Information on EC 2.7.7.41 - phosphatidate cytidylyltransferase

New: Word Map on EC 2.7.7.41
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


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

EC NUMBER
COMMENTARY hide
2.7.7.41
-
RECOMMENDED NAME
GeneOntology No.
phosphatidate cytidylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CTP + phosphatidate = diphosphate + CDP-diacylglycerol
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
CDP-diacylglycerol biosynthesis
-
-
CDP-diacylglycerol biosynthesis I
-
-
CDP-diacylglycerol biosynthesis II
-
-
CDP-diacylglycerol biosynthesis III
-
-
Glycerophospholipid metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
CTP:phosphatidate cytidylyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9067-83-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain Marburg
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Micrococcus cerificans
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain PCC6803
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme can substitute for the corresponding enzyme in Plasmodium knowlesi. Both the C-terminal cytidylyltransferase domain and the N-terminal extension are essential to Plasmodium spp.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CTP + 1,2-diarachidonoyl phosphatidic acid
diphosphate + CDP-1,2-diarachidonoylglycerol
show the reaction diagram
-
-
-
-
?
CTP + 1,2-dicaproyl phosphatidic acid
diphosphate + CDP-1,2-dicaproylglycerol
show the reaction diagram
-
-
-
-
?
CTP + 1,2-dioleoyl phosphatidic acid
diphosphate + CDP-dioleoylglycerol
show the reaction diagram
CTP + 1,2-dipalmitoyl phosphatidic acid
diphosphate + CDP-dipalmitoylglycerol
show the reaction diagram
CTP + 1,2-distearoyl phosphatidic acid
diphosphate + CDP-1,2-distearoylglycerol
show the reaction diagram
-
-
-
-
?
CTP + 1-arachidonoyl-2-stearoyl phosphatidic acid
diphosphate + CDP-1-arachidonoyl-2-stearoylglycerol
show the reaction diagram
-
-
-
-
?
CTP + 1-oleoyl-2-palmitoyl phosphatidic acid
diphosphate + CDP-1-oleoyl-2-palmitoylglycerol
show the reaction diagram
-
reaction with 1-oleoyl-2-palmitoyl phosphatidic acid at 83.4% of the activity with phosphatidic acid from egg phosphatidylcholine
-
-
?
CTP + 1-oleoyl-2-stearoyl phosphatidic acid
diphosphate + CDP-1-oleoyl-2-stearoylglycerol
show the reaction diagram
-
-
-
-
?
CTP + 1-palmitoyl-2-oleoyl phosphatidic acid
diphosphate + CDP-1-palmitoyl-2-oleoylglycerol
show the reaction diagram
CTP + 1-stearoyl-2-arachidonoyl phosphatidic acid
diphosphate + CDP-1-stearoyl-2-arachidonoylglycerol
show the reaction diagram
CTP + 1-stearoyl-2-oleoyl phosphatidic acid
diphosphate + CDP-1-stearoyl-2-oleoylglycerol
show the reaction diagram
-
-
-
-
?
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
show the reaction diagram
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
show the reaction diagram
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
show the reaction diagram
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
CTP + phosphatidate
diphosphate + CDP-diacylglycerol
show the reaction diagram
CTP + phosphatidate
diphosphate + CDPdiacylglycerol
show the reaction diagram
dCTP + phosphatidate
diphosphate + dCDPdiacylglycerol
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates at low concentrations, decrease in activity at higher concentrations
Co2+
-
activates at low concentrations, decrease in activity at higher concentrations
NH4+
Micrococcus cerificans
-
only about half of the activity observed with K+
Rb+
Micrococcus cerificans
-
only about half of the activity observed with K+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
-
-
Ca2+
-
2 mM, 45% inhibition, even in presence of optimal Mg2+ concentrations
cardiolipin
CDP-diacylglycerol
-
-
CDP-dipalmitin
-
inhibits diphosphorolysis of CDP-dipalmitin
CHAPS
-
at 0.3%
Co2+
-
2 mM, 58% inhibition, even in presence of optimal Mg2+ concentrations
deoxycholate
-
partial inhibition
diphosphate
FeSO4
-
2 mM, 97% inhibition, even in presence of optimal Mg2+ concentrations
hydrazine
Micrococcus cerificans
-
-
lysolecithin
-
1 mM, 89% inhibition
lysophosphatidylcholine
-
the solubilized but not the microsomal enzyme is strongly inhibited
NEM
-
-
oleic acid
-
2 mM, 84% inhibition
palmitic acid
-
2 mM, 76% inhibition
palmitoyl-CoA
phosphatidylethanolamine
-
2 mM, 16% inhibition
phosphatidylinositol
-
2 mM, 23% inhibition
phosphatidylinositol 4,5-bisphosphate
strong
phosphatidylserine
-
2 mM, 46% inhibition
Sodium deoxycholate
sodium lauryl sulfate
Micrococcus cerificans
-
-
Sulfram
Micrococcus cerificans
-
-
-
Thiophosphatidate
-
competitive
-
Triton X-100
Tween 20
ZWT-12
-
2 mM, 86% inhibition
-
ZWT-14
-
2 mM, 92% inhibition
-
additional information
-
no inhibition by 1.65 mM ADP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bovine serum albumin
-
activity is 6fold increased
-
cationic detergent
-
the phosphatidate must be emulsified in a cationic detergent for optimal activity
-
CHAPS
-
maximal activity at 0.5%
Cutsum
Micrococcus cerificans
-
enhances activity
-
ITP
-
stimulates only in presence of either lecithin or sphingomyelin
lecithin
-
stimulates
non-ionic detergent
Norfenfluramine
-
can partially replace the divalent cation requirement
phosphatidylcholine
-
the solubilized but not the microsomal enzyme is activated
sphingomyelin
-
stimulates
Triton X-100
UTP
-
stimulates only in presence of either lecithin or sphingomyelin
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.114
1,2-dioleoyl-sn-glycero-3-phosphate
pH 7.5, 30C
0.102
1-stearoyl-2-arachidonoyl-sn-glycero-3-phosphate
pH 7.5, 30C
0.17 - 1
CTP
0.26 - 0.9
dCTP
0.5 - 2.5
phosphatidate
0.08 - 0.3
phosphatidic acid
additional information
