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.