Carbamate kinase

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In enzymology, a carbamate kinase (EC 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.


  • IUBMB entry for
  • BRENDA references for (Recommended.)
  • PubMed references for
  • PubMed Central references for
  • Google Scholar references for
  • Bishop SH, Grisolia S (1966). "Crystalline carbamate kinase". Biochim. Biophys. Acta. 118: 211&ndash, 5. PMID 4959296.
  • Davis RH (1965). "Carbamyl phosphate synthesis in Neurospora crassa. I. Preliminary characterization of arginine-specific carbamyl phosphokinase". Biochim. Biophys. Acta. 107: 44&ndash, 53. PMID 5857367.
  • Glasziou KT (1956). "The metabolism of arginine in Serratia marcescens. II Carbamyladenosine diphosphate phosphoferase". Aust. J. Biol. Sci.: 253&ndash, 262.
  • Jones ME, Spector L and Lipmann F (1955). "Carbamyl phosphate, the carbamyl donor in enzymatic citrulline synthesis". J. Am. Chem. Soc. 77: 819&ndash, 820.
  • 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: 9532&ndash, 41. PMID 6895223.

External links

The CAS registry number for this enzyme class is 9026-69-1.

Gene Ontology (GO) codes