additional information
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8.92
CTP
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.24
CDP
-
pH 7.2, 37C
5.6
CMP
-
pH 7.5, 25C
0.48 - 0.59
CTP
0.75
dCTP
1.5
diphosphate
-
pH 7.2, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00011
-
-
0.1333
Micrococcus cerificans
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
Micrococcus cerificans
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8 - 7.6
-
pH 5.8: 60% of maximal activity, pH 7.6: about 55% of maximal activity
6 - 9.3
Micrococcus cerificans
-
pH 6.0: about 45% of maximal activity, pH 9.3: about 40% of maximal activity
6 - 8.5
-
pH 6.0: 70% of maximal activity, pH 8.5: about 70% of maximal activity
6.2 - 8.7
-
pH 6.2: 54% of maximal activity, pH 8.7: 56% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
Micrococcus cerificans
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
-
20C: about 35% of maximal activity, 60C: about 45% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
calculated from the deduced amino acid sequence
7.57
-
calculated from nucleotide sequence
7.62
calculated from the deduced amino acid sequence
9.62
calculated from nucleotide sequence for full-length enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
embryonic heart myoblastic cells, cells grown in cell culture and treated with ethyl-p-chlorophenoxyisobutyrate (clofibrate), no effect of clofibrate on enzyme activity
Manually annotated by BRENDA team
inner segment of
Manually annotated by BRENDA team
expressed in photoreceptors but not in other layers of the retina; ganglion cell layer and inner nuclear layer, not expressed in photoreceptors
Manually annotated by BRENDA team
the enzyme is only weakly transcribed in ring stages, while major transcription occurs in the trophozoite and schizont stages
Manually annotated by BRENDA team
the enzyme is only weakly transcribed in ring stages, while major transcription occurs in the trophozoite and schizont stages
Manually annotated by BRENDA team
-
low activity
Manually annotated by BRENDA team
the enzyme is only weakly transcribed in ring stages, while major transcription occurs in the trophozoite and schizont stages
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
peripheral membrane protein that is trafficked outside the parasite to the parasitophorous vacuole
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
114000
400000
-
approximately, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
stability is good at pH 7 and dropps rapidly above
643314
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
24 h, enzyme in extract from microsomal membranes loses 50% of its activity
30
-
20 min, labile above
40
-
with detergent already inactivated at
55
Micrococcus cerificans
-
30 min, irreversible inactivation
57
-
30 min, no loss of activity of membrane-bound enzyme, 70% loss of activity of partially purified enzyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, enzyme is very unstable when the disrupted lymphocyte homogenate or the isolated microsomes are stored, 75% loss of activity after 24 h. Stable for at least 1 month if stored in intact lymphocytes
-
solubilized enzyme is stable to freezing and thawing
-
stable to at least 2 cycles of freezing and thawing
the pure enzyme can be dialyzed, but to maintain activity the dialyzing buffer must contain 1% n-octyl-beta-D-glucopyranoside, 0.25 mM dithiothreitol and at least 200 mM salt
-
the solubilized protein is quite labile. Its stability is markedly enhanced by exchange dialysis against 10% glycerol, 20% propylene glycol, 25 mM cacodylate buffer, pH 6.5, 10 mM MgCl2
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 24 h, enzyme in isolated microsomes, 75% loss of activity
-
-70C, solubilized enzyme is stable for at least several months
-
-72C, the enzyme extract from microsomal membranes is indefinitely stable
-
-80C, cell envelope preparations stable for at least 2 months
-
-80C, in presence of 1 mM CTP the purified enzyme is 90-100% stable for at least 3 months
-
0-4C, solubilized enzyme is stable for at least several weeks
-
4C, the enzyme extract from microsomal membranes is stable for at least 24 h
-
purified enzyme can be stored frozen for months if quick-frozen in liquid nitrogen
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
mitochondrial enzyme
-
partial
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as GFP-fusion protein
-
expressed in CHO-1 cells; expressed in CHO-1 cells
expression in COS cells
expression in Escherichia coli. Fusion protein of glutathione S-transferase and residues 108 to 424 of the Solanum tuberosum enzyme is produced by Escherichia coli cells transformed with the isopropyl-beta-galactopyranoside inducible plasmid pGEXstCD1
-
expression under the control of a GAL1 promoter in a null cds1 mutant yeast strain complements its growth defect and produces enzyme activity when induced with galactose
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the 78 kDa predicted protein is recovered as a 50 kDa conserved C-terminal cytidylyltransferase domain C-CDS and a 28 kDa fragment that corresponds to the long hydrophilic asparagine-rich N-terminal extension N-CDS. The two fragments are the processed forms of the 78 kDa pro-form that is encoded from a single transcript with no alternate translation start site for C-CDS
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C102Y
mutation is the molecular basis for the inositol excretion phenotype
additional information
-
the cdsA-inactivated PAL mutant strain lacks phycobilisomes
Show AA Sequence (11619 entries)
Longer loading times are possible. Please use the Sequence Search for a certain query.