Skip to main navigation Skip to main content
The University of Southampton
Biological Sciences

Enzyme suicide and cofactor cannibalism for the sake of thiamin biosynthesis in yeast Seminar

Professor Steven Ealick
Time:
17:00
Date:
21 November 2011
Venue:
Building 85, seminar room 2207

For more information regarding this seminar, please telephone Margaret Miles on 023 8959 3349 or email m.s.miles@southampton.ac.uk .

Event details

The topic of this lecture will be thiamin biosynthesis in eukaryotes, the details of which are just beginning to emerge.

Steven E. Ealick is the William T. Miller Professor in the Department of Chemistry and Chemical Biology at Cornell University. Professor Ealick has a long standing interest in protein crystallography and has made important contributions to studies on purine and pyrimidine metabolism, thiamin biosynthesis, and polyamine biosynthesis, among others. In addition, Professor Ealick has been actively involved in the development of synchroton radiation facilities for structural biology, first as the director of MacCHESS (1991-2000) and then as the director of NE-CAT (2000-present). In collaboration with Professor Tadhg Begley, Professor Ealick has unraveled most of the mechanistic details of thiamin biosynthesis in prokaryotes.

The topic of this lecture will be thiamin biosynthesis in eukaryotes, the details of which are just beginning to emerge. While biosynthesis of thiamin phosphate in B. subtilis requires nine gene products, only three gene products are required in yeast. These three gene products display fascinating biochemistry and their study has raised intriguing new questions about the role of thiamin.

Speaker information

Professor Steven E Ealick , Department of Chemistry and Chemical Biology, Cornell University, USA. The Ealick group studies the structure and function of proteins using X-ray crystallography. The main goals of the research are to understand the structural basis of enzyme mechanism, to design small molecules of potential chemotherapeutic importance, to study the basis of protein evolution, and to expand the tools available to macromolecular crystallographers.

Privacy Settings