also at this step, N-acetylglutamate exerts its regulatory control on the mediating enzyme, carbamyl phosphate synthetase (CPS). (medscape.com)
Synthetase5
Carbamoyl phosphate synthetase catalyzes the ATP-dependent synthesis of carbamoyl phosphate from glutamine (EC 6.3.5.5) or ammonia (EC 6.3.4.16) and bicarbonate. (wikipedia.org)
There are three different forms that serve very different functions: Carbamoyl phosphate synthetase I (mitochondria, urea cycle) Carbamoyl phosphate synthetase II (cytosol, pyrimidine metabolism). (wikipedia.org)
Carbamoyl phosphate synthetase III (found in fish). (wikipedia.org)
Carbamoyl phosphate synthase (CPSase) is a heterodimeric enzyme composed of a small and a large subunit (with the exception of CPSase III, which is composed of a single polypeptide that may have arisen from gene fusion of the glutaminase and synthetase domains). (wikipedia.org)
MGS-like domain, Carbamoyl-phosphate synthase L chain, Carbamoyl-phosphate synthetase large chain [Interproscan]. (ntu.edu.sg)
Glutamate3
The small subunit contains the glutamine binding site and catalyses the hydrolysis of glutamine to glutamate and ammonia, which is in turn used by the large chain to synthesize carbamoyl phosphate. (wikipedia.org)
Ammonia incorporation in animals occurs through the actions of glutamate dehydrogenase and glutamine synthase. (medmuv.com)
A pair of principal enzymes, glutamate dehydrogenase and glutamine synthatase, are found in all organisms and effect the conversion of ammonia into the amino acids glutamate and glutamine, respectively. (medmuv.com)
Small subunit3
CPSase has three active sites, one in the small subunit and two in the large subunit. (wikipedia.org)
The small subunit has a 3-layer beta/beta/alpha structure, and is thought to be mobile in most proteins that carry it. (wikipedia.org)
The C-terminal domain of the small subunit of CPSase has glutamine amidotransferase activity. (wikipedia.org)
Enzyme3
This enzyme catalyzes the reaction of ATP and bicarbonate to produce carboxy phosphate and ADP. (wikipedia.org)
The catalytic mechanism of CPSase involves the diffusion of carbamate through the interior of the enzyme from the site of synthesis within the N-terminal domain of the large subunit to the site of phosphorylation within the C-terminal domain. (wikipedia.org)
indicates that genes are non-redundant within the group ( e.g. genes encoding different subunits of the same enzyme). (umassmed.edu)
Urea cycle2
Since N -acetylglutamate (NAG) is the allosteric activator of carbamoylphosphate synthase, the entry step into the urea cycle, decreased ureagenesis occurs with accumulation of free ammonia. (medscape.com)
Inhibition of carbamoyl-phosphate synthase (ammonia) by Tris and Hepes. (wikipedia.org)
Studies suggest that the underlying cause of the hyperammonemia is the inhibition of N -acetylglutamate synthase (NAGS) activity by free propionic acid. (medscape.com)
Ensembl1
Carbamoyl-phosphate synthase large chain [Ensembl]. (ntu.edu.sg)
Protein2
Ammonia the highly toxic product of protein catabolism, is rapidly inactivated by a variety of reactions. (medmuv.com)
Reduced nitrogen enters the human body as dietary free amino acids, protein, and the ammonia produced by intestinal tract bacteria. (medmuv.com)
Synthesis1
the second locus, on chromosome 3, controls synthesis of the β subunit. (medscape.com)
Allosteric1
The large subunit in bacterial CPSase has four structural domains: the carboxy phosphate domain 1, the oligomerisation domain, the carbamoyl phosphate domain 2 and the allosteric domain. (wikipedia.org)
Biochemical1
Plasma ammonia for example, is considered the best available biochemical read-out of AMD, but does not provide insight in other pathophysiological processes that may occur during AMD. (biomedcentral.com)
Gene1
DHPS deficiency is a rare genetic disease caused by biallelic hypomorphic variants in the Deoxyhypusine synthase (DHPS) gene. (bvsalud.org)
