Single Enzyme Kinetics: A Study of the Yeast Enzyme Candida Antarctica Lipase B

Abstract

Enzymes are a class of (bio)molecules that function as catalysts of (bio)chemical reactions. They highly accelerate the rate of (bio)chemical reactions (Fersht 1985). During the past decades, our knowledge about enzymes has greatly increased. Enzymes are almost always proteins which are very complex structures having many degrees of motional freedom. Much insight into the structures of these and other biomolecules is obtained by X-ray crystallography (Fersht 1985), nuclear magnetic resonance (NMR; Matthews and Van Holde (1996)), and molecular dynamics simulations (MDS) studies (Jensen et al. 2002). Most of the information available on enzymes has been primarily obtained by means of ensemble measurements. Unfortunately, these data do not give further insight in the static and dynamic heterogeneities. This is important as enzymes are not static molecules. The primary structure can fold into many slightly different conformations with different chemical activity (Frauenfelder et al. 1991). A well-studied process, for example, is the binding of carbon monoxide (CO) to myoglobin (Mb).