Carbamate kinase
| Carbamate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.2.2 | ||||||||
| CAS no. | 9026-69-1 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Carbamate kinase (EC 2.7.2.2) is an enzyme that catalyzes a reversible chemical reaction:
The enzyme characterised from Streptococcus faecalis,[1] Serratia marcescens,[2] Neurospora crassa,[3] and Lathyrus sativus[4] transfers a phosphate group between adenosine triphosphate (ATP) and adenosine diphosphate (ADP). In the forward direction shown, ammonia and carbonic acid are components of the reaction, giving water and carbamoyl phosphate as products. However, an important function of the enzyme is to make ATP from ADP.[5]
This enzyme is a transferase, specifically one 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.[5]
Structural studies
As of late 2007, three structures have been solved for this class of enzymes, with PDB accession codes PDB: 1B7B, PDB: 1E19, and PDB: 2E9Y. The first was published in 1966.[6]
References
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- 1 2 Enzyme 2.7.2.2 at KEGG Pathway Database.
- ↑ 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.
Categories: