The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions that produces urea (NH2)2CO from ammonia (NH3). Animals that use this cycle, mainly amphibians and mammals, are called ureotelic.
Putrescine is an organic compound with the formula (CH2)4(NH2)2. It is a colorless solid that melts near room temperature. It is classified as a diamine. Together with cadaverine, it is largely responsible for the foul odor of putrefying flesh, but also contributes to other unpleasant odors.
Aspartate carbamoyltransferase catalyzes the first step in the pyrimidine biosynthetic pathway.
A transferase is any one of a class of enzymes that catalyse the transfer of specific functional groups from one molecule to another. They are involved in hundreds of different biochemical pathways throughout biology, and are integral to some of life's most important processes.
Spermine is a polyamine involved in cellular metabolism that is found in all eukaryotic cells. The precursor for synthesis of spermine is the amino acid ornithine. It is an essential growth factor in some bacteria as well. It is found as a polycation at physiological pH. Spermine is associated with nucleic acids and is thought to stabilize helical structure, particularly in viruses. It functions as an intracellular free radical scavenger to protect DNA from free radical attack. Spermine is the chemical primarily responsible for the characteristic odor of semen.
N-Acetylglutamate synthase (NAGS) is an enzyme that catalyses the production of N-acetylglutamate (NAG) from glutamate and acetyl-CoA.
Carbamoyl phosphate synthetase I is a ligase enzyme located in the mitochondria involved in the production of urea. Carbamoyl phosphate synthetase I transfers an ammonia molecule to a molecule of bicarbonate that has been phosphorylated by a molecule of ATP. The resulting carbamate is then phosphorylated with another molecule of ATP. The resulting molecule of carbamoyl phosphate leaves the enzyme.
N-Acetylglutamate synthase deficiency is an autosomal recessive urea cycle disorder.
Carbamoyl phosphate synthetase catalyzes the ATP-dependent synthesis of carbamoyl phosphate from glutamine or ammonia and bicarbonate. This enzyme catalyzes the reaction of ATP and bicarbonate to produce carboxy phosphate and ADP. Carboxy phosphate reacts with ammonia to give carbamic acid. In turn, carbamic acid reacts with a second ATP to give carbamoyl phosphate plus ADP.
Carbamoyl phosphate synthetase (glutamine-hydrolysing) is an enzyme that catalyzes the reactions that produce carbamoyl phosphate in the cytosol. Its systemic name is hydrogen-carbonate:L-glutamine amido-ligase .
In enzymology, a putrescine N-methyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a 3-hydroxymethylcephem carbamoyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a lysine carbamoyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, a N-acetylornithine carbamoyltransferase (EC 2.1.3.9) is an enzyme that catalyzes the chemical reaction
In enzymology, an oxamate carbamoyltransferase is an enzyme that catalyzes the chemical reaction
In enzymology, an agmatinase (EC 3.5.3.11) is an enzyme that catalyzes the chemical reaction
In enzymology, an agmatine deiminase (EC 3.5.3.12) is an enzyme that catalyzes the chemical reaction
In enzymology, a carbamate kinase (EC 2.7.2.2) is an enzyme that catalyzes the chemical reaction
In molecular biology, the ATCase/OTCase family is a protein family which contains two related enzymes: aspartate carbamoyltransferase EC 2.1.3.2 and ornithine carbamoyltransferase EC 2.1.3.3. It has been shown that these enzymes are evolutionary related. The predicted secondary structure of both enzymes is similar and there are some regions of sequence similarities. One of these regions includes three residues which have been shown, by crystallographic studies to be implicated in binding the phosphoryl group of carbamoyl phosphate and may also play a role in trimerisation of the molecules. The N-terminal domain is the carbamoyl phosphate binding domain. The C-terminal domain is an aspartate/ornithine-binding domain.
N-succinylornithine carbamoyltransferase (EC 2.1.3.11, succinylornithine transcarbamylase, N-succinyl-L-ornithine transcarbamylase, SOTCase) is an enzyme with systematic name carbamoyl phosphate:N2-succinyl-L-ornithine carbamoyltransferase. This enzyme catalyses the following chemical reaction
