Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.7.2.2 - carbamate kinase and Organism(s) Pyrococcus furiosus and UniProt Accession P95474

for references in articles please use BRENDA:EC2.7.2.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pyrococcus furiosus
UNIPROT: P95474
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
ATP
+
NH3
+
hydrogencarbonate
=
ADP
+
carbamoyl phosphate
+
H2O
+
+
=
+
+
Synonyms
carbamate kinase, ckase, atp:carbamate phosphotransferase, carbamyl phosphokinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
anabolic carbamyl kinase
-
carbamoyl phosphokinase
-
-
-
-
carbamyl phosphokinase
-
-
-
-
CKase
kinase, carbamate (phosphorylating)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
show the reaction diagram
mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
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
-
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
ATP + carbamate
ADP + carbamoyl phosphate
show the reaction diagram
-
-
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
show the reaction diagram
ATP + NH3 + CO2
ADP + 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
ADP + carbamoyl phosphate
ATP + NH3 + CO2
show the reaction diagram
carbamate kinase with an anabolic role. The extreme living conditions of the pyrococci may render unnecessary the enzymatic synthesis of carbamate by carbamoyl-phosphate synthetase with the associated expenditure of an extra ATP molecule, as a prelude to making carbamoyl phosphate, explaining the use of carbamate kinase for carbamoyl phosphate synthesis in this organisms
-
-
?
ATP + carbamate
ADP + carbamoyl phosphate
show the reaction diagram
-
-
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
show the reaction diagram
-
provides carbamoyl phosphate which is the precursor of the synthesis of pyrimidines and arginine
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
10 mM used in assay conditions
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
ADP
pH 8.0, 37°C
0.017
ATP
pH 8.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4 - 11.4
the enzyme is active over the entire pH range studied (7.4-11.4), with optimum activity at pH 9.9 and above
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
carbamoyl-phosphate synthetase and ornithine carbamoyltransferase form an efficient channeling cluster for carbamoyl phosphate, an extremely thermolabile and potentially toxic metabolic intermediate. Therefore, by physically interacting with each other, carbamoyl-phosphate synthetase and ornithine carbamoyltransferase prevent the thermodenaturation of carbamoyl phosphate in the aqueous cytoplasmic environment
physiological function
-
physically interacting with each other, carbamate kinase and ornithine carbamoyltransferase prevent thermodenaturation of carbamoyl phosphate (a precursor of pyrimidines and arginine, which is an extremely labile and potentially toxic intermediate) in the aqueous cytoplasmic environment. The carbamoyl phosphate channelling complex involves carbamate kinase, ornithine carbamoyltransferase and aspartate carbamoyltransferase
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
x * 34000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
homodimer, crystalline structure
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of the pyrococcal enzyme grown in the absence or presence of MgATP (Fig. 7) diffracted with a conventional X-ray source to at least 2.6 and 2.0 Å resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme can replace in vivo carbamoyl phosphate synthetase of Escherichia coli
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
there is no measurable change in catalysis after incubation at 40°C for 60 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified enzyme, 6 months, no loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-affinity column chromatography
recombinant protein from Saccharomyces cerevisiae
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expressed in Escherichia coli Rosetta(DE3) and Saccharomyces cerevisiae
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ramon-Maiques, S.; Marina, A.; Uriarte, M.; Fita, I.; Rubio, V.
The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases
J. Mol. Biol.
299
463-476
2000
Pyrococcus furiosus (P95474), Pyrococcus furiosus
Manually annotated by BRENDA team
Uriarte, M.; Marina, A.; Ramon-Maiques, S.; Fita, I.; Rubio, V.
The carbamoyl-phosphate synthetase of Pyrococcus furiosus is enzymologically and structurally a carbamate kinase
J. Biol. Chem.
274
16295-16303
1999
Pyrococcus furiosus, Pyrococcus furiosus (P95474)
Manually annotated by BRENDA team
Alcantara, C.; Cervera, J.; Rubio, V.
Carbamate kinase can replace in vivo carbamoyl phosphate synthetase. Implications for the evolution of carbamoyl phosphate biosynthesis
FEBS Lett.
484
261-264
2000
Pyrococcus furiosus
Manually annotated by BRENDA team
Massant, J.; Glansdorff, N.
New experimental approaches for investigating interactions between Pyrococcus furiosus carbamate kinase and carbamoyltransferases, enzymes involved in the channeling of thermolabile carbamoyl phosphate
Archaea
1
365-373
2005
Pyrococcus furiosus
Manually annotated by BRENDA team
Massant, J.; Glansdorff, N.
Metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus: dynamic enzyme-enzyme interactions involved in the formation of the channelling complex
Biochem. Soc. Trans.
32
306-309
2004
Pyrococcus furiosus
Manually annotated by BRENDA team
Massant, J.; Verstreken, P.; Durbec, V.; Kholti, A.; Legrain, C.; Beeckmans, S.; Cornelis, P.; Glansdorff, N.
Metabolic channeling of carbamoyl phosphate, a thermolabile intermediate Evidence for physical interaction between carbamate kinase-like carbamoyl-phosphate synthetase and ornithine carbamoyltransferase from the hyperthermophile Pyrococcus furiosus
J. Biol. Chem.
277
18517-18522
2002
Pyrococcus furiosus (P95474), Pyrococcus furiosus
Manually annotated by BRENDA team
Hennessy, J.E.; Latter, M.J.; Fazelinejad, S.; Philbrook, A.; Bartkus, D.M.; Kim, H.K.; Onagi, H.; Oakeshott, J.G.; Scott, C.; Alissandratos, A.; Easton, C.J.
Hyperthermophilic carbamate kinase stability and anabolic in vitro activity at alkaline pH
Appl. Environ. Microbiol.
84
e02250-17
2018
no activity in Clostridium tetani, Thermosipho melanesiensis (A6LPA8), Fervidobacterium nodosum (A7HNY8), Thermococcus sibiricus (C6A5J0), Thermococcus barophilus (F0LK57), Enterococcus faecalis (P0A2X7), Pyrococcus furiosus (P95474), Enterococcus faecalis ATCC 700802 (P0A2X7), Pyrococcus furiosus ATCC 43587 (P95474), Fervidobacterium nodosum ATCC 35602 (A7HNY8), Thermosipho melanesiensis DSM 120209 (A6LPA8), Thermococcus sibiricus DSM 12597 (C6A5J0), Thermococcus barophilus DSM 11836 (F0LK57)
Manually annotated by BRENDA team
Shi, D.; Caldovic, L.; Tuchman, M.
Sources and fates of carbamyl phosphate a labile energy-rich molecule with multiple facets
Biology
7
34
2018
Enterococcus faecalis (P0A2X7), Enterococcus faecalis ATCC 700802 (P0A2X7), Pyrococcus furiosus (P95474), Pyrococcus furiosus ATCC 43587 (P95474)
Manually annotated by BRENDA team