Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.15 extracted from

  • Ding, Z.; Taneva, S.G.; Huang, H.K.; Campbell, S.A.; Semenec, L.; Chen, N.; Cornell, R.B.
    A 22-mer segment in the structurally pliable regulatory domain of metazoan CTP:phosphocholine cytidylyltransferase facilitates both silencing and activating functions (2012), J. Biol. Chem., 287, 38980-38991.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.15

Protein Variants

Protein Variants Comment Organism
additional information 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 Caenorhabditis elegans
additional information 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 Drosophila melanogaster
additional information creation of a chimeric enzyme by fusing the catalytic domain of Rattus norvegicus CCTalpha to the regulatory tail of CCT from Saccharomyces cerevisiae Saccharomyces cerevisiae
additional information 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 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans
-
-
-
Drosophila melanogaster
-
-
-
Rattus norvegicus
-
-
-
Saccharomyces cerevisiae
-
-
-

Subunits

Subunits Comment Organism
More the enzyme is composed of a catalytic head domain and a regulatory tail Drosophila melanogaster
More the enzyme is composed of a catalytic head domain and a regulatory tail Rattus norvegicus
More the enzyme is composed of a catalytic head domain and a regulatory tail Saccharomyces cerevisiae
More the enzyme is composed of a catalytic head domain and a regulatory tail Caenorhabditis elegans

Synonyms

Synonyms Comment Organism
CCT
-
 Drosophila melanogaster
CCT
-
 Rattus norvegicus
CCT
-
 Saccharomyces cerevisiae
CCT
-
 Caenorhabditis elegans
CTP:phosphocholine cytidylyltransferase
-
 Drosophila melanogaster
CTP:phosphocholine cytidylyltransferase
-
 Rattus norvegicus
CTP:phosphocholine cytidylyltransferase
-
 Saccharomyces cerevisiae
CTP:phosphocholine cytidylyltransferase
-
 Caenorhabditis elegans

General Information

General Information Comment Organism
additional information the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding Rattus norvegicus
additional information the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan Drosophila melanogaster
additional information the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan Saccharomyces cerevisiae
additional information the enzyme is composed of a catalytic head domain and a regulatory tail, the latter is composed of a long membrane lipid-inducible amphipathic helix, followed by a highly disordered segment. The tail region has dual functions as a regulator of membrane binding/enzyme activation and as an inhibitor of catalysis in the unbound form of the enzyme, suggesting conformational plasticity. Full activation of CCTmay require not only loss of a silencing conformation in the membrane-inducible amphipathic helix but a gain of an activating conformation, promoted by membrane binding. The conserved 22-residue segment in domain M contributes to both silencing and membrane binding/activation of metazoan Caenorhabditis elegans
physiological function CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis Drosophila melanogaster
physiological function CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis Rattus norvegicus
physiological function CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis Saccharomyces cerevisiae
physiological function CTP:phosphocholine cytidylyltransferase is an amphitropic enzyme that regulates phosphatidylcholine synthesis Caenorhabditis elegans