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 ReferencesUrease of Corynebacterium glutamicum: organization of corresponding genes and investigation of activity. Nolden L FEMS microbiology letters 2000 Aug 1510930756
Characterization of the urease operon of Brucella abortus and assessment of its role in virulence of the bacterium. Sangari FJ Infection and immunity 2007 Feb17101645
Proteus mirabilis urease: nucleotide sequence determination and comparison with jack bean urease. Jones BD Journal of bacteriology 1989 Dec2687233
Organization of Ureaplasma urealyticum urease gene cluster and expression in a suppressor strain of Escherichia coli. Neyrolles O Journal of bacteriology 1996 Feb8550495
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 1115542602
Shuttle cloning and nucleotide sequences of Helicobacter pylori genes responsible for urease activity. Labigne A Journal of bacteriology 1991 Mar2001995
Web linksModel of K. aerogenes urease activation
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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.