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Information on EC 2.7.2.2 - carbamate kinase and Organism(s) Enterococcus faecalis and UniProt Accession P0A2X7
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2.7.2.2 carbamate kinaseIUBMB 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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Word Map
- 2.7.2.2
- ornithine
- deiminase
-
dihydrolase
- citrulline
-
transcarbamoylase
-
carbamyltransferase
-
arcabc
- n-acetyl-l-glutamate
- drug development
- degradation
The taxonomic range for the selected organisms is: Enterococcus faecalis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carbamoyl phosphokinase
-
-
-
-
carbamyl phosphokinase
-
-
-
-
CKase
-
-
-
-
kinase, carbamate (phosphorylating)
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
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
9026-69-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
reaction proceeds more readily in direction of ATP synthesis
-
r
additional information
?
-
-
stereochemistry of binding of thiophosphate analogs of ATP and ADP
-
-
?
additional information
?
-
-
some carbamate kinases also utilize acetate
-
-
?
additional information
?
-
-
MgdATP2- is as effective a phosphate donor as MgATP2-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Bivalent cation
-
required, Mg2+ is the most commonly used, enzyme from Streptococcus lactis is also fully active with Mn2+ and less so with Fe2+ and Co2+
Co2+
-
bivalent cation required, Mg2+ is the most commonly used, enzyme from Streptococcus lactis is also fully active with Mn2+ and less so with Fe2+ and Co2+
Fe2+
-
bivalent cation required, Mg2+ is the most commonly used, enzyme from Streptococcus lactis is also fully active with Mn2+ and less so with Fe2+ and Co2+
Mg2+
Mn2+
Mg2+
-
bivalent cation required, Mg2+ is the most commonly used, enzyme from Streptococcus lactis is also fully active with Mn2+ and less so with Fe2+ and Co2+
Mn2+
-
bivalent cation required, Mg2+ is the most commonly used, enzyme from Streptococcus lactis is also fully active with Mn2+ and less so with Fe2+ and Co2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-Butanedione
-
in borate buffer, inactivation, implying the presence of an essential arginine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
there is no measurable change in catalysis after incubation at 40°C for 60 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
putative gene for carbamate kinase is ef0735 on the DNA strand of the Enterococcus faecalis V583 chromosome. The arginine deiminase pathway of arginine catabolism probably supplies the genes for PTC and CK but not those for the agmatine/putrescine antiporter
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raijman, L.; Jones, M.E.
Carbamate kinase
The Enzymes,3rd Ed. (Boyer,P. D. ,ed. )
9
97-119
1973
Enterococcus faecalis, Enterococcus faecalis D10, Lactococcus lactis, Mycoplasma hominis, Neurospora crassa, Serratia marcescens
-
Wang, T.T.; Bishop, S.H.; Himoe, A.
Detection of carbamate as a product of the carbamate kinase-catalyzed reaction by stopped flow spectrophotometry
J. Biol. Chem.
247
4437-4440
1972
Enterococcus faecalis, Enterococcus faecalis D10
Pillai, R.P.; Raushel, F.M.; Villafranca, J.J.
Stereochemistry of binding of thiophosphate analogs of ATP and ADP to carbamate kinase, glutamine synthetase, and carbamoyl-phosphate synthetase
Arch. Biochem. Biophys.
199
7-15
1980
Enterococcus faecalis
Pillai, R.P.; Marshall, M.; Villafranca, J.J.
Modification of an essential arginine of carbamate kinase
Arch. Biochem. Biophys.
199
16-20
1980
Enterococcus faecalis
Pillai, R.P.; Marshall, M.; Villafranca, J.J.
Substrate and metal ion binding to carbamate kinase: NMR and EPR studies
Arch. Biochem. Biophys.
199
21-27
1980
Enterococcus faecalis
Pandey, V.N.; Pradhan, D.S.
Reverse and forward reactions of carbamyl phosphokinase from Streptococcus faecalis R. Participation of nucleotides and reaction mechanisms
Biochim. Biophys. Acta
660
284-292
1981
Enterococcus faecalis
Llacer, J.L.; Polo, L.M.; Tavarez, S.; Alarcon, B.; Hilario, R.; Rubio, V.
The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction
J. Bacteriol.
189
1254-1265
2007
Enterococcus faecalis, Enterococcus faecalis ATCC 700802
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)
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)
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