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David Leys, PhD


Personal profile


David did both his undergraduate and postgraduate studies at the University of Ghent, Belgium, where he obtained a PhD in Biochemistry in 2000. Following a brief postdoctoral fellowship at the University of Edinburgh with Prof. S.K. Chapman on a Belgian Government fellowship, David joined the University of Leicester Biochemistry department in 2001 as a tenure track research fellow. He obtained a Royal Society University Research fellowship in 2003 (until 2011) and a EMBO YIP award in 2004. He moved to Manchester in 2005 to take a position as Reader in Molecular Enzymology. He was made Professor in Structural Biology in 2010, and was awarded the 2015 Wain medal for his research in biochemistry.

David is interested in the atomic basis of life, and uses structural biology combined with a range of biochemical techniques to understand how structure relates to function in biology.  David's research has focused on elucidation of novel mechanisms of interprotein electron transfer, the evolution of substrate channelling strategies, enzymatic H-tunnelling reactions, and the basis of organohalide respiration. His group recently uncovered new roles for vitamins B2 and B12.

In recent years, David has established an independent research group with funding from BBSRC, ERC, the Royal Society and industry, currently comprising ~4 postdoctoral scientists and 5 PhD students working in the area of protein structure-function analysis.

Research interests

Macromolecular structure and function

We use x-ray crystallography to address how macromolecular structure determines function. We focus on several aspects: how do proteins interact with other macromolecules (RNA, DNA, proteins) or their substrates?  How do enzymes work, particularly those for which mechanistic insight is lacking? Protein structures also form the basis of protein engineering and for structure-based drug design. We are studying proteins of biotechnological interest (ie biofuel production) to provide for the much needed structural insight into these enzymes.


Mechanistic enzymology at the atomic level           Detailed insights into transcriptional regulation


Hot of the press: new paper in Nature on a PAS enzyme

Recent publications:

1. Karl A.P. Payne, Mark D. White, Karl Fisher, Basile Khara, Samuel S. Bailey, David Parker, Nicholas J.W. Rattray, Drupad K. Trivedi, Royston Goodacre, Rebecca Beveridge, Perdita Barran, Stephen E.J. Rigby, Nigel S. Scrutton, Sam Hay, David Leys (2015) New cofactor supports reversible decarboxylation of α,β-unsaturated acids via 1,3-dipolar cycloaddition chemistry. Nature 522, 497–501
2. Mark D. White, Karl A.P. Payne, Karl Fisher, Stephen A. Marshall, David Parker, Nicholas J.W. Rattray, Drupad K. Trivedi, Royston Goodacre, Stephen E.J. Rigby, Nigel S. Scrutton, Sam Hay, David Leys (2015) UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis. Nature 522, 502–507
3. Karl A.P. Payne, Carolina P. Quezada, Karl Fisher, Mark S. Dunstan, Fraser A. Collins, Hanno Sjuts, Colin Levy, Sam Hay, Stephen E.J. Rigby, David Leys (2015) Reductive dehalogenase structure suggest a mechanism for B12-dependent dehalogenation. Nature 517, 513-516
Mary Ortmayer, Pierre Lafite, Binuraj RK Menon, Tewes Tralau, Karl Fisher, Lukas Denkhaus, Nigel S Scrutton, Stephen EJ Rigby, Andrew W Munro, Sam Hay, David Leys (2016) An oxidative N-demethyase reveals PAS transition from ubiquitous sensor to enzyme. Nature doi:10.1038/nature20159


Expertise related to UN Sustainable Development Goals

In 2015, UN member states agreed to 17 global Sustainable Development Goals (SDGs) to end poverty, protect the planet and ensure prosperity for all. This person’s work contributes towards the following SDG(s):

  • SDG 3 - Good Health and Well-being
  • SDG 7 - Affordable and Clean Energy
  • SDG 13 - Climate Action
  • SDG 14 - Life Below Water

Research Beacons, Institutes and Platforms

  • Biotechnology
  • Sustainable Futures
  • Manchester Institute of Biotechnology


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Collaborations and top research areas from the last five years

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