D
IPR011612

Urease alpha-subunit, N-terminal domain

InterPro entry
Short nameUrease_alpha_N_dom
Overlapping
homologous
superfamilies
 

Description

Urease (urea amidohydrolase,
3.5.1.5
) catalyses the hydrolysis of urea to form ammonia and carbamate. The subunit composition of urease from different sources varies
[1]
, but each holoenzyme consists of four structural domains
[3]
: three structural domains and a nickel-binding catalytic domain common to amidohydrolases
[2]
. Urease is unique among nickel metalloenzymes in that it catalyses a hydrolysis rather than a redox reaction. In Helicobacter pylori, the gamma and beta domains are fused and called the alpha subunit (
IPR008223
). The catalytic subunit (called beta or B) has the same organisation as the Klebsiella alpha subunit. Jack bean (Canavalia ensiformis) urease has a fused gamma-beta-alpha organisation (
IPR008221
).

The N-terminal domain is a composite domain and plays a major trimer stabilising role by contacting the catalytic domain of the symmetry related alpha-subunit
[3]
.

References

1.Molecular biology of microbial ureases. Mobley HL, Island MD, Hausinger RP. Microbiol. Rev. 59, 451-80, (1995). View articlePMID: 7565414

2.An evolutionary treasure: unification of a broad set of amidohydrolases related to urease. Holm L, Sander C. Proteins 28, 72-82, (1997). View articlePMID: 9144792

3.The crystal structure of urease from Klebsiella aerogenes. Jabri E, Carr MB, Hausinger RP, Karplus PA. Science 268, 998-1004, (1995). View articlePMID: 7754395

Cross References

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