Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA.
J Biol Chem. 2013 May 10;288(19):13178-85. doi: 10.1074/jbc.R112.446526. Epub 2013 Mar 28.
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.
金属酶通常需要精心设计的金属中心组装系统来创建功能性的活性位点。医学上重要的双核镍酶脲酶为研究金属中心组装提供了一个极好的模型。镍在 GTP 依赖性过程中被插入脲酶活性部位,辅助蛋白为 UreD/UreH、UreE、UreF 和 UreG。这些辅助蛋白通过递呈合适的金属、促进蛋白质构象变化,并可能提供必要的翻译后修饰,来协调脱辅基蛋白的激活。脲酶成熟过程中每种辅助蛋白的激活机制和作用是正在进行的研究课题,本综述介绍了最新的发现。