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Literature summary extracted from

  • Cornell, R.B.; Taneva, S.G.; Dennis, M.K.; Tse, R.; Dhillon, R.K.; Lee, J.
    Disease-linked mutations in the phosphatidylcholine regulatory enzyme CCTalpha impair enzymatic activity and fold stability (2019), J. Biol. Chem., 294, 1490-1501 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.15 expression in COS-1 cells, which have very low endogenous CTP:phosphocholine cytidylyltransferase activity Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.15 A93T moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes retinal dystrophy Homo sapiens
2.7.7.15 A99T moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia Homo sapiens
2.7.7.15 A99V moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia Homo sapiens
2.7.7.15 E129K moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia Homo sapiens
2.7.7.15 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 Homo sapiens
2.7.7.15 F191L severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia Homo sapiens
2.7.7.15 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 Homo sapiens
2.7.7.15 R223S mutation in a signal-transducing linker between the catalytic and membrane-binding domains, impaired enzymatic activity without fold-destabilization. Mutation causes spondylometaphyseal dysplasia Homo sapiens
2.7.7.15 R283stop severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia Homo sapiens
2.7.7.15 S114T severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia Homo sapiens
2.7.7.15 S333L.fs164 severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes lipodystrophy Homo sapiens
2.7.7.15 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 Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.15 CTP + phosphocholine Homo sapiens
-
 diphosphate + CDP-choline
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.15 Homo sapiens P49585
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.7.15 fibroblast
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.15 CTP + phosphocholine
-
 Homo sapiens diphosphate + CDP-choline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.15 CCTalpha
-
 Homo sapiens
2.7.7.15 CTP:phosphocholine cytidylyltransferase CCT
-
 Homo sapiens
2.7.7.15 PCYT1A
-
 Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.7.15 47.5
-
 Tm-value for mutant enzyme A99T Homo sapiens
2.7.7.15 48.7
-
 Tm-value for mutant enzyme E129K Homo sapiens
2.7.7.15 49.5
-
 Tm-value for mutant enzyme A93T Homo sapiens
2.7.7.15 50.3
-
 Tm-value for mutant enzyme A99V Homo sapiens
2.7.7.15 50.7
-
 Tm-value for mutant enzyme E280del Homo sapiens
2.7.7.15 54.5
-
 Tm-value for wild-type enzyme isolated from the particulate fraction after denaturation and renaturation Homo sapiens
2.7.7.15 55
-
 Tm-value for wild-type enzyme purified in native form from the soluble fraction of COS cells Homo sapiens
2.7.7.15 56.1
-
 Tm-value for mutant enzyme Y240H Homo sapiens
2.7.7.15 57.1
-
 Tm-value for mutant enzyme R223S Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.7.15 malfunction mutations in the gene encoding CTP:phosphocholine cytidylyltransferase (PCYT1A) cause three distinct pathologies in humans: lipodystrophy, spondylometaphyseal dysplasia with cone-rod dystrophy (SMD-CRD), and isolated retinal dystrophy Homo sapiens
2.7.7.15 metabolism CTP:phosphocholine cytidylyltransferase is the key regulatory enzyme in phosphatidylcholine synthesis Homo sapiens