Back يورياز Arabic Ureaza BS Ureasa Catalan Wreas Welsh Urease Danish Urease German Ureasa Spanish Ureasaren proba Basque اورهآز Persian Ureaasi Finnish
 3D model of urease from Klebsiella aerogenes, two Ni2+-ions are shown as green spheres.[1] | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| EC no. | 3.5.1.5 | ||||||||
| CAS no. | 9002-13-5 | ||||||||
| 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 | ||||||||
| |||||||||
Ureases (EC 3.5.1.5), functionally, belong to the superfamily of amidohydrolases and phosphotriesterases.[2] Ureases are found in numerous Bacteria, Archaea, fungi, algae, plants, and some invertebrates. Ureases are nickel-containing metalloenzymes of high molecular weight.[3] Ureases are distinct from Urecases are important in degrading avian faecal matter, which is rich in uric acid, the breakdown product of which is urea, which is then degraded by urease as described here.
These enzymes catalyze the hydrolysis of urea into carbon dioxide and ammonia:
- (NH2)2CO + H2O CO2 + 2NH3
The hydrolysis of urea occurs in two stages. In the first stage, ammonia and carbamic acid are produced. The carbamate spontaneously and rapidly hydrolyzes to ammonia and carbonic acid. Urease activity increases the pH of its environment as ammonia is produced, which is basic.
- ^ PDB: 2KAU; Jabri E, Carr MB, Hausinger RP, Karplus PA (May 1995). "The crystal structure of urease from Klebsiella aerogenes". Science. 268 (5213): 998–1004. Bibcode:1995Sci...268..998J. doi:10.1126/science.7754395. PMID 7754395.
- ^ Holm L, Sander C (1997). "An evolutionary treasure: unification of a broad set of amidohydrolases related to urease". Proteins. 28 (1): 72–82. CiteSeerX 10.1.1.621.2752. doi:10.1002/(SICI)1097-0134(199705)28:1<72::AID-PROT7>3.0.CO;2-L. PMID 9144792. S2CID 38845090.
- ^ Krajewska B, van Eldik R, Brindell M (13 August 2012). "Temperature- and pressure-dependent stopped-flow kinetic studies of jack bean urease. Implications for the catalytic mechanism". Journal of Biological Inorganic Chemistry. 17 (7): 1123–1134. doi:10.1007/s00775-012-0926-8. PMC 3442171. PMID 22890689.