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Issue 3, 2009
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Interplay of metal ions and urease

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Urease, the first enzyme to be crystallized, contains a dinuclear nickel metallocenter that catalyzes the decomposition of urea to produce ammonia, a reaction of great agricultural and medical importance. Several mechanisms of urease catalysis have been proposed on the basis of enzyme crystal structures, model complexes, and computational efforts, but the precise steps in catalysis and the requirement of nickel versus other metals remain unclear. Purified bacterial urease is partially activated via incubation with carbon dioxide plus nickel ions; however, in vitro activation also has been achieved with manganese and cobalt. In vivo activation of most ureases requires accessory proteins that function as nickel metallochaperones and GTP-dependent molecular chaperones or play other roles in the maturation process. In addition, some microorganisms control their levels of urease by metal ion-dependent regulatory mechanisms.

Graphical abstract: Interplay of metal ions and urease

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Publication details

The article was received on 19 Feb 2009, accepted on 23 Mar 2009 and first published on 09 Apr 2009

Article type: Critical Review
DOI: 10.1039/B903311D
Citation: Metallomics, 2009,1, 207-221

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    Interplay of metal ions and urease

    E. L. Carter, N. Flugga, J. L. Boer, S. B. Mulrooney and R. P. Hausinger, Metallomics, 2009, 1, 207
    DOI: 10.1039/B903311D

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