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heterotrimer
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CPS.A-subunit, CPS.B-subunit and glutaminase-subunit, 1* 64000 Da, 1 * 63000 Da and 1 * 45000 Da, but only the CPS.A-CPS.B-dimer has catalytic activity, SDS-PAGE
octamer
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4 * 42000 + 4 * 118000
tetramer
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at high concentrations in presence of ornithine
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x * 40000 + x * 118000
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x * 56000 (subunit N) + x * 71000 (subunit C), SDS-PAGE
?
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the large catalytic subunit has a MW of 130000, SDS-PAGE
dimer
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1 * 40000, glutaminase subunit, + 1 * 120000, synthase subunit. The synthase subunit consists of two homologous domains, CPS.A and CPS.B, which catalyze the two different ATP-dependent partial reactions involved in carbamoyl-phosphate synthesis
dimer
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1 * 40000, subunit contains the binding site for glutamine, + 1 * 133000, subunit contains the binding sites for NH4+, HCO3-, ATP, and the allosteric effectors. The light and heavy subunits are encoded by the genetically linked car A and car B genes, respectively
dimer
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1 * 40000 + 1 * 130000, SDS-PAGE
dimer
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1 * 41400 + 1 * 117700, the large subunit catalyses the carbamoyl phosphate synthesis from ammonia in three steps, and binds the effectors in its 15000 domain
dimer
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2 * 58000, SDS-PAGE, chimeric protein
dimer
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at low concentrations in presence of UMP
dimer
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The enzyme consists of an amidotransferase domain or subunit, GLN, 40000 Da, that hydrolyzes glutamine and transfers the ammonia to the synthetase component, CPS, 120000 Da, where the biosynthetic reaction occurs. The CPS domain is composed of two homologous subdomains, CPS.A and CPS.B, that catalyse different ATP-dependent reactions involved in the carbamoyl phosphate synthesis. The CPS.A and CPS.B monomers could each catalyse all of the partial reactions, but catalysis of the overall synthesis of carbamoyl phosphate requires a dimer composed of two of the equivalent domains.
dimer
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1 * 40000 + 1 * 130000, SDS-PAGE
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dimer
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1 * 41400 + 1 * 117700, the large subunit catalyses the carbamoyl phosphate synthesis from ammonia in three steps, and binds the effectors in its 15000 domain
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dimer
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000 + 1 * 118000, carbamoyl-phosphate synthase belonging to the pyrimidine pathway, SDS-PAGE
dimer
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1 * 44000 + 1 * 12200, SDS-PAGE
dimer
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1 * 45000, beta, + 1 * 110000, alpha
heterodimer
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small and large subunit, the small subunit contains a class I (trpG)-type glutaminase domain to hydrolyze glutamine to ammonia. carB is composed of three exons encoding a 120 kDa large subunit, consisting of the duplicated synthetase regions and the ATP-binding domains to synthesize carbamoyl phosphate
heterodimer
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1 * 42000 + 1 * 118000
heterodimer
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alpha,beta, 1 * 42000 + 1 * 118000
heterodimer
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alpha,beta, 1 * 42000 + 1 * 118000, the ammonia tunnel is responsible for the migration of ammonia, that is produced at the active site of the small subunit and migrates to the large subunit, the carbamate tunnel connects the two active sites contained within the carboxy phosphate and carbamoyl phosphate domains of the large subunit
heterodimer
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alpha,beta, 1 * 42000 + 1 * 118000, the effectors ornithine, IMP and UMP modulate the oligomerization of the heterodimer to higher ordered species
heterodimer
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alpha,beta, that readily converts to an tetrameric species: 4 * alpha, beta in presence of positive allosteric effectors, the smaller of two subunits contains 382 amino acid residues and is responsible for the hydrolysis of free ammonia, the larger subunit contains 1073 amino acid residues and provides the binding sites for the two MgATP2 molecules required for the assembly of carbamoyl phosphate, structure and reaction mechanism
heterodimer
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alpha,beta, that readly coverts to an tetrameric species: 4 * alpha, beta in presence of positive allosteric effectors
heterodimer
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alpha,beta, the heteodimer aggregates to form tetramers of dimers, structure
heterodimer
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alpha,beta, the small subunit is able to catalyze the hydrolysis of glutamine, the large subunit catalyses the formation of carbamoyl phosphate using ammonia as a nitrogen source
heterodimer
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the small subunit belongs to the class I amidotransferase family of enzymes, the reaction mechanism of the small subunit proceeds through the formation of the glutamyl thioester intermediate
heterodimer
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1 * 42000, small subunit, + 118000, large subunit
homotrimer
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2 * 40000, SDS-PAGE
homotrimer
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2 * 40000, SDS-PAGE
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additional information
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enzyme can exist in different monomer conformations and states of association
additional information
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reversible concentration-dependent self-association. When the enzyme concentration is lower than 0.01 g/L the enzyme exists as monomer under all conditions
additional information
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enzyme exists in monomer, dimer, and higher oligomeric forms, which are associated with its regulation by allosteric effectors. In barbital buffer the enzyme is present as a monomer. In sodium phosphate buffer, the enzyme exists as a partially dissociating dimer. In presence of phosphate and a positive allosteric effector, the maximum association state of the enzyme is a tetramer. UMP promotes conversion to a dimer
additional information
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NH4+ or Orn promotes oligomer formation. Tetramer or higher oligomeric species in potassium phosphate buffer containing Orn
additional information
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in absence of effectors the enzyme behaves as a dissociating system possibly reflecting the dimer-tetramer equilibrium
additional information
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the enzyme consists of two polypeptide chains referred to as small and large subunits, which contain a total of three separate active sites that are connected by an intramolecular tunnel
additional information
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crystal structure modelling and analysis, A2 is the glutamine amidotransferase domain and A1 is involved in communicating active site occupancy between the amidotransferase and synthetase active sites. Domains B and C are regions of internal duplication andeach contains an ATP grasp fold. Domains D' and D contain the interfaces for eCPS self-association. In addition to this role, domain D is the site for allosteric regulation of eCPS. The intramolecular tunnel connecting the three active sites
additional information
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the smaller subunit contains the binding site for the hydrolysis of glutamine, whereas the large subunit catalyzes the formation of carbamoyl phosphate. The enzyme posssesses three distinct active sites and an ammonia tunnel, that starts at the active site in the small subunit and leads to the active site in the N-terminal domain of the large subunit
additional information
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presence of three spatially distinct active sites that are linked by two long molecular tunnels that extend approximately 100 A from one end of the protein to the other
additional information
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enzyme exists in monomer, dimer, and higher oligomeric forms, which are associated with its regulation by allosteric effectors. In barbital buffer the enzyme is present as a monomer. In sodium phosphate buffer, the enzyme exists as a partially dissociating dimer. In presence of phosphate and a positive allosteric effector, the maximum association state of the enzyme is a tetramer. UMP promotes conversion to a dimer
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additional information
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additional information
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the homologous CPS.A. and CPS.B. subdomains are functionally equivalent, although in the native enzyme they may have different functions resulting from their juxtaposition relative to the other components in the complex
additional information
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self-association does not play a role in regulation of enzyme activity