Carbamate kinase

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
Search PMC articles PubMed articles NCBI proteins

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

ATP + NH₃ + CO₂${\displaystyle \rightleftharpoons }$ 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 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. Bibcode:1955JAChS..77..819J. 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. doi: 10.1016/S0021-9258(19)68795-8 . PMID   6895223.