6.3.5.5: carbamoyl-phosphate synthase (glutamine-hydrolysing)

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For detailed information about carbamoyl-phosphate synthase (glutamine-hydrolysing), go to the full flat file.

Reaction

2 ATP +

Synonyms

CAD, CAD carbamoyl-phosphate synthetase, CAD protein, Carbamoyl phosphate synthase (glutamine), carbamoyl phosphate synthetase, Carbamoyl phosphate synthetase (glutamine-hydrolyzing), carbamoyl phosphate synthetase 1, carbamoyl phosphate synthetase II, carbamoyl phosphate synthetase III, carbamoyl-phosphate synthetase, Carbamoyl-phosphate synthetase (glutamine-hydrolysing), carbamoyl-phosphate synthetase 2, Carbamoylphosphate synthase, Carbamoylphosphate synthetase, Carbamoylphosphate synthetase II, Carbamyl phosphate synthetase (glutamine), Carbamyl phosphate sythetase II, carbamylphosphate synthetase - aspartate transcarbamylase, CPA2, CPS, CPS II (glutamine-dependent), CPS III, CPS III (glutamine- and N-acetyl-L-glutamine-dependent), CPS1, CPSase, CPSase type II, CPSase-A, CPSase-P, CPSII, EC 2.7.2.9, Glutamine-dependent carbamyl phosphate synthetase, glutamine-hydrolyzing CPSase, MGG_04503, More, MtCPSs1, MtCPSs2, Synthase, carbamoylphosphate (glutamine), Synthetase, carbamoylphosphate (glutamine-hydrolyzing)

ECTree

     6 Ligases

         6.3 Forming carbon-nitrogen bonds

             6.3.5 Carbon-nitrogen ligases with glutamine as amido-N-donor

                6.3.5.5 carbamoyl-phosphate synthase (glutamine-hydrolysing)

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Results	in table
66	Activating Compound
87162	AA Sequence
2	Application
1	CAS Registry Number
28	Cloned(Commentary)
22	Cofactor
8	Crystallization (Commentary)
76	Disease/ Diagnostics
3	Expression
9	General Information
2	General Stability
4	IC50 Value
100	Inhibitors
3	Ki Value [mM]
200	KM Value [mM]
14	Localization
21	Metals/Ions
43	Molecular Weight [Da]
56	Natural Substrates/ Products (Substrates)
490	Organism
1	Oxidation Stability
12	Pathway
91	PDB ID
17	pH Optimum
2	pH Range
1	pH Stability
5	Posttranslational Modification
209	Protein Variants
28	Purification (Commentary)
27	Reaction
3	Reaction Type
137	Reference
36	Source Tissue
17	Specific Activity [micromol/min/mg]
2	Storage Stability
219	Substrates and Products (Substrate)
46	Subunits
73	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
3	Temperature Stability [°C]
145	Turnover Number [1/s]

Crystallization

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Crystallization on EC 6.3.5.5 - carbamoyl-phosphate synthase (glutamine-hydrolysing)

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Escherichia coli

-

1749

C248D mutant of small subunit, crystals are grown at 4°C by batch from 8% poly(ethylene glycol) 8000, 0.65 M tetraethylammonium chloride, 0.5 mM MnCl2, 100 mM KCl, 1.5 mM ADP, 25 mM GEPES, pH 7.4, 0.5 mM L-Orn. The crystals belong to the space group P2(1)2(1)2(1) with unit cell dimensions of a = 151.1 A, b = 164.2 A, and c = 331.5A and one complete (alphabeta)4-heeterotetramer per asymmetric unit

Escherichia coli

-

663329

in presence of both IMP and ornithine, structural analysis of the nucleotide monophosphate allosteric binding site for enzyme

Escherichia coli

-

651937

molecular dynamics simulation. Carbamate, the product of the reaction involving ATP, bicarbonate, and ammonia, must be delivered from the site of formation to the site of utilization by traveling nearly 40 A within the enzyme. The tunnel is composed of three continuous water pockets and two narrow connecting parts, near residues A23 and G575. The two narrow parts render two free energy barriers of 6.7 and 8.4 kcal/mol, respectively. Three water pockets are filled with about 21, 9, and 9 waters, respectively, and the corresponding relative free energies of carbamate residing in these free energy minima are 5.8, 0, and 1.6 kcal/mol, respectively. The release of phosphate into solution at the site for the formation of carbamate allows the side chain of R306 to rotate toward E25, E383, and E604. This rotation is virtually prohibited by a barrier of at least 23 kcal/mol when phosphate remains bound. This conformational change not only opens the entrance of the tunnel but also shields the charge-charge repulsion from the three glutamate residues when carbamate passes through the tunnel

Escherichia coli

P00968

715279

the structure of enzyme cocrystallized in the presence of the 5’-adenylylimidodiphosphate, is determined to 2.1 A by X-ray crystallographic analysis, the three active sites of enzyme communicate via domain movements, the first example of such a domain movement is described

Escherichia coli

-

649886

the three active sites within the alpha,beta heterodimer are separated by a linear distance of nearly 100 A and are interconnected by two molecular tunnels

Escherichia coli

-

650927

X-ray crystallographic analysis, the three active sites on the protein are widely separated from one another

Escherichia coli

-

650798

X-ray crystallographic structure

Escherichia coli

-

649849