Ren Dobson in lab high-res

ProfessorRenwick Dobson

Julius von Haast 620
Internal Phone: 95145

Qualifications & Memberships

Research Interests

Research in our lab focuses on the structure, function and inhibition of key enzymes involved in infection and disease. We are also interested in the evolution of enzyme function, and conversely its design and manipulation.

We study a variety of enzymes: from those responsible for the biosynthesis of amino acids, in particular lysine, since these are validated drug targets; to glycolytic enzymes, such as pyruvate kinase, since these are tractable model systems to understand enzyme allostery. The list is ever increasing.

A common theme in the lab is the role protein-protein interactions in a variety of biological systems, mostly derived from bacteria, but more recently including eukaryotic proteins involved in cancer, where we hope to address the twin problems of how and why proteins form complexes and the functional consequences of these associations.

Recent Publications

  • Adams LE., Rynkiewicz P., Babbitt GA., Mortensen JS., North RA., Dobson RCJ. and Hudson AO. (2020) Comparative Molecular Dynamics Simulations Provide Insight Into Antibiotic Interactions: A Case Study Using the Enzyme L,L-Diaminopimelate Aminotransferase (DapL). Frontiers in Molecular Biosciences 7
  • Coombes D., Davies JS., Newton-Vesty MC., Horne CR., Setty TG., Subramanian R., Moir JWB., Rosmarie Friemann X., Panjikar S. and Griffin MDW. (2020) The basis for non-canonical ROK family function in the N-acetylmannosamine kinase from the pathogen Staphylococcus aureus. Journal of Biological Chemistry 295(10): 3301-3315.
  • Cree SL., Chua EW., Crowther J., Dobson RCJ. and Kennedy MA. (2020) G-quadruplex structures bind to EZ-Tn5 transposase. Biochimie 177: 190-197.
  • Horne CR., Kind L., Davies JS. and Dobson RCJ. (2020) Cover Image, Volume 88, Issue 5. Proteins: Structure, Function, and Bioinformatics 88(5)
  • Horne CR., Kind L., Davies JS. and Dobson RCJ. (2020) On the structure and function of Escherichia coli YjhC: An oxidoreductase involved in bacterial sialic acid metabolism. Proteins: Structure, Function and Bioinformatics 88(5): 654-668.