Literature summary for 6.3.5.5 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.

Search for more literature for 6.3.5.5

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	allosteric effectors bind at domain D of eCPS	Escherichia coli
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)

Cloned (Comment)	Organism
expression of wild-type and mutant enzymes	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
G919C	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	Escherichia coli
P909C	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	Escherichia coli
P909C/G919C	site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	allosteric effectors bind at domain D of eCPS	Escherichia coli
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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Escherichia coli

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + L-glutamine + HCO3- + H2O	Escherichia coli	-	ADP + phosphate + L-glutamate + carbamoyl phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.348	-	recombinant mutant P909C/G919C	Escherichia coli
0.472	-	recombinant mutant P909C	Escherichia coli
0.524	-	recombinant mutant G919C	Escherichia coli
0.855	-	recombinant wild-type enzyme	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + L-glutamine + HCO3- + H2O	-	Escherichia coli	ADP + phosphate + L-glutamate + carbamoyl phosphate	-	?
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

Subunits	Comment	Organism
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
octamer	4 * 42000 + 4 * 118000	Escherichia coli

Synonyms

Synonyms	Comment	Organism
carbamoyl-phosphate synthetase	-	Escherichia coli
CPS	-	Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	37	assay at	Escherichia coli

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.6	-	assay at	Escherichia coli

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Escherichia coli

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Release 2023.1 (January 2023)