dr. A.M.W.H. Thunnissen
Exploring enzyme structure for biocatalyst design
Natural biocatalysts offer great advantages for “green” production of fine chemicals and pharmaceuticals, a potential which is further enhanced by the rational design of variants with improved or new functions. Rational biocatalyst design critically relies on a detailed knowledge of the 3D structure of the biocatalyst and of the interactions that substrates or inhibitors make in the active site. My research interests and expertise focus on exploring the 3D structures of various biotechnologically relevant enzymes, using protein X-ray crystallography and modeling tools, with the aim to characterize and understand structure-activity relationships and to guide engineering initiatives towards tailored enzymes with altered or improved activity, selectivity and stability. Enzymes of interest include ammonia-lyases, tautomerases, transaminases and cytochrome P450s. Important challenges are to obtain high resolution crystallographic “snapshots” of relevant catalytic states and to integrate X-ray crystallography with computational modeling and molecular dynamics simulations in order to provide a more complete dynamic picture of the enzyme structure and its relation to molecular recognition and catalytic function.
|Laatst gewijzigd:||14 april 2017 08:38|