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Literature summary extracted from

  • Tian, S.; Ohtsuka, J.; Wang, S.; Nagata, K.; Tanokura, M.; Ohta, A.; Horiuchi, H.; Fukuda, R.
    Human CTP:phosphoethanolamine cytidylyltransferase: enzymatic properties and unequal catalytic roles of CTP-binding motifs in two cytidylyltransferase domains (2014), Biochem. Biophys. Res. Commun., 449, 26-31.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.14 H226A mutation in histidine residue in the HxGH motif of the C-terminal CT domain. Decrease in activity Homo sapiens
2.7.7.14 H229A mutation in histidine residue in the HxGH motif of the N-terminal CT domain. Activity similar to wild-type activity Homo sapiens
2.7.7.14 H35A mutation in histidine residue in the HxGH motif of the N-terminal CT domain. Complete loss of activity Homo sapiens
2.7.7.14 H38A mutation in histidine residue in the HxGH motif of the N-terminal CT domain. Strong decrease in activity Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.14 0.042
-
 CTP mutant H229A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.048
-
 CTP wild-type, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.074
-
 CTP mutant H38A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.111
-
 CTP mutant H226A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.179
-
 Ethanolamine phosphate wild-type, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.275
-
 Ethanolamine phosphate mutant H226A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.301
-
 Ethanolamine phosphate mutant H229A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.88
-
 Ethanolamine phosphate mutant H38A, pH 7.7, 37°C Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.14 Mg2+ required Homo sapiens
2.7.7.14 Mn2+ may partly substitute for Mg2+ Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.14 Homo sapiens Q99447
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.14 CTP + ethanolamine phosphate
-
 Homo sapiens CDP-ethanolamine + diphosphate
-
 ?
2.7.7.14 additional information catalytic reaction of ECT obeys Michaelis-Menten kinetics with respect to both CTP and phosphoethanolamine Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.14 ECT
-
 Homo sapiens
2.7.7.14 Pcyt2
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.7.14 37
-
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.7.14 0.015
-
 CTP mutant H38A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.016
-
 Ethanolamine phosphate mutant H38A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.19
-
 CTP mutant H226A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.2
-
 CTP mutant H229A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.23
-
 Ethanolamine phosphate mutant H226A, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.25
-
 CTP wild-type, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.25
-
 Ethanolamine phosphate wild-type, pH 7.7, 37°C Homo sapiens
2.7.7.14 0.26
-
 Ethanolamine phosphate mutant H229A, pH 7.7, 37°C Homo sapiens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.7.14 7.2 9
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.7.14 physiological function enzyme is composed of two tandem cytidylyltransferase domains. The histidines, especially the first histidine, in the CTP-binding motif HxGH in the N-terminal CT domain are critical for its catalytic activity in vitro, while those in the C-terminal CT domain are not. Overexpression of the wild-type mutants containing amino acid substitutions in the HxGH motif in the C-terminal CT domain suppresses the growth defect of the Saccharomyces cerevisiae mutant of ECT1 in the absence of a phosphatidylethanolamine supply via the decarboxylation of phosphatidylserine, but overexpression of ECT mutants of the N-terminal CT domain does not Homo sapiens