Use of virus-like particles to study the influence of molecular crowding on biocatalysis

During my PhD I focused on understanding enzyme evolution in bacteria, using enzyme purification, characterisation and strucutre-function studies. My new project involves studying the impact of molecular crowding on enzyme activity in virus-like-particles, using isoprenoid pathway enzymes.

​Lygie completed her Master’s degree in life sciences and applied statistics at Agrocampus Ouest (Rennes, France) in 2012. After moving to Australia, she worked as a pharmaceutical patent searcher in Sydney for two years. She completed her PhD in 2018 under the supervision of Dr Colin Scott at CSIRO (Biocatalysis Team) and ANU (Easton lab, Canberra). Lygie’s PhD focused on studying the enzymatic basis of bacterial resistance to atrazine, a herbicide, and understanding the evolution of new functions in bacteria. She is now a Postdoctoral Research Fellow in the Vicker’s group, working on understanding biocatalysis in crowded environments using Virus-Like Particles.

Key Publications

Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841. Plos One 13:e0192736. 2018. Esquirol L., T. Peat, M. Wilding, D. Lucent, N. French, C. Hartley, J. Newman, and C. Scott.

An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. J Biol Chem jbc RA118.001996. 2018. Esquirol L., T. Peat, M. Wilding, J.-W. Liu, N. French, C. Hartley, H. Onagi, T. Nebl, C. Easton, J. Newman, and C. Scott.

A novel decarboxylating amidohydrolase involved in avoiding metabolic dead ends during cyanuric acid catabolism in Pseudomonas sp. strain ADP. Esquirol L., T. Peat, M. Wilding, C. Hartley, C. Scott. PLOS ONE 13(11): e0206949. 2018.