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Information on EC 6.3.4.16 - carbamoyl-phosphate synthase (ammonia) and Organism(s) Methanobrevibacter smithii and UniProt Accession A5UK38

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EC Tree
IUBMB Comments
The enzyme catalyses the first committed step in the urea cycle. The reaction proceeds via three separate chemical reactions: phosphorylation of hydrogencarbonate to carboxyphosphate; a nucleophilic attack of ammonia on carboxyphosphate yielding carbamate; and the phosphorylation of carbamate forming carbamoyl phosphate. Two moles of ATP are utilized for the synthesis of one molecule of carbamyl phosphate, making the reaction essentially irreversible. The enzyme requires the allosteric activator N-acetyl-L-glutamate. cf. EC 6.3.5.5, carbamoyl-phosphate synthase (glutamine-hydrolysing).
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Methanobrevibacter smithii
UNIPROT: A5UK38
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The taxonomic range for the selected organisms is: Methanobrevibacter smithii
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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2
ATP
+
NH3
+
hydrogencarbonate
=
2
ADP
+
phosphate
+
carbamoyl phosphate
2
+
+
=
2
+
+
Synonyms
carbamoyl phosphate synthetase, cpsase, carbamoyl-phosphate synthetase, carbamoylphosphate synthetase, cps i, cps-i, carbamyl phosphate synthetase i, cps-1, carbamoylphosphate synthase, carbamoyl phosphate synthetase i, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbamoyl phosphate synthetase
-
Carbamoyl-phosphate synthetase I
-
-
-
-
Carbamoylphosphate synthase
-
-
-
-
Carbamoylphosphate synthase (ammonia)
-
-
-
-
Carbamoylphosphate synthetase (ammonia)
-
-
-
-
Carbamoylphosphate synthetase I
-
-
-
-
Carbamyl phosphate synthase I
-
-
-
-
Carbamylphosphate synthetase
-
-
-
-
Carbamylphosphate synthetase I
-
-
-
-
carbmoylphosphate synthetase
-
-
-
-
Carbon-dioxide-ammonia ligase
-
-
-
-
Carbonate kinase (phosphorylating)
-
-
-
-
CPS I
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
carbon-dioxide:ammonia ligase (ADP-forming, carbamate-phosphorylating)
The enzyme catalyses the first committed step in the urea cycle. The reaction proceeds via three separate chemical reactions: phosphorylation of hydrogencarbonate to carboxyphosphate; a nucleophilic attack of ammonia on carboxyphosphate yielding carbamate; and the phosphorylation of carbamate forming carbamoyl phosphate. Two moles of ATP are utilized for the synthesis of one molecule of carbamyl phosphate, making the reaction essentially irreversible. The enzyme requires the allosteric activator N-acetyl-L-glutamate. cf. EC 6.3.5.5, carbamoyl-phosphate synthase (glutamine-hydrolysing).
CAS REGISTRY NUMBER
COMMENTARY hide
9026-23-7
-
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 + 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 + NH4+ + HCO3-
2 ADP + phosphate + carbamoyl phosphate
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 1
ATP
at pH 8.0 and 37°C
1 - 4.5
HCO3-
at pH 8.0 and 37°C
15.6
NH4+
at pH 8.0 and 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043
ATP
at pH 8.0 and 37°C
0.044
HCO3-
at pH 8.0 and 37°C
0.052
NH4+
at pH 8.0 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0705
ATP
at pH 8.0 and 37°C
0.003
HCO3-
at pH 8.0 and 37°C
0.0033
NH4+
at pH 8.0 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00452
ATP synthetase reverse reaction rate, at pH 8.0 and 37°C
0.077
carbamoyl phosphate synthetase reaction rate, at pH 8.0 and 37°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.6
calculated from amino acid sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DSM 861
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41403
2 * 41403, calculated from amino acid sequence
44000
2 * 44000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Popa, E.; Perera, N.; Kibedi-Szabo, C.Z.; Guy-Evans, H.; Evans, D.R.; Purcarea, C.
The smallest active carbamoyl phosphate synthetase was identified in the human gut archaeon Methanobrevibacter smithii
J. Mol. Microbiol. Biotechnol.
22
287-299
2012
Methanobrevibacter smithii (A5UK38), Methanobrevibacter smithii
Manually annotated by BRENDA team