Any feedback?
Information on EC 2.7.2.2 - carbamate kinase
for references in articles please use BRENDA:EC2.7.2.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Word Map
- 2.7.2.2
- ornithine
- deiminase
-
dihydrolase
- citrulline
-
transcarbamoylase
-
carbamyltransferase
-
arcabc
- n-acetyl-l-glutamate
- drug development
- degradation
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
carbamate kinase, ckase, atp:carbamate phosphotransferase, carbamyl phosphokinase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ACK
anabolic carbamyl kinase
carbamate kinase
carbamoyl phosphokinase
-
-
-
-
carbamyl phosphokinase
-
-
-
-
catabolic carbamyl kinase
CCK
CKase
kinase, carbamate (phosphorylating)
-
-
-
-
putrescine synthase
-
enzyme has inherent activities of agmatine iminohydrolase, putrescine transcarbamylase, ornithinetranscarbamylase and carbamate kinase
CKase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + carbamate = ADP + carbamoyl phosphate
(1a)
-
-
-
NH3 + hydrogencarbonate = carbamate + H2O
(1b), spontaneous
-
-
-
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
mechanism
-
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
mechanism
-
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
mechanism
-
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
mechanism
-
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
mechanism
-
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
mechanism
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
random type reaction mechanism
-
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
comparison of carbamate kinases and carbamoyl phosphate synthases
-
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
overall reaction
-
-
-
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
the protein residues involved in ligand binding, together with a model of the transition state, suggest that catalysis follows an in-line, predominantly dissociative, phosphotransfer reaction mechanism, and that closure of the flexible auxiliary domain is required to protect the transition state from bulk solvent. Model of the transition state, overview
ATP + NH3 + hydrogencarbonate = ADP + carbamoyl phosphate + H2O
mechanism
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9026-69-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
ADP + carbamoyl phosphate
ATP + NH3 + CO2
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
-
-
?
ADP + carbamoyl phosphate
ATP + NH3 + CO2
-
The parasite actively transports arginine and ornithine, which are converted via the arginine dihydrolase pathway to citrulline and carbamoyl phosphate, resulting in the formation of ATP via carbamate kinase
-
-
?
ADP + carbamoyl phosphate
ATP + NH3 + CO2
-
The parasite actively transports arginine and ornithine, which are converted via the arginine dihydrolase pathway to citrulline and carbamoyl phosphate, resulting in the formation of ATP via carbamate kinase
-
-
?
ATP + carbamate
ADP + carbamoyl phosphate
-
-
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
reaction proceeds more readily in direction of ATP synthesis
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
reaction proceeds more readily in direction of ATP synthesis
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
reaction proceeds more readily in direction of ATP synthesis
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
multifunctional enzyme, involved in biosynthesis of putrescine
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
reaction proceeds more readily in direction of ATP synthesis
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
reaction proceeds more readily in direction of ATP synthesis
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
carbamoyl phosphate synthetase is a carbamate synthase
-
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
carbamoyl phosphate synthetase is a carbamate synthase
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
provides carbamoyl phosphate which is the precursor of the synthesis of pyrimidines and arginine
-
-
?
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-
-
-
?
additional information
?
-
-
some carbamate kinases also utilize acetate
-
-
?
additional information
?
-
ligand binding involves conformational flexibility of an auxiliary domain (amino acid residues 123-170), which exhibits open or closed conformations or structural disorder, depending on the bound ligand
-
-
?
additional information
?
-
-
ligand binding involves conformational flexibility of an auxiliary domain (amino acid residues 123-170), which exhibits open or closed conformations or structural disorder, depending on the bound ligand
-
-
?
additional information
?
-
-
some carbamate kinases also utilize acetate
-
-
?
additional information
?
-
-
some carbamate kinases also utilize acetate
-
-
?
additional information
?
-
-
some carbamate kinases also utilize acetate
-
-
?
additional information
?
-
-
activity with acetylphosphate is approximately 5% of that with carbamoyl phosphate as phosphoryl donor
-
-
?
additional information
?
-
-
some carbamate kinases also utilize acetate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
ADP + carbamoyl phosphate
ATP + NH3 + CO2
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
-
-
?
ADP + carbamoyl phosphate
ATP + NH3 + CO2
-
The parasite actively transports arginine and ornithine, which are converted via the arginine dihydrolase pathway to citrulline and carbamoyl phosphate, resulting in the formation of ATP via carbamate kinase
-
-
?
ADP + carbamoyl phosphate
ATP + NH3 + CO2
-
The parasite actively transports arginine and ornithine, which are converted via the arginine dihydrolase pathway to citrulline and carbamoyl phosphate, resulting in the formation of ATP via carbamate kinase
-
-
?
ATP + carbamate
ADP + carbamoyl phosphate
-
-
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
multifunctional enzyme, involved in biosynthesis of putrescine
-
r
ATP + NH3 + CO2
ADP + carbamoyl phosphate
-
provides carbamoyl phosphate which is the precursor of the synthesis of pyrimidines and arginine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
nucleotide binding structure and conformational flexibility analysis, overview
-
additional information
-
nucleotide binding structure and conformational flexibility analysis, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Bivalent cation
Co2+
Fe2+
Mg2+
Mn2+
additional information
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+
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+
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+
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+
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+
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+
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+
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+
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+
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+
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+
-
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+
-
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+
-
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+
-
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+
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+
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+
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+
additional information
-
activity in HEPES buffer is twice that in potassium citrate buffer at pH 6.0
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,3-Butanedione
-
in borate buffer, inactivation, implying the presence of an essential arginine
Disulfiram
the anti-alcoholism drug kills the trophozoites and inhibits the enzyme. Disulfiram acts by modifying Cys-242 adjacent to the active site and cures giardiasis in mice. The compound thiocarbamoylates Cys242, a residue located at the edge of the active site. The modified Cys242 prevents a conformational transition of a loop adjacent to the ADP/ATP binding site, which is required for the stacking of Tyr245 side chain against the adenine moiety
metronidazole
irreversible inactivation mechanism, the thiuram compounds can circumvent the resistance mechanism that renders metronidazole ineffectiveness in drug resistance cases of giardiasis