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Literature summary for 6.3.4.2 extracted from

  • Zalkin, H.
    CTP synthetase (1985), Methods Enzymol., 113, 282-287.
    View publication on PubMed
Search for more literature for 6.3.4.2

Inhibitors

Inhibitors Comment Organism Structure
6-diazo-5-oxo-L-norleucine
-
 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli B / ATCC 11303
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.8 6.1
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UTP + glutamine maximal activity with NH4+ is at least 20% greater than with glutamine Escherichia coli ADP + phosphate + CTP + Glu
-
 ?
ATP + UTP + glutamine maximal activity with NH4+ is at least 20% greater than with glutamine Escherichia coli B / ATCC 11303 ADP + phosphate + CTP + Glu
-
 ?
ATP + UTP + NH4+
-
 Escherichia coli ADP + phosphate + CTP
-
 ?
ATP + UTP + NH4+
-
 Escherichia coli B / ATCC 11303 ADP + phosphate + CTP
-
 ?

Subunits

Subunits Comment Organism
dimer the enzyme is a dimer of 108000 Da, the dimer associates to form a tetramer in the presence of either ATP or UTP Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5 9.3 glutamine-dependent activity Escherichia coli
10.3 10.4 ammonia-dependent activity,maximal activity with NH4+ is at least 20% greater than with glutamine Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7 10 ammonia-dependent activity rises linearly from pH 7 to pH 10 Escherichia coli

pH Stability

pH Stability pH Stability Maximum Comment Organism
10.3 10.4 rapid denaturation at Escherichia coli