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Literature summary for 2.7.7.15 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
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Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
A93T moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes retinal dystrophy Homo sapiens
A99T moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia Homo sapiens
A99V moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia Homo sapiens
E129K moderate solubility, but impaired catalytic activity and thermal destabilization. Mutation causes spondylometaphyseal dysplasia Homo sapiens
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
F191L severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia Homo sapiens
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
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
R283stop severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia Homo sapiens
S114T severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes spondylometaphyseal dysplasia Homo sapiens
S333L.fs164 severely reduced expression levels, suggesting aggregation and potential degradation of misfolded protein. Mutation causes lipodystrophy Homo sapiens
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)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens P49585
-
-

Source Tissue

Source Tissue Comment Organism Textmining
fibroblast
-
 Homo sapiens
-

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Stability [°C]

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

General Information

General Information Comment Organism
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
metabolism CTP:phosphocholine cytidylyltransferase is the key regulatory enzyme in phosphatidylcholine synthesis Homo sapiens