Reaction1
These inter-domain tunnels connect the three distinct active sites, and function as conduits for the transport of unstable reaction intermediates (ammonia and carbamate) between successive active sites. (wikipedia.org)
Intermediate1
however, the N-terminal carboxy phosphate domain catalyses the phosphorylation of biocarbonate, while the C-terminal domain catalyses the phosphorylation of the carbamate intermediate. (wikipedia.org)
Pyruvate2
The carboxy phosphate domain found duplicated in the large subunit of CPSase is also present as a single copy in the biotin-dependent enzymes acetyl-CoA carboxylase (ACC), propionyl-CoA carboxylase (PCCase), pyruvate carboxylase (PC) and urea carboxylase. (wikipedia.org)
In the liver, alanine transaminase transfers the ammonia to α-KG and regenerates pyruvate. (medmuv.com)
Acute care: Hospital admission for children with insufficient oral intake and/or signs of metabolic decompensation such as encephalopathy in order to provide IV fluids (maintenance glucose plus extra calories via IV lipids) and to monitor plasma ammonia, serum lactate, serum glucose, blood gases, electrolytes, and liver parameters. (nih.gov)
Pyrimidine2
The six membered pyrimidine ring is made first and then attached to ribose phosphate. (web.app)
Apr 04, 2002 purine and pyrimidine nucleotides are major energy carriers, subunits of nucleic acids and precursors for the synthesis of nucleotide cofactors such as nad and sam. (web.app)
Carbamate3
however, the N-terminal carboxy phosphate domain catalyses the phosphorylation of biocarbonate, while the C-terminal domain catalyses the phosphorylation of the carbamate intermediate. (wikipedia.org)
These inter-domain tunnels connect the three distinct active sites, and function as conduits for the transport of unstable reaction intermediates (ammonia and carbamate) between successive active sites. (wikipedia.org)
Glutamine8
The small subunit contains the glutamine binding site and catalyses the hydrolysis of glutamine to glutamate and ammonia, which is in turn used by the large chain to synthesize carbamoyl phosphate. (wikipedia.org)
The C-terminal domain of the small subunit of CPSase has glutamine amidotransferase activity. (wikipedia.org)
Ammonia incorporation in animals occurs through the actions of glutamate dehydrogenase and glutamine synthase. (tdmuv.com)
A pair of principal enzymes, glutamate dehydrogenase and glutamine synthatase, are found in all organisms and effect the conversion of ammonia into the amino acids glutamate and glutamine, respectively. (tdmuv.com)
If ammonia-lowering medication is needed, consider use of carglumic acid, which (while not yet approved for this indication) has anecdotally shortened the period of hyperammonemia. (nih.gov)
Proteins2
The small subunit has a 3-layer beta/beta/alpha structure, and is thought to be mobile in most proteins that carry it. (wikipedia.org)
UniProt Number - a unique identifier assigned to all proteins, including enzymes, hemoglobin subunits, and immunoglobulin chains. (nih.gov)
Enzymes1
The carboxy phosphate domain found duplicated in the large subunit of CPSase is also present as a single copy in the biotin-dependent enzymes acetyl-CoA carboxylase (ACC), propionyl-CoA carboxylase (PCCase), pyruvate carboxylase (PC) and urea carboxylase. (wikipedia.org)
Gene1
DHPS deficiency is a rare genetic disease caused by biallelic hypomorphic variants in the Deoxyhypusine synthase (DHPS) gene. (bvsalud.org)
Alpha1
DNA polymerase III subunits gamma and tau domain III, DNA polymerase III subunits tau domain IV DnaB-binding, DNA polymerase III tau subunit V interacting with alpha [Interproscan]. (ntu.edu.sg)
A common clinical finding is mild-to-moderate blood ammonia elevation, which may contribute by direct neurotoxicity to changes in a patient's mentation. (medscape.com)