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Urea, synthesis

Mono-substituted and unsymmetrical di-substituted ureas may be prepared by a modification of Wohler s urea synthesis, salts of primary or secondary amines being used instead of the ammonium salt for interaction with potassium cyanate. Thus when an aqueous solution containing both aniline hydrochloride and potassium cyanate is heated, aniline cyanate is first formed, and then C,HjNH,HCl -h KCNO = C,H6NHj,HCNO -h KCl C,HsNH HCNO = C.H NHCONH, by the usual molecular rearrangement is converted into monophenyburea. [Pg.124]

All defects in urea synthesis result in ammonia intoxication. Intoxication is more severe when the metabolic block occurs at reactions 1 or 2 since some covalent linking of ammonia to carbon has already occurred if citrulline can be synthesized. Clinical symptoms common to all urea cycle disorders include vomiting, avoidance of high-protein foods, intermittent ataxia, irritability, lethargy, and mental retardation. The clinical features and treatment of all five disorders discussed below are similar. Significant improvement and minimization of brain damage accompany a low-protein diet ingested as frequent small meals to avoid sudden increases in blood ammonia levels. [Pg.247]

Glutamine synthase converts NH3 to nontoxic glutamine. Glutaminase releases NH3 for use in urea synthesis. [Pg.248]

Hepatic urea synthesis takes place in part in the mitochondrial matrix and in part in the cytosol. Inborn errors of metabolism are associated with each reaction of the urea cycle. [Pg.248]

Figure 34-7 summarizes the roles of the intermediates and enzymes of pyrimidine nucleotide biosynthesis. The catalyst for the initial reaction is cytosolic carbamoyl phosphate synthase II, a different enzyme from the mitochondrial carbamoyl phosphate synthase I of urea synthesis (Figure 29-9). Compartmentation thus provides two independent pools of carbamoyl phosphate. PRPP, an early participant in purine nucleotide synthesis (Figure 34-2), is a much later participant in pyrimidine biosynthesis. Figure 34-7 summarizes the roles of the intermediates and enzymes of pyrimidine nucleotide biosynthesis. The catalyst for the initial reaction is cytosolic carbamoyl phosphate synthase II, a different enzyme from the mitochondrial carbamoyl phosphate synthase I of urea synthesis (Figure 29-9). Compartmentation thus provides two independent pools of carbamoyl phosphate. PRPP, an early participant in purine nucleotide synthesis (Figure 34-2), is a much later participant in pyrimidine biosynthesis.
Brusilow, S., Tinker, J. and Batshaw, M. L. Amino acid acylation A mechanism of nitrogen excretion in inborn errors of urea synthesis. Science 207 659,1980. [Pg.683]

SNAM (1) [Societa Nazionale Metandotti] A urea synthesis process, developed in the late 1960s and now widely used worldwide. [Pg.248]

Only a minor amount of chlorinated copper phthalocyanine, for instance, especially in the 4-position of the copper phthalocyanine molecule, prevents a change of modification from a to (3. Approximately 3 to 4% chlorine is commonly used, which corresponds to the formula CuPc-Cl0.5, also referred to as semi-chloro-CuPc . The phthalic anhydride/urea synthesis, for instance, affords a partially chlorinated product if 4-chlorophthalic anhydride is added to the reaction mixture. Copper chlorides in the phthalonitrile process have the same effect. [Pg.434]

It was not until 1933 after Krebs had decided to leave Freiburg that he formulated urea synthesis in its now common cycle form ... [Pg.106]

In addition to the common pathways, glycolysis and the TCA cycle, the liver is involved with the pentose phosphate pathway regulation of blood glucose concentration via glycogen turnover and gluconeogenesis interconversion of monosaccharides lipid syntheses lipoprotein formation ketogenesis bile acid and bile salt formation phase I and phase II reactions for detoxification of waste compounds haem synthesis and degradation synthesis of non-essential amino acids and urea synthesis. [Pg.171]

Urea synthesis Liver Part cytosolic and part mitochondrial 6.2.1... [Pg.321]

This enzyme is found in many tissues, where it catalyzes the reversible oxidative deamination of the amino acid glutamate. It produces the citric acid cycle intermediate a-ketoglutarate, which serves as an entry point to the cycle for a group of glucogenic amino adds. Its role in urea synthesis and nitrogen removal is stiU controversial, but has heen induded in Figure 1-17-1 and Table 1-17-1. [Pg.244]

Product formed by argiainosuccinate lyase during urea synthesis. [Pg.262]

The formation and excretion of urea is the primary mechanism by which excess nitrogen, in the form of ammonia, is removed from the body. Surprisingly, it was found that the actual rate of urea synthesis exceeded considerably the rate of excretion of the urea. The interesting question, therefore, is what is the fate of this lost urea The answer is that urea enters the large intestine, where it is degraded by microorganisms that possess the enzyme urease, which catalyses the reaction ... [Pg.177]


See other pages where Urea, synthesis is mentioned: [Pg.76]    [Pg.120]    [Pg.14]    [Pg.245]    [Pg.247]    [Pg.247]    [Pg.250]    [Pg.1020]    [Pg.96]    [Pg.29]    [Pg.162]    [Pg.5]    [Pg.177]    [Pg.177]    [Pg.178]    [Pg.178]    [Pg.199]    [Pg.243]    [Pg.246]    [Pg.273]   
See also in sourсe #XX -- [ Pg.233 , Pg.234 , Pg.235 , Pg.236 , Pg.237 ]

See also in sourсe #XX -- [ Pg.595 , Pg.596 ]

See also in sourсe #XX -- [ Pg.595 , Pg.596 ]

See also in sourсe #XX -- [ Pg.845 , Pg.1162 , Pg.1163 ]

See also in sourсe #XX -- [ Pg.845 , Pg.1162 , Pg.1163 ]




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