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Rudolf K. Allemann is a Distinguished Research Professor and head of Chemical Biology at Cardiff University. His research focuses on the elucidation of enzymatic mechanisms by studying terpene cyclases such as aristolochene synthase, germacrene-A synthase and delta-cadinene synthase and dihydrofolate reductase variants from different species, eg. Escherichia coli and Thermotoga maritima.

Education
Allemann earned his Dipl. Chem from the ETH Zurich. He recieved his PhD from Harvard University and the ETH Zurich for research into the use of evolutionary guidance as a tool for organic synthesis before completing his habilitation at ETH Zurich.

Career
In 1989 Allemann secured a position as a postdoctoral fellow at the National Institute for Medical Research, where he later became a Staff Scientist before returning to the ETH Zurich in 1992 as a research group leader in Biological Chemistry. He completed his habilitation in 1999 and then joined the University of Birmingham, first as a Senior Lecturer and then Professor of Chemical Biology. Since 2005 he has been a Distinguished Research Professor at Cardiff University.

Enzyme Mechanisms
The Allemann group conducts fundamental research to try to uncover the physical basis of the exceptional efficiency of enzyme catalysis. Two different classes of enzymes are studied, the first are terpene cyclases that convert linear isoprene-derived chains to the diverse spectrum of terpene and terpenoid natural products. Some terpenoid products are often used as insect pheromones and are examples of entirely natural insecticides (See verbenone or germacrene).

The second class are Dihydrofolate reductase (DHFR) enzymes, some of which which are the targets of antibiotics and anticancer drugs (methotrexate). The mechanism of action of DHFR enzymes is a hotly-debated topic with some arguing that enzyme motions promote hydride transfer and others suggesting enzyme dynamics are not necessary to explain experimental results. Recent experiments in the Allemann laboratory failed to find evidence of the coupling of protein motions to hydride transfer.