title: Biosynthesis of the urease metallocenter.
abstract: Metalloenzymes often require elaborate metallocenter assembly systems to create functional active sites. The medically important dinuclear nickel enzyme urease provides an excellent model for studying metallocenter assembly. Nickel is inserted into the urease active site in a GTP-dependent process with the assistance of UreD/UreH, UreE, UreF, and UreG. These accessory proteins orchestrate apoprotein activation by delivering the appropriate metal, facilitating protein conformational changes, and possibly providing a requisite post-translational modification. The activation mechanism and roles of each accessory protein in urease maturation are the subject of ongoing studies, with the latest findings presented in this minireview.
authors.affiliation: Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
authors.forename: Mark A
authors.initials: MA
authors.lastname: Farrugia
authors.forename: Lee
authors.initials: L
authors.lastname: Macomber
authors.forename: Robert P
authors.initials: RP
authors.lastname: Hausinger
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis / Q000737:chemistry*; D020134:Catalytic Domain; D003067:Coenzymes / Q000096:biosynthesis / Q000737:chemistry; D004789:Enzyme Activation; D006801:Humans; D007501:Iron / Q000737:chemistry; D008958:Models, Molecular; D009532:Nickel / Q000737:chemistry*; D010940:Plant Proteins / Q000096:biosynthesis / Q000737:chemistry; D014510:Urease / Q000096:biosynthesis / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D003067:Coenzymes; D010940:Plant Proteins; D009532:Nickel; D007501:Iron; D014510:Urease
keywords: Biosynthesis; Chaperone Chaperonin; GTPase; Metalloenzymes; Nickel; Urease
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