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Information on EC 6.3.5.5 - carbamoyl-phosphate synthase (glutamine-hydrolysing) and Organism(s) Saccharomyces cerevisiae and UniProt Accession P07259

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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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Saccharomyces cerevisiae
UNIPROT: P07259
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
carbamylphosphate synthetase - aspartate transcarbamylase
multifunctional protein
Carbamoyl phosphate synthase (glutamine)
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-
-
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Carbamoyl phosphate synthetase (glutamine-hydrolyzing)
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Carbamoyl-phosphate synthetase (glutamine-hydrolysing)
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-
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Carbamoylphosphate synthase
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-
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Carbamoylphosphate synthetase
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-
-
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Carbamoylphosphate synthetase II
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-
-
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Carbamyl phosphate synthetase (glutamine)
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-
-
-
Carbamyl phosphate sythetase II
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-
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-
CPS
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-
-
-
CPSase
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-
-
-
CPSase-A
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-
-
-
CPSase-P
-
-
-
-
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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-
-
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amination
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-
-
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amide group transfer
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-
-
-
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 + 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 product carbamoyl phosphate is utilized for the arginine biosynthesis
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
UTP
competitive, feedback inhibitor, binds to a regulatory site located in the vicinity of the carbamylphosphate synthetase catalytic subsite
UMP
-
the nonresponsive enzyme can bind UMP at domain D and allosteric effect on chimeric enzyme
UTP
-
feed-back inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
IMP
-
the nonresponsive enzyme can bind UMP at domain D and allosteric effect on chimeric enzyme
L-ornithine
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allosteric effect on chimeric enzyme, no effect on Saccharomyces cerevisae enzyme
phosphate
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multifunctional proteins are phosphorylated in vivo and in vitro. This covalent modification has only a small effect on the enzymic activity, and might be a signal for protein degradation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
carbamoyl-phosphate-synthase/aspartate-transcarbamoylase complex
Manually annotated by BRENDA team
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
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construction of a chimeric enzyme, in which the C-terminal 136 residues of Escherichia coli enzyme are replaced by the corresponding residues of Saccharomyces cerevisae enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D1220Y
aspartate transcarbamylase activity of the multifunctional mutant protein carbamylphosphate synthetase/aspartate transcarbamylase is no longer inhibited by UTP, carbamylphosphate synthetase activity retains fully sensitive to this effector
N1094D
aspartate transcarbamylase activity of the multifunctional mutant protein carbamylphosphate synthetase/aspartate transcarbamylase is no longer inhibited by UTP, carbamylphosphate synthetase activity retains fully sensitive to this effector
R1076S
aspartate transcarbamylase activity of the multifunctional mutant protein carbamylphosphate synthetase/aspartate transcarbamylase is no longer inhibited by UTP, carbamylphosphate synthetase activity retains fully sensitive to this effector
Y1096C
aspartate transcarbamylase activity of the multifunctional mutant protein carbamylphosphate synthetase/aspartate transcarbamylase is no longer inhibited by UTP, carbamylphosphate synthetase activity retains fully sensitive to this effector
Y1112L
aspartate transcarbamylase activity of the multifunctional mutant protein carbamylphosphate synthetase/aspartate transcarbamylase is no longer inhibited by UTP, carbamylphosphate synthetase activity retains fully sensitive to this effector
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Saccharomyces pombe
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Herve, G.; Nagy, M.; Le Gouar, M.; Penverne, B.; Ladjimi, M.
The carbamoyl phosphate synthetase-aspartate transcarbamoylase complex of Saccharomyces cerevisiae: molecular and cellular aspects
Biochem. Soc. Trans.
21
195-198
1993
Saccharomyces cerevisiae, Escherichia coli, eukaryota, Mesocricetus auratus
Manually annotated by BRENDA team
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
Eroglu, B.; Powers-Lee, S.G.
Unmasking a functional allosteric domain in an allosterically nonresponsive carbamoyl-phosphate synthetase
J. Biol. Chem.
277
45466-45472
2002
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Serre, V.; Penverne, B.; Souciet, J.L.; Potier, S.; Guy, H.; Evans, D.; Vicart, P.; Herve, G.
Integrated allosteric regulation in the S. cerevisiae carbamylphosphate synthetase - aspartate transcarbamylase multifunctional protein
BMC Biochem.
5
6
2004
Saccharomyces cerevisiae (P07259), Saccharomyces cerevisiae
Manually annotated by BRENDA team