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Literature summary extracted from

  • Hewagama, A.; Guy, H.I.; Vickrey, J.F.; Evans, D.R.
    Functional linkage between the glutaminase and synthetase domains of carbamoyl-phosphate synthetase. Role of serine 44 in carbamoyl-phosphate synthetase-aspartate carbamoyltransferase-dihydroorotase (CAD) (1999), J. Biol. Chem., 274, 28240-28245.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.3.5.5 S44A mutant of hybrid enzyme shows km value similar to the wild-type hybrid, the kcat values of glutamine and ATP are 14fold lower in comparison to wild-type hybrid, the functional linkage that coordinates the reactions on the glutaminase and carbamoyl-phosphate synthetase domains is lost as a result of mutation Mammalia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.5.5 additional information
-
 additional information
-
 Mammalia
6.3.5.5 0.111
-
 L-glutamine pH 7.4, 37°C, mutant hybrid enzyme Mammalia
6.3.5.5 0.114
-
 L-glutamine pH 7.4, 37°C, wild-type hybrid enzyme Mammalia
6.3.5.5 1.66
-
 ATP pH 7.4, 37°C, wild-type hybrid enzyme Mammalia
6.3.5.5 1.83
-
 ATP pH 7.4, 37°C, mutant hybrid enzyme Mammalia

Organism

EC Number Organism UniProt Comment Textmining
6.3.5.5 Escherichia coli
-
-
-
6.3.5.5 Mammalia
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.3.5.5 side-chain modification formation of a hybrid complex consisting of the mammalian glutaminase domain and the isolated Escherichia coli carbamoyl-phosphate synthetase domains, the steady state kinetic parameters of the hybrid are similar to those obtained for carbamoyl-phosphate synthase-aspartate carbamoyltransferase-dihydroorotase Mammalia

Reaction

EC Number Reaction Comment Organism Reaction ID
6.3.5.5 2 ATP + L-glutamine + hydrogencarbonate + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate the mammalian enzyme is part of carbamoyl-phosphate synthase-aspartate carbamoyltransferase-dihydroorotase, CAD, the carbamoyl phosphate synthesis requires the concerted action of the glutaminase and carbamoyl-phosphate synthetase domains of CAD Mammalia
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.5.5 2 ATP + L-Gln + HCO3-
-
 Mammalia 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
6.3.5.5 2 ATP + L-Gln + HCO3-
-
 Escherichia coli 2 ADP + phosphate + L-Glu + carbamoyl phosphate
-
 ?
6.3.5.5 2 ATP + NH4+ + HCO3-
-
 Mammalia 2 ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.5.5 2 ATP + NH4+ + HCO3-
-
 Escherichia coli 2 ADP + phosphate + carbamoyl phosphate
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.3.5.5 additional information
-
 additional information
-
 Mammalia
6.3.5.5 164
-
 ATP pH 7.4, 37°C, mutant hybrid enzyme Mammalia
6.3.5.5 193
-
 L-glutamine pH 7.4, 37°C, mutant hybrid enzyme Mammalia
6.3.5.5 2500
-
 ATP pH 7.4, 37°C, wild-type hybrid enzyme Mammalia
6.3.5.5 2660
-
 L-glutamine pH 7.4, 37°C, wild-type hybrid enzyme Mammalia