| carbamate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.2.2 | ||||||||
| CAS no. | 9026-69-1 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a carbamate kinase (EC 2.7.2.2) is an enzyme that catalyzes the chemical reaction
- ATP + NH3 + CO2 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 1B7B, 1E19, and 2E9Y.
References
- Bishop SH, Grisolia S (1966). "Crystalline carbamate kinase". Biochim. Biophys. Acta. 118 (1): 211–5. doi:10.1016/s0926-6593(66)80163-7. PMID 4959296.
- Davis RH (1965). "Carbamyl phosphate synthesis in Neurospora crassa. I. Preliminary characterization of arginine-specific carbamyl phosphokinase" (PDF). Biochim. Biophys. Acta. 107 (1): 44–53. doi:10.1016/0304-4165(65)90387-9. hdl:2027.42/31986. PMID 5857367.
- Glasziou KT (1956). "The metabolism of arginine in Serratia marcescens. II Carbamyladenosine diphosphate phosphoferase". Aust. J. Biol. Sci. Sci. (2): 253–262. doi:10.1071/BI9560253.
- Jones ME, Spector L, Lipmann F (1955). "Carbamyl phosphate, the carbamyl donor in enzymatic citrulline synthesis". J. Am. Chem. Soc. 77 (3): 819–820. doi:10.1021/ja01608a101.
- Srivenugopal KS, Adiga PR (1981). "Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase)". J. Biol. Chem. 256 (18): 9532–41. PMID 6895223.