carbamate kinase

{{infobox enzyme

| Name = carbamate kinase

| EC_number = 2.7.2.2

| CAS_number = 9026-69-1

| GO_code = 0008804

| image =

| width =

| caption =

}}

In enzymology, a carbamate kinase ({{EC number|2.7.2.2}}) is an enzyme that catalyzes the chemical reaction

:ATP + NH₃ + CO₂ $\rightleftharpoons$ ADP + carbamoyl phosphate

The 3 substrates of this enzyme are ATP, NH₃, and CO₂, whereas its two products are ADP and carbamoyl phosphate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:carbamate phosphotransferase. Other names in common use include CKase, carbamoyl phosphokinase, and carbamyl phosphokinase. This enzyme participates in 4 metabolic pathways: purine metabolism, glutamate metabolism, arginine and proline metabolism, and nitrogen metabolism.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes {{PDB link|1B7B}}, {{PDB link|1E19}}, and {{PDB link|2E9Y}}.

References

{{cite journal | vauthors = Bishop SH, Grisolia S | date = 1966 | title = Crystalline carbamate kinase | journal = Biochim. Biophys. Acta | volume = 118 | pages = 211–5 | pmid = 4959296 | issue = 1 | doi = 10.1016/s0926-6593(66)80163-7 }}
{{cite journal | author = Davis RH | date = 1965 | title = Carbamyl phosphate synthesis in Neurospora crassa. I. Preliminary characterization of arginine-specific carbamyl phosphokinase | journal = Biochim. Biophys. Acta | volume = 107 | pages = 44–53 | pmid = 5857367 | issue = 1 | doi=10.1016/0304-4165(65)90387-9| hdl = 2027.42/31986 | url = https://deepblue.lib.umich.edu/bitstream/2027.42/31986/1/0000028.pdf| hdl-access = free }}
{{cite journal | author = Glasziou KT | date = 1956 | title = The metabolism of arginine in Serratia marcescens. II Carbamyladenosine diphosphate phosphoferase | journal = Aust. J. Biol. Sci. | volume = Sci. | issue = 2 | pages = 253–262 | doi = 10.1071/BI9560253 | doi-access = free }}
{{cite journal |vauthors=Jones ME, Spector L, Lipmann F | date = 1955 | title = Carbamyl phosphate, the carbamyl donor in enzymatic citrulline synthesis | journal = J. Am. Chem. Soc. | volume = 77 | issue = 3 | pages = 819–820 | doi = 10.1021/ja01608a101 }}
{{cite journal |vauthors=Srivenugopal KS, Adiga PR | date = 1981 | title = Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase) | journal = J. Biol. Chem. | volume = 256 | pages = 9532–41 | pmid = 6895223 | issue = 18 | doi = 10.1016/S0021-9258(19)68795-8 | doi-access = free }}

Category:EC 2.7.2

Category:Enzymes of known structure