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Information on EC 6.3.5.5 - carbamoyl-phosphate synthase (glutamine-hydrolysing) and Organism(s) Drosophila melanogaster and UniProt Accession P05990

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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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This record set is specific for:
Drosophila melanogaster
UNIPROT: P05990
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Word Map
The taxonomic range for the selected organisms is: Drosophila melanogaster
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
cps iii, cad protein, carbamoyl phosphate synthetase iii, carbamoyl phosphate synthetase ii, cpsii, carbamoyl-phosphate synthetase 2, glutamine-dependent carbamyl phosphate synthetase, carbamoyl phosphate synthetase (glutamine-hydrolyzing), cpsase type ii, carbamylphosphate synthetase - aspartate transcarbamylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Carbamoyl phosphate synthase (glutamine)
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Carbamoyl phosphate synthetase (glutamine-hydrolyzing)
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Carbamoyl-phosphate synthetase (glutamine-hydrolysing)
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Carbamoylphosphate synthase
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Carbamoylphosphate synthetase
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Carbamoylphosphate synthetase II
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Carbamyl phosphate synthetase (glutamine)
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Carbamyl phosphate sythetase II
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CPS
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CPSase
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CPSase-A
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CPSase-P
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Glutamine-dependent carbamyl phosphate synthetase
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Synthase, carbamoylphosphate (glutamine)
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Synthetase, carbamoylphosphate (glutamine-hydrolyzing)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Phosphorylation
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amination
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amide group transfer
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -, -, -
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
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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
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?
2 ATP + L-Gln + HCO3-
2 ADP + phosphate + L-Glu + carbamoyl phosphate
show the reaction diagram
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
UTP
slight UTP inhibition of SU(b) mutant enzyme is probably due to the chelating of Mg2+ by UTP
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.4 - 3
HCO3-
0.04 - 0.057
L-glutamine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
supressor of black mutation
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PYR1_DROME
2224
0
246672
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
supressor of black mutation, Su(b), which causes a loss of UTP feedback inhibition, is a missense mutation resulting in a glutamate to lysine substitution within the second ATP binding site of enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nara, T.; Gao, G.; Yamasaki, H.; Nakajima-Shimada, J.; Aoki, T.
Carbamoyl-phosphate synthetase II in kinetoplastids
Biochim. Biophys. Acta
1387
462-468
1998
Dictyostelium discoideum, Drosophila melanogaster, Escherichia coli, Leishmania mexicana (O15829), Mesocricetus auratus, Saccharomyces cerevisiae, Trypanosoma cruzi (O15830)
Manually annotated by BRENDA team
Simmons, A.J.; Rawls, J.M.; Piskur, J.; Davidson, J.N.
A mutation that uncouples allosteric regulation of carbamyl phosphate synthetase in Drosophila
J. Mol. Biol.
287
277-285
1999
Drosophila melanogaster (P05990)
Manually annotated by BRENDA team