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

BRENDA support

Literature summary for 2.7.7.14 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
Search for more literature for 2.7.7.14

Protein Variants

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

KM Value [mM]

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

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Homo sapiens Q99447
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
ECT
-
 Homo sapiens
Pcyt2
-
 Homo sapiens

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Range

pH Minimum pH Maximum Comment Organism
7.2 9
-
 Homo sapiens

General Information

General Information Comment Organism
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