Rational Design of Protein Cages for Alternative Enzymatic Functions
作者
Nicholas Marshall,Kyle D. Miner,Tiffany D. Wilson,Yi Lu
标识
DOI:10.1002/9781118571811.ch5
摘要
This chapter discusses several studies from various classes of metalloenzymes, in which a functional property of the protein, such as electron transfer or catalysis, was either predictably improved or completely altered, or cases where new functionality was engineered into a protein scaffold by modifying the protein cage, as opposed to the catalytic site itself. The chapter focuses on inorganic chemistry, special emphasis is given to metalloenzymes and, where available, the methods used in each study in order to serve as a guide for future studies in metalloenzyme design and engineering. The recent progress in rational design of protein cages for alternative enzymatic functions, and in particular, studies that have strived to predictably alter or impart new functionality to metalloenzymes, have led to important advances in our knowledge of how metalloenzymes work and have set the groundwork for producing designer proteins with a selected function and high rates of catalysis.