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Literature summary extracted from

  • Hart, E.J.; Powers-Lee, S.G.
    Role of Cys1327 and Cys1337 in redox sensitivity and allosteric monitoring in human carbamoyl phosphate synthetase (2008), J. Biol. Chem., 284, 5977-5985.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.4.16 N-acetylglutamate the enzyme requires binding of and allosteric activation by N-acetylglutamate for catalytic activity Homo sapiens
6.3.5.5 additional information allosteric effectors bind at domain D of eCPS Escherichia coli
6.3.5.5 ornithine co-substrate with carbamoyl phosphate for the second step of arginine biosynthesis, acts as a positive allosteric effector for eCPS, the catalyst for the first pathway step Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.4.16 gene CPSI, expression of the N-terminally His6-FLAG-tagged enzyme in Schizosaccharomyces pombe from pESP5 Homo sapiens
6.3.5.5 expression of wild-type and mutant enzymes Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.16 C1327A the mutant shows reduced activity compared to the wild-type enzyme, the mutation significantly alters activity at the domain C ATP site, binding of N-acetylglutamate is affected, overview Homo sapiens
6.3.4.16 C1337A the mutant shows reduced activity compared to the wild-type enzyme, the mutation significantly alters activity at the domain C ATP site, binding of N-acetylglutamate is affected, overview Homo sapiens
6.3.5.5 G919C site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
6.3.5.5 P909C site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli
6.3.5.5 P909C/G919C site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.3.5.5 additional information allosteric effectors bind at domain D of eCPS Escherichia coli
6.3.5.5 UMP product of the pyrimidine nucleotide pathway, acts as a negative allosteric effector for eCPS, which also catalyzes the first step of this pathway Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.3.4.16 additional information
-
 additional information kinetics of wild-type and mutant enzymes, overview. The Km of the enzyme for ammonia is 100fold lower than that for CPSs that also use glutamine, EC 6.3.5.5 Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.3.4.16 mitochondrial matrix
-
 Homo sapiens 5759
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.4.16 Mg2+
-
 Homo sapiens
6.3.5.5 Mg2+
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
6.3.5.5 42000
-
 4 * 42000 + 4 * 118000 Escherichia coli
6.3.5.5 118000
-
 4 * 42000 + 4 * 118000 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.4.16 ATP + NH4+ + HCO3- + H2O Homo sapiens
-
 ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.5.5 ATP + L-glutamine + HCO3- + H2O Escherichia coli
-
 ADP + phosphate + L-glutamate + carbamoyl phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.16 Homo sapiens P31327 gene CPSI
-
6.3.5.5 Escherichia coli
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.4.16 liver
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.3.4.16 0.43
-
 purified recombinant tagged mutant C1327A Homo sapiens
6.3.4.16 0.47
-
 purified recombinant tagged mutant C1337A Homo sapiens
6.3.4.16 0.86
-
 purified recombinant tagged wild-type enzyme Homo sapiens
6.3.5.5 0.348
-
 recombinant mutant P909C/G919C Escherichia coli
6.3.5.5 0.472
-
 recombinant mutant P909C Escherichia coli
6.3.5.5 0.524
-
 recombinant mutant G919C Escherichia coli
6.3.5.5 0.855
-
 recombinant wild-type enzyme Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.16 ATP + NH4+ + HCO3- + H2O
-
 Homo sapiens ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.4.16 ATP + NH4+ + HCO3- + H2O synthesis of carbamoyl phosphate requires coordination of two hCPS active sites with ATP cleavage occurring at duplicated ATP grasp domains B and C Homo sapiens ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.5.5 ATP + L-glutamine + HCO3- + H2O
-
 Escherichia coli ADP + phosphate + L-glutamate + carbamoyl phosphate
-
 ?
6.3.5.5 ATP + L-glutamine + HCO3- + H2O neither residue P909 nor residue G919 is critical for eCPS function due to the absence of vicinal cysteinyl residues in wild-type eCPS Escherichia coli ADP + phosphate + L-glutamate + carbamoyl phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.5.5 More 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 Escherichia coli
6.3.5.5 octamer 4 * 42000 + 4 * 118000 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
6.3.4.16 Carbamoyl-phosphate synthetase I
-
 Homo sapiens
6.3.4.16 CPS1
-
 Homo sapiens
6.3.4.16 urea-specific CPS
-
 Homo sapiens
6.3.5.5 carbamoyl-phosphate synthetase
-
 Escherichia coli
6.3.5.5 CPS
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.4.16 25 30 assay at Homo sapiens
6.3.5.5 25 37 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.16 7.6
-
 assay at Homo sapiens
6.3.5.5 7.6
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
6.3.4.16 ATP
-
 Homo sapiens
6.3.5.5 ATP
-
 Escherichia coli