Retracing the evolution of enzyme regulation
Fiona Given - PhD Oral
Biomolecular Interaction Centre, PhD student with Emily Parker’s group
Time & Place
Thu, 13 Dec 2018 11:00:00 NZDT in Room 446, Jack Erskine Buidling
All are welcome
α-isopropylmalate synthase (IPMS) catalyses the first committed step in the biosynthesis of leucine in microorganisms and some plants. IPMS is allosterically inhibited by leucine, thus controlling flux through the pathway. The mode of allostery of this enzyme is not well understood; X-ray crystal structures of IPMS showed no major conformational changes upon leucine binding. Of additional interest are homologous enzymes catalyse a similar reaction in other biosynthetic pathways but lack the structural framework that enables allosteric regulation, thus providing a way to explore catalysis and allostery independently.
In this project, a combination of biochemical and computational techniques was employed to investigate the mechanism of allostery, and the evolution of this mechanism, in IPMS from Neisseria meningitidis and similar enzymes.