
-
x * 43913, calculation from nucleotide sequence
?
-
x * 98000, calculation from nucleotide sequence
monomer
-
1 * 90000, SDS-PAGE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
30 min, complete loss of activity in absence of lipid
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, in presence of phospholipid, stable for 2 months
-
-20C, pH 7.4, 20 mM phosphate buffer, 50% v/v glycerol, best storage conditions
-
-78C, 25% glycerol, less than 10% loss of activity after 6 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant His6-tagged protein
-
wild-type and six-histidine-tagged mutant enzymes H266A, Y317F, E239A, and E239Q
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
His-tagged recombinant protein
-
overproduced as a His6-tagged protein
-
overproduction of the enzyme via multicopy cfa plasmids
-
recombinantly expressed in Escherichia coli
-
expressed in yeast and Nicotiana tabacum BY2 cells
-
expressed in Escherichia coli strains YYC1273 and MG1655
-
fusion protein of an FAD-containing oxidase at the N-terminus and a methyltransferase at the C-terminus, expression in tobacco cells
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme expression is promoted by acid pH and high osmolarity
-
enzyme expression is promoted by acid pH and high osmolarity
Brucella abortus 2308 NalR
-
-
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
-
CPS gene transcript levels increase with seed development
-
the level of cfa transcripts increases when cells are harvested in stationary phase and when cells are grown in the presence of ethanol or at low pH
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
C176S
-
150% of wild-type activity
C354S
-
63% of wild-type activity
E239A
-
catalytic efficiency is 0.2% of wild-type value
E239A
-
mutant shows 0.57% 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
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
I733T
-
the CPS2 mutant expresses only trace amounts of cyclopropane