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Information on EC 2.7.2.2 - carbamate kinase and Organism(s) Pseudomonas aeruginosa

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EC Tree
IUBMB Comments
The enzyme catalyses the reversible conversion of carbamoyl phosphate and ADP to ATP and carbamate, which hydrolyses to ammonia and hydrogencarbonate. The physiological role of the enzyme is to generate ATP.
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This record set is specific for:
Pseudomonas aeruginosa
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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Synonyms
carbamate kinase, ckase, atp:carbamate phosphotransferase, carbamyl phosphokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbamoyl phosphokinase
-
-
-
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carbamyl phosphokinase
-
-
-
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CKase
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-
-
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kinase, carbamate (phosphorylating)
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
show the reaction diagram
comparison of carbamate kinases and carbamoyl phosphate synthases
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:carbamate phosphotransferase
The enzyme catalyses the reversible conversion of carbamoyl phosphate and ADP to ATP and carbamate, which hydrolyses to ammonia and hydrogencarbonate. The physiological role of the enzyme is to generate ATP.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-69-1
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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
ADP + carbamoyl phosphate
ATP + NH3 + CO2
show the reaction diagram
-
-
-
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
show the reaction diagram
-
-
-
r
additional information
?
-
-
activity with acetylphosphate is approximately 5% of that with carbamoyl phosphate as phosphoryl donor
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
activity in HEPES buffer is twice that in potassium citrate buffer at pH 6.0
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
activity in HEPES buffer is twice that in potassium citrate buffer at pH 6.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
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pH 5.0: about 50% of maximum activity, pH 8.0: about 60% of maximum activity
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?
A0A367M4L1_PSEAI
176
0
18728
TrEMBL
-
A0A367M711_PSEAI
167
0
18232
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
2 * 37000, SDS-PAGE
74000
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sucrose density gradient centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 37000, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
comparison of carbamate kinases and carbamoyl phosphate synthases
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abdelala, A.T.; Bibb, W.F.; Nainan, O.
Carbamate kinase from Pseudomonas aeruginosa: purification, characterization, physiological role, and regulation
J. Bacteriol.
151
1411-1419
1982
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Rubio, V.; Cervera, J.
The carbamoyl-phosphate synthase family and carbamate kinase: structure-function studies
Biochem. Soc. Trans.
23
879-883
1995
Pseudomonas aeruginosa
Manually annotated by BRENDA team