2.7.7.15: choline-phosphate cytidylyltransferase
This is an abbreviated version!
For detailed information about choline-phosphate cytidylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.15
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2.7.7.15
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phosphatidylcholine
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phospholipid
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phosphatidylethanolamine
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surfactant
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fetal
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diacylglycerol
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phospholipase
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ptdcho
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alveolar
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cholinephosphotransferase
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oleate
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phosphatidylglycerol
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amphipathic
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membrane-binding
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n-methyltransferase
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disaturated
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lysophosphatidylcholine
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phosphatidate
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3hcholine
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vance
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kennedy
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cytidyltransferase
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1,2-diacylglycerols
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phosphoethanolamine
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3hglycerol
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amphitropic
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l-forms
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methyl-14ccholine
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hexadecylphosphocholine
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analysis
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diagnostics
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choline-deficient
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cdpcholine
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methyl-3hcholine
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2.7.8.2
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14ccholine
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ctp:phosphoethanolamine
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choline-containing
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cdp-ethanolamine
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medicine
- 2.7.7.15
- phosphatidylcholine
- phospholipid
- phosphatidylethanolamine
- surfactant
- fetal
- diacylglycerol
- phospholipase
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ptdcho
- alveolar
-
cholinephosphotransferase
- oleate
- phosphatidylglycerol
-
amphipathic
-
membrane-binding
- n-methyltransferase
-
disaturated
- lysophosphatidylcholine
- phosphatidate
-
3hcholine
-
vance
-
kennedy
-
cytidyltransferase
- 1,2-diacylglycerols
- phosphoethanolamine
-
3hglycerol
-
amphitropic
-
l-forms
-
methyl-14ccholine
- hexadecylphosphocholine
- analysis
- diagnostics
-
choline-deficient
- cdpcholine
-
methyl-3hcholine
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2.7.8.2
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14ccholine
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ctp:phosphoethanolamine
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choline-containing
- cdp-ethanolamine
- medicine
Reaction
Synonyms
AtCCT1, CCT, CCT-alpha, CCT1, CCT2, CCTalpha, CCTalpha236, CCTbeta, CCTbeta2, CCTbeta3, CDP-choline pyrophosphorylase, CDP-choline synthetase, choline phosphate cytidylyltransferase, choline-phosphate cytidylyltransferase A, choline-phosphate cytidylyltransferase-alpha, cholinephosphate cytidylyltransferase, CpCCT1, cpcT, CTalpha, CTbeta2, CTP-phosphocholine cytidylyltransferase, CTP:cholinephosphate cytidylyltransferase, CTP:phosphocholine cytidylyltransferase, CTP:phosphocholine cytidylyltransferase alpha, CTP:phosphocholine cytidylyltransferase alpha-isoform, CTP:phosphocholine cytidylyltransferase beta2, CTP:phosphocholine cytidylyltransferase beta3, CTP:phosphocholine cytidylyltransferase CCT, CTP:phosphocholine cytidylyltransferase-alpha, CTP:phosphocholine cytidylyltransferase-beta2, CTP:phosphocholine cytidylyltranspherase alpha, CTP:phosphorylcholine cytidylyltransferase, CTP:phosphorylcholine cytidylyltransferase CCT1, CTP:phosphorylcholine cytidylyltransferase CCT2, cytidine diphosphocholine pyrophosphorylase, cytidylyltransferase, cytidylyltransferase, choline phosphate, LmjF.18.1330, More, PCYT1A, PF3D7_1316600, PfCCT, phosphocholine cytidylyltransferase, phosphocholine cytidylyltransferase alpha, phosphorylcholine cytidylyltransferase, phosphorylcholine transferase, phosphorylcholine:CTP cytidylyltransferase
ECTree
2.7.7.15 choline-phosphate cytidylyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.7.15 - choline-phosphate cytidylyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L246S/W249S/I256S/I257S
part of a putative amphipathic alpha helix
A93T
moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes retinal dystrophy
A99T
moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia
A99V
moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia
E129K
moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia
E280del
a single amino acid deletion in the autoinhibitory helix increases the constitutive (lipid-independent) enzyme activity x024fold. E280del enhances the response of the enzyme to anionic lipid vesicles 4fold. Mutation causes lipodystrophy in heterozygous status. Mutation causes lipodystrophy
F191L
severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia
P150A
missense variant in the catalytic domain, low solubility linked to reduced activity in cell lysates, consistent with aberrant folding and aggregation. Mutation causes spondylometaphyseal dysplasia with cone-rod dystrophy
R223S
mutation in a signal-transducing linker between the catalytic and membrane-binding domains, impaired enzymatic activity without fold-destabilization. Mutation causes spondylometaphyseal dysplasia
R283stop
severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia
S114T
severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia
S333L.fs164
severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes lipodystrophy
V142M
missense variant in the catalytic domain, low solubility linked to reduced activity in cell lysates, consistent with aberrant folding and aggregation. Mutation causes lipodystrophy in heterozygous status
K238R/K239R/Y240F
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increased resistance to calpain cleavage, resistance to enzyme degradation by oxidized low density lipoprotein
Q243A
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the mutation results in loss of calmodulin binding and leads to complete calpain resistance in vitro and in vivo
H630N
mutation diminishes the catalytic rate constant of the enzyme
H89A
H89G
H89N
H89Q
H92A
H92G
H92N
H92Q
K122A
R196K
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decreased Vmax, 5fold increased Km for phosphorylcholine, 23fold increased Km for CTP
additional information
additional information
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mutants truncated after amino acids 225 or 245 are active in the absence of lipids and not further activated in the presence of lipids, mutants truncated after amino acids 226, 281 or 319 are activated by lipid similar to wild-type enzyme
additional information
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creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Caenorhabditis elegans, the tail domain of the invertebrate CCT is competent for both suppression of catalytic activity and for activation by lipid vesicles
additional information
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creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Drosophila melanogaster, the tail domain of the invertebrate CCT is competent for both suppression of catalytic activity and for activation by lipid vesicles
additional information
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deletion of CCTalpha beginning at embryonic day 7.5 does not restrict lung development but results in severe respiratory failure at birth
additional information
loss of the CCTbeta2 isoform expression in mice results in gonadal dysfunction
additional information
loss of the CCTbeta2 isoform expression in mice results in gonadal dysfunction
additional information
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deletion of 55 C-terminal amino acids has no effect on enzyme activity, deletion of 139 C-terminal amino acids results in 90% decrease of enzyme activity
additional information
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deletion mutant lacking the putative membrane binding domain
additional information
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DELTA delta257-367 exhibits significantly lower specific activity and can not be activated by lipid, deletion mutant DELTA231-367 can not be activated by lipid
additional information
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deletion mutant which is truncated after residue 236, called CCTalpha236, independent of lipids, 50fold increase in activity
additional information
deletion construct 1-236 (lacks the regulatory domain, displays constitutive activity)
additional information
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creation of chimeric enzymes by fusing the catalytic domain of rat CCTalpha to the regulatory tail of CCTs from Drosophila melanogaster, Caenorhabditis elegans, or Saccharomyces cerevisiae or to alpha-synuclein. Deletion of the a highly amphipathic 22-residue segment in the membrane-inducible amphipathic helix increased the lipid-independent Vmax by 10fold, equivalent to the effect of deleting the entire tail, and severely weakened membrane binding affinity, but membrane binding is required for additional increases in catalytic efficiency. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan
additional information
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construction of a truncated version of rat CCTalpha, CCTalpha236. The full length CCT requires activation via association with lipids and has been reported to have activity 50fold lower in the absence of lipids when compared to the activity of CCTalpha236
additional information
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creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Saccharomyces cerevisiae
