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Literature summary extracted from

  • Pekkala, S.; Martinez, A.I.; Barcelona, B.; Gallego, J.; Bendala, E.; Yefimenko, I.; Rubio, V.; Cervera, J.
    Structural insight on the control of urea synthesis: identification of the binding site for N-acetyl-L-glutamate, the essential allosteric activator of mitochondrial carbamoyl phosphate synthetase (2009), Biochem. J., 424, 211-220.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
6.3.4.16 inosine monophosphate weak activator, the IMP binding site is located at the C-terminus, binding structure analysis from crystal structure with bound IMP, PDB ID 1CE8 Escherichia coli
6.3.4.16 N-acetyl-L-beta-phenylglutamate lower activation of CPSI compared to N-acetyl-L-glutamate Homo sapiens
6.3.4.16 N-acetyl-L-glutamate i.e. NAG, allosteric activator, binding mode and site structure analysis by MALDI-TOF mass spectrometry, overview Rattus norvegicus
6.3.4.16 N-acetyl-L-glutamate i.e. NAG, allosteric activator, the binding mode and site in the crystal structure of human CPSI, PDB ID 2YVQ, is located in the C-terminal domain, docking experiments and structure, overview Homo sapiens
6.3.4.16 ornithine
-
 Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.3.4.16 cloning of N-terminally His6-tagged wild-type and mutant CPSIs in Escherichia coli and expression in Spodopetra frugiperda SF9 cells Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
6.3.4.16 N1437D site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme Rattus norvegicus
6.3.4.16 N1440D site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme Rattus norvegicus
6.3.4.16 T1391V site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme Rattus norvegicus
6.3.4.16 T1394A site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme Rattus norvegicus
6.3.4.16 W1410K site-directed mutagenesis, the mutant binds N-acetyl-L-beta-phenylglutamate at the N-acetyl-L-glutamate binding site Homo sapiens
6.3.4.16 W1410K site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
6.3.4.16 mitochondrion
-
 Rattus norvegicus 5739
-
6.3.4.16 mitochondrion
-
 Homo sapiens 5739
-

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.4.16 2 ATP + NH3 + CO2 + H2O Escherichia coli
-
 2 ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.4.16 2 ATP + NH3 + CO2 + H2O Rattus norvegicus
-
 2 ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.4.16 2 ATP + NH3 + CO2 + H2O Homo sapiens
-
 2 ADP + phosphate + carbamoyl phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.3.4.16 Escherichia coli
-
-
-
6.3.4.16 Homo sapiens P31327
-
-
6.3.4.16 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.4.16 recombinant His6-tagged wild-type and mutant CPSIs from Spodoptera frugiperda SF9 cells by affinity chromatography Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.3.4.16 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.4.16 2 ATP + NH3 + CO2 + H2O
-
 Escherichia coli 2 ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.4.16 2 ATP + NH3 + CO2 + H2O
-
 Rattus norvegicus 2 ADP + phosphate + carbamoyl phosphate
-
 ?
6.3.4.16 2 ATP + NH3 + CO2 + H2O
-
 Homo sapiens 2 ADP + phosphate + carbamoyl phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
6.3.4.16 carbamoyl phosphate synthetase
-
 Escherichia coli
6.3.4.16 carbamoyl phosphate synthetase
-
 Rattus norvegicus
6.3.4.16 carbamoyl phosphate synthetase
-
 Homo sapiens
6.3.4.16 carbamoyl phosphate synthetase I
-
 Rattus norvegicus
6.3.4.16 carbamoyl phosphate synthetase I
-
 Homo sapiens
6.3.4.16 CPS
-
 Escherichia coli
6.3.4.16 CPSI
-
 Rattus norvegicus
6.3.4.16 CPSI
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.3.4.16 37
-
 assay at Escherichia coli
6.3.4.16 37
-
 assay at Rattus norvegicus
6.3.4.16 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.3.4.16 7.4
-
 assay at Escherichia coli
6.3.4.16 7.4
-
 assay at Rattus norvegicus
6.3.4.16 7.4
-
 assay at Homo sapiens

Cofactor

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

General Information

EC Number General Information Comment Organism
6.3.4.16 metabolism CPSI is the first urea cycle enzyme Rattus norvegicus
6.3.4.16 metabolism CPSI is the first urea cycle enzyme Homo sapiens
6.3.4.16 physiological function CPSI is a key regulator of the urea cycle for ammonia detoxification in animals Rattus norvegicus
6.3.4.16 physiological function CPSI is a key regulator of the urea cycle for ammonia detoxification in animals, including humans Homo sapiens