About Associate Professor Charles Collyer

I am interested in the biochemical mechanisms of enzyme action and rich information is derived from X-ray structures of enzyme-inhibitor complexes.

I am a specialist in Structural Biology focusing on enzymes with an interest in developing inhibitors which have potential for use in clinical treatments. My research career began with work on the structures of ligand/protein complexes of the enzyme xylose isomerase and this was a key element of an industry-based protein engineering initiative funded by ICI. This project based at Imperial College, London, aimed to enhance the efficiency of these enzymes in bioreactors used in the production of high fructose corn syrupsMore structural work followed at Pharmacia SpA in Italy leading to the discovery of a new class of serine protease inhibitors which attach themselves covalently at two positions in the active site of the enzyme. These novel inhibitors were developed as drug leads for the treatment of emphysema. In 1995 I joined Mitchell Guss at the University of Sydney and collaborated with him to determine the first ever structure of a sulfatase. Novel features were observed in this enzyme structure which were consistent with only one of many previously postulated chemical mechanisms. My interest in enzyme structure and mechanism continued in a collaboration with Matthew Templeton from HortResearch NZ. This included the study of transition-state like inhibitors of ornithine transcarbamoylase and the publication of this work included for the first time a discussion of the chirality of the transition state. These non-covalent inhibitors are the tightest known for this class of enzyme and are models for the design of drug leads for the treatment of cancer and malaria.

Assoc Prof Charles Collyer is a researcher at the School of Life and Environmental Sciences
For more information about Assoc Prof Charles Collyer, refer to his Academic Profile Online