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Information on EC 6.3.5.5 - carbamoyl-phosphate synthase (glutamine-hydrolysing) and Organism(s) Geobacillus stearothermophilus and UniProt Accession O50302

for references in articles please use BRENDA:EC6.3.5.5
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EC Tree
IUBMB Comments
The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides . The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length . The amidotransferase domain within the small subunit of the enzyme hydrolyses glutamine to ammonia via a thioester intermediate. The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate . cf. EC 6.3.4.16, carbamoyl-phosphate synthase (ammonia).
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Geobacillus stearothermophilus
UNIPROT: O50302
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The taxonomic range for the selected organisms is: Geobacillus stearothermophilus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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2
ATP
+
L-glutamine
+
hydrogencarbonate
+
H2O
=
2
ADP
+
phosphate
+
L-glutamate
+
carbamoyl phosphate
2
+
+
+
=
2
+
+
+
Synonyms
cps iii, cad protein, carbamoyl phosphate synthetase ii, carbamoyl phosphate synthetase iii, cpsii, carbamoyl-phosphate synthetase 2, glutamine-dependent carbamyl phosphate synthetase, carbamoyl phosphate synthetase (glutamine-hydrolyzing), carbamylphosphate synthetase - aspartate transcarbamylase, cpsase type ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Carbamoyl phosphate synthase (glutamine)
-
-
-
-
Carbamoyl phosphate synthetase (glutamine-hydrolyzing)
-
-
-
-
Carbamoyl-phosphate synthetase (glutamine-hydrolysing)
-
-
-
-
Carbamoylphosphate synthase
-
-
-
-
Carbamoylphosphate synthetase
-
-
-
-
Carbamoylphosphate synthetase II
-
-
-
-
Carbamyl phosphate synthetase (glutamine)
-
-
-
-
Carbamyl phosphate sythetase II
-
-
-
-
CPS
-
-
-
-
CPSase
-
-
-
-
CPSase-A
-
-
-
-
CPSase-P
-
-
-
-
Glutamine-dependent carbamyl phosphate synthetase
-
-
-
-
Synthase, carbamoylphosphate (glutamine)
-
-
-
-
Synthetase, carbamoylphosphate (glutamine-hydrolyzing)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phosphorylation
-
-
-
-
amination
-
-
-
-
amide group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating)
The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides [4]. The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length [8]. The amidotransferase domain within the small subunit of the enzyme hydrolyses glutamine to ammonia via a thioester intermediate. The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate [6]. cf. EC 6.3.4.16, carbamoyl-phosphate synthase (ammonia).
CAS REGISTRY NUMBER
COMMENTARY hide
37233-48-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ATP + L-Gln + HCO3-
2 ADP + phosphate + L-Glu + carbamoyl phosphate
show the reaction diagram
2 ATP + L-Gln + HCO3-
2 ADP + phosphate + L-Glu + carbamoyl phosphate
show the reaction diagram
-
-
-
?
2 ATP + NH4+ + HCO3-
2 ADP + phosphate + carbamoyl phosphate
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 ATP + L-Gln + HCO3-
2 ADP + phosphate + L-Glu + carbamoyl phosphate
show the reaction diagram
the enzyme catalyses the first step in the arginine and pyrimidine biosynthesis
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Arg
-
arginine-specific carbamoyl-phosphate synthase is repressed, pyrimidine-specific enzyme not
UMP
-
carbamoyl-phosphate synthase belonging to the pyrimidine pathway, carbamoyl-phosphate synthase belonging to the arginine pathway is not inhibited
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-phospho-alpha-D-ribosyl 1-diphosphate
-
pyrimidine-specific carbamoyl-phosphate synthase is activated, arginine-specific enzyme not
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.18 - 22
L-Gln
9.8
NH4+
-
carbamoyl-phosphate synthase belonging to the pyrimidine pathway
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CARB_GEOSE
1064
0
116243
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
116200
the large subunit
118000
-
000 + 1 * 118000, carbamoyl-phosphate synthase belonging to the pyrimidine pathway, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
000 + 1 * 118000, carbamoyl-phosphate synthase belonging to the pyrimidine pathway, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the thermal stability of cloned enzyme is identical regardless of the growth temperature of Bacillus stearothermophilus between 42°C and 63°C. The thermal stability of the cloned enzyme is not affected by expression at 37°C in Bacillus subtilis or E. coli
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
pyrAb encodes the large subunit
carbamoyl-phosphate synthase belonging to the pyrimidine pathway
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, H.; Park, S.M.; Nolan, W.G.; Lu, C.D.; Abdelal, A.T.
Cloning and characterization of the arginine-specific carbamoyl-phosphate synthetase from Bacillus stearothermophilus
Eur. J. Biochem.
249
443-449
1997
Geobacillus stearothermophilus
Manually annotated by BRENDA team
Vlaskova, H.; Krasny, L.; Fucik, V.; Jonak, J.
The pyrAb gene coding for the large subunit of carbamoylphosphate synthetase from Bacillus stearothermophilus: molecular cloning and functional characterization
Folia Biol. (Praha)
44
163-172
1998
Geobacillus stearothermophilus (O50302)
Manually annotated by BRENDA team