Carbamate kinase

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carbamate kinase
Identifiers
EC number2.7.2.2
CAS number9026-69-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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[edit]

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

References[edit]

  • 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. PMID 5857367.
  • Glasziou KT (1956). "The metabolism of arginine in Serratia marcescens. II Carbamyladenosine diphosphate phosphoferase". Aust. J. Biol. Sci. Sci.: 253–262.
  • 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.