Per Jemth, Associate Professor

Enzyme Structure and Mechanism

In the living part of nature, chemical reactions are normally catalyzed. Most of these reactions have such a high activation energy that they do not occur at all unless the activation energy is lowered by a catalyst. By enhancing certain chemical reactions at the right time in the right place, the catalysts control all vital chemical reactions in an organism. Natureís catalysts are called enzymes and they are catalytic proteins. Enzymes display a seemingly unlimited ability to facilitate various chemical reactions. Having this capacity, enzymes are literally the executive committee of life on earth.

During my postdoc in Ulf Lindahl's group my interest in enzyme mechanism was focused on enzymes involved in the metabolism of heparan sulfate, for example heparanase and O-sulfotransferases. Owing to the heterogeneity of heparan sulfate and probblems in obtaining pure oligosaccharides, it is difficult to obtain defined substrates for the different enzymes. In vitro-generated heparan sulfate libraries and oligosaccharides were used to identify different substrates and measure substrate specificities.

During my graduate studies I worked on the catalytic mechanism and/or evolution of glutathione transferase, glyoxalase I, and glyoxalase II.