1 Biosynthesis of the Urease Metallocenter

Metalloenzymes often require elaborate metallocenter assembly systems to create functional active sites. The medicallyimportant, 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 posttranslational modification. The activation mechanism and roles of each accessory protein in urease maturation is the subject of ongoing studies, with the latest findings presented in this review.