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 hide
2.1.1.79
-
RECOMMENDED NAME
GeneOntology No.
cyclopropane-fatty-acyl-phospholipid synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cyclopropane fatty acid (CFA) biosynthesis
-
-
lipid metabolism
-
-
mycolate biosynthesis
-
-
sterculate 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).
CAS REGISTRY NUMBER
COMMENTARY hide
51845-48-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
Brucella abortus 2308 NalR
-
-
-
Manually annotated by BRENDA team
Eubacterium HX
moderately-halophilic
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Lactobacillus reuteri ATCC PTA 6475
-
-
-
Manually annotated by BRENDA team
strain MG1363
-
-
Manually annotated by BRENDA team
strain MG1363
-
-
Manually annotated by BRENDA team
clone JPCM5 MCAN/ES/98/LLM-877
-
-
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
strain RmP110
-
-
Manually annotated by BRENDA team
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
S-adenosyl-L-homocysteine + phosphatidylcholine
S-adenosyl-L-homocysteine + ?
show the reaction diagram
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 + oleic acid
S-adenosyl-L-homocysteine + dihydrosterculic acid
show the reaction diagram
S-adenosyl-L-methionine + phosphatidylcholine
?
show the reaction diagram
-
the enzyme acts primarily on the sn-1 position of + phosphatidylcholine
-
-
?
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 + phospholipids
S-adenosyl-L-homocysteine + phospholipid + cyclopropane fatty acid
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + triacylglycerol
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + vaccenic acid
S-adenosyl-L-homocysteine + lactobacillic acid
show the reaction diagram
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
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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
COMMENTARY hide
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
5,5'-dithiobis(2-nitrobenzoic acid)
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
Borate
-
competitive
dioctylamine
-
-
Hexadecyltrimethylammonium bromide
-
-
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
phosphatidylcholine
-
-
S-adenosylhomocysteine
sinefungin
sorbitol monolaurate ester
-
-
sorbitol monooleate ester
-
-
vinylfluorine
-
-
additional information
-
identification of new inhibitors of Escherichia coli cyclopropane fatty acid synthase using a colorimetric assay
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53
phosphatidylethanolamine
-
-
0.057 - 2.6
S-adenosyl-L-methionine
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025 - 100
S-adenosyl-L-methionine
0.217
Se-adenosyl-L-selenomethionine
Escherichia coli
-
-
0.06
Te-adenosyl-L-telluromethionine
Escherichia coli
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
0.000011 - 0.001
A9145C
2.02
Borate
-
-
0.00013 - 0.00026
dioctylamine
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 - 0.0072
sinefugin
0.00022
sinefungin
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
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 - 0.01
sinefungin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000113
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 8.5
-
about 50% of activity maximum at pH 5.5 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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, 2 and 3 show high, intermediate and low levels, respectively, of transcripts in stem
Manually annotated by BRENDA team
additional information
-
no activity in leaves
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
during the early log phase of extracellular growth, the enzyme shows partial localisation to the endoplasmic reticulum
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90000
-
equilibrium sedimentation, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 90000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
30 min, complete loss of activity in absence of lipid
GENERAL STABILITY
ORGANISM
UNIPROT
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
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
LITERATURE
Ni-NTA agarose column chromatography
-
partial
recombinant His6-tagged protein
-
wild-type and six-histidine-tagged mutant enzymes H266A, Y317F, E239A, and E239Q
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana
-
expressed in Escherichia coli strains YYC1273 and MG1655
-
expressed in Lactococcus lactis subsp. cremoris strain MG1363 and Escherichia coli BL21(DE3) cells
-
expressed in yeast and Nicotiana tabacum BY2 cells
-
fusion protein of an FAD-containing oxidase at the N-terminus and a methyltransferase at the C-terminus, expression in tobacco cells
-
His-tagged recombinant protein
-
mutant enzyme G236E os 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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
enzyme expression is promoted by acid pH and high osmolarity
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
COMMENTARY hide
LITERATURE
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
I733T
-
the CPS2 mutant expresses only trace amounts of cyclopropane
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