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6.3.4.16: carbamoyl-phosphate synthase (ammonia)

This is an abbreviated version!
For detailed information about carbamoyl-phosphate synthase (ammonia), go to the full flat file.

Word Map on EC 6.3.4.16

Reaction

2 ATP +

NH3
+
hydrogencarbonate
=
2 ADP
+
phosphate
+
Carbamoyl phosphate

Synonyms

arginine-specific CPS, CarB, carbamate kinase-like carbamoyl phosphate synthetase, carbamate kinase-like carbamoyl-phosphate synthetase, carbamoyl phosphate synthase-1, carbamoyl phosphate synthetase, carbamoyl phosphate synthetase 1, carbamoyl phosphate synthetase I, carbamoyl phosphate synthetase-1, carbamoyl-phosphate synthetase, carbamoyl-phosphate synthetase 1, Carbamoyl-phosphate synthetase I, Carbamoylphosphate synthase, Carbamoylphosphate synthase (ammonia), Carbamoylphosphate synthetase, Carbamoylphosphate synthetase (ammonia), Carbamoylphosphate synthetase I, carbamoylphosphate synthetase-I, Carbamyl phosphate synthase I, carbamyl phosphate synthetase I, carbamyl-phosphate synthetase I, Carbamylphosphate synthetase, carbamylphosphate synthetase 1, Carbamylphosphate synthetase I, carbmoylphosphate synthetase, Carbon-dioxide-ammonia ligase, Carbonate kinase (phosphorylating), CK-like CPS, CPS, CPS 1, CPS I, CPS I-like (ammonia- and N-acetyl-L-glutamate-dependent), CPS-1, CPS-I, CPS1, CPSase, CPSase I, CPSI, EC 2.7.2.5, mitochondrial carbamoylphosphate synthetase I, MS-s, Msm_0361, p165, urea-specific CPS

ECTree

     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.16 carbamoyl-phosphate synthase (ammonia)

General Stability

General Stability on EC 6.3.4.16 - carbamoyl-phosphate synthase (ammonia)

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
acetylglutamate ATP accelerates the oxidative inactivation by mixtures of Fe3+, ascorbate, and O2
-
elastase inactivates. Addition of ATP, Mg2+, K+ and N-acetyl-L-glutamate protects entirely
-
elastase inactivates. Addition of ATP, Mg2+, K+ and N-acetyl-L-glutamate protects entirely. Acetylglutamate alone speeds inactivation
-
glycerol and DTT stabilize during purification
-
inactivated by the Fe3+-oxygen-ascorbate model system for mixed-function oxidation. The susceptibility is markedly increased by acetylglutamate, when ATP is absent. ATP, and even more a mixture of ATP and bicarbonate protect from inactivation
-
no inactivation by elastase
Frog
-
stabilty under pressure, progressive inactivation down to 50% of initial activity at 200 MPa, this residual activity is constant at 200 MPa for at least 50 min
-
trypsin, chymotrypsin, and papain also hydrolyze the oxidized enzyme considerybly faster than the native enzyme
-