590-55-6

Basic information

• Product Name: Carbamoylphosphate
• Synonyms: Carbamoylphosphate;Carbamic acid, monoanhydride with phosphoric acid;Carbamyl Phosphate;Carbamic phosphoric anhydride;Carbamylphosphoric acid;Phosphoric acid carbamoyl ester;Phosphoric carbamic anhydride
• CAS NO: 590-55-6
• Molecular Formula: CH₄NO₅P
• Molecular Weight: 141.02
• Mol File: 590-55-6.mol
• Article Data: 1

Chemical Properties

• Boiling Point: 403.3°Cat760mmHg
• Flash Point: 197.7°C
• Appearance: /
• Density: 1.976g/cm³
• Vapor Pressure: 1.24E-07mmHg at 25°C
• Refractive Index: 1.526
• CAS DataBase Reference: Carbamoylphosphate(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamoylphosphate(590-55-6)
• EPA Substance Registry System: Carbamoylphosphate(590-55-6)

Safety Data

• Hazardous Substances Data: 590-55-6(Hazardous Substances Data)

Usage

General Description

Carbamoylphosphate is a key intermediate in the urea cycle, a metabolic pathway that occurs in the liver and it plays a crucial role in the removal of ammonia from the body. This molecule is formed from the reaction between ammonia, bicarbonate, and ATP, and the reaction is catalyzed by the enzyme carbamoylphosphate synthetase. Carbamoylphosphate is further utilized in the synthesis of citrulline, an amino acid that is also involved in the urea cycle. Overall, carbamoylphosphate is an essential compound in the regulation of ammonia levels in the body and in the metabolism of amino acids.

InChI:InChI=1/CH4NO5P/c2-1(3)7-8(4,5)6/h(H2,2,3)(H2,4,5,6)

Synthetic route

potassium hydrogencarbonate (298-14-6) → carbamoyl phosphate (590-55-6)

Conditions	Yield
With L-ornithine; L-glutamine; potassium chloride; ATP; magnesium chloride pH=7.6; Kinetics; Reagent/catalyst; aq. buffer; Enzymatic reaction;

sodium azide + carbamoyl phosphate (590-55-6) → carbamoyl azide (13125-56-9)

Conditions	Yield
In hydrogenchloride pH = 4 until 4.5; at room temp.; shaking with double volume of ether for 25 hs;	30%
In hydrogenchloride pH = 4 until 4.5; at room temp.; shaking with double volume of ether for 25 hs;	30%

carbamoyl phosphate (590-55-6) → carbon dioxide (124-38-9) + NH4+, H2PO4

Conditions	Yield
With aspartate transcarbamylase (ATCase) at 37℃; for 24h; Mechanism; other enzymes and in absence of enzyme;

carbamoyl phosphate (590-55-6) + N-{7-[(6-deoxy-5-C-methyl-4-O-methyl-α-L-lyxohexopyranosyl)oxy]-4-hydroxy-8-methyl-2-oxo-2H-1-benzopyran-3-yl}-4-hydroxy-3-(3-methyl-2-buten-1-yl)benzamide → novobiocin (303-81-1, 107781-69-1)

Conditions	Yield
With Streptomyces spheroides NovN enzyme; ATP; bovine serum albumin; magnesium chloride In water; dimethyl sulfoxide at 20℃; pH=9.0; Enzyme kinetics;

L-2,4-diaminobutyrate (1758-80-1) + carbamoyl phosphate (590-55-6) → L-2-amino-4-ureidobutyrate (1190-47-2)

Conditions	Yield
With N-carbamoyltransferase for 0.333333h; Enzymatic reaction;

Upstream product

• 298-14-6 potassium hydrogencarbonate 

Downstream Products

• 303-81-1 novobiocin 

Relevant articles and documents

Carbamate transport in carbamoyl phosphate synthetase: A theoretical and experimental investigation

The transport of carbamate through the large subunit of carbamoyl phosphate synthetase (CPS) from Escherichia coli was investigated by molecular dynamics and site-directed mutagenesis. 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. Potentials of mean force (PMF) calculations along the entire tunnel for the translocation of carbamate indicate that the tunnel is composed of three continuous water pockets and two narrow connecting parts, near Ala-23 and Gly-575. The two narrow parts render two free energy barriers of 6.7 and 8.4 kcal/mol, respectively. Three water pockets were 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 Arg-306 to rotate toward Glu-25, Glu-383, and Glu-604. 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. Two mutants, A23F and G575F, were designed to block the migration of carbamate through the narrowest parts of the carbamate tunnel. The mutants retained only 1.7% and 3.8% of the catalytic activity for the synthesis of carbamoyl phosphate relative to the wild type CPS, respectively.