Understanding of important enzyme-catalysed reactions, using a combination of the following techniques: synthesis of enzymatic substrates and inhibitors, isotope labelling experiments, enzyme purification and enzyme kinetics. Major areas of interest are enzymes involved in the bacterial degradation of aromatic compounds