Subsystem: Urease subunits
This subsystem's description is:
Urease is a nickel metallo enzyme that catalyzes the degredation of urea to ammonia and carbamine acid. The latter compound decomposes spontaneously to form a second molecule of ammonia and carbon dioxide.
The enzyme consists of three subunits, alpha, beta and gamma. This heterotrimer forms multimers, mainly trimers.
UreA and UreB = needed for the association of the urease heterotrimer UreABC
UreC = catalytic domain containing an active site with a Ni2+ center complexed by a carbamylated lysine
UreE = metallochaperone assisting the insertion of a Ni2+ ion in the active site of urease
UreF = modulates activation of urease by eliminating Ni2+ irons from the non-carbamylated protein
UreG = GTP hydrolase needed for the assembly of the Ni2+ metallocenter of urease
UreD = needed for the assembly of the Ni2+ metallocenter
Nomenclature for urease subunits in Helicobacter might differ from this SS
For more information, please check out the description and the additional notes tabs, below
Literature References | Urease of Corynebacterium glutamicum: organization of corresponding genes and investigation of activity. Nolden L FEMS microbiology letters 2000 Aug 15 | 10930756 | Characterization of the urease operon of Brucella abortus and assessment of its role in virulence of the bacterium. Sangari FJ Infection and immunity 2007 Feb | 17101645 | Proteus mirabilis urease: nucleotide sequence determination and comparison with jack bean urease. Jones BD Journal of bacteriology 1989 Dec | 2687233 | Organization of Ureaplasma urealyticum urease gene cluster and expression in a suppressor strain of Escherichia coli. Neyrolles O Journal of bacteriology 1996 Feb | 8550495 | UreG, a chaperone in the urease assembly process, is an intrinsically unstructured GTPase that specifically binds Zn2+. Zambelli B The Journal of biological chemistry 2005 Feb 11 | 15542602 | Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity. Labigne A Journal of bacteriology 1991 Mar | 2001995 |
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Web links | Model of K. aerogenes urease activation |
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Diagram | Functional Roles | Subsystem Spreadsheet | Description | Additional Notes | |||||||||
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Urease is a nickel metallo enzyme that catalyzes the degredation of urea to ammonia and carbamine acid. The latter compound decomposes spontaneously to form a second molecule of ammonia and carbon dioxide. The enzyme consists of three subunits, alpha, beta and gamma. This heterotrimer forms multimers, mainly trimers. UreA and UreB = needed for the association of the urease heterotrimer UreABC UreC = catalytic domain containing an active site with a Ni2+ center complexed by a carbamylated lysine UreE = metallochaperone assisting the insertion of a Ni2+ ion in the active site of urease UreF = modulates activation of urease by eliminating Ni2+ irons from the non-carbamylated protein UreG = GTP hydrolase needed for the assembly of the Ni2+ metallocenter of urease UreD = needed for the assembly of the Ni2+ metallocenter Nomenclature for urease subunits in Helicobacter might differ from this SS Sodalis glossinidius str. 'morsitans'has only remnants of the alphs and beta subunit genes Urease is a virulence factor that plays a role in the resistance of Brucella and other pathogens to low pH conditions. Urease-producing strains were found to be resistant in vitro to strong acid conditions in the presence of urea, while urease-negative mutants were susceptible to acid treatment. Similarly, the urease-negative mutants were killed more efficiently than the urease-producing strains during transit through the stomach. These results suggested that urease protects brucellae during their passage through the stomach when the bacteria are acquired by the oral route, which is the major route of infection in human brucellosis. note: Brucella have 2 ure gene clusters ure1 and ure2 (an acid-activated urea transporter (low-affinity urea transporter) and a nickel ECF transporter follow the ure2 gene cluster) In H.pylori UreI (located within the ure gene cluster) functions as a H+-gated urea channel regulating cytoplasmic urease that is essential for gastric survival and colonization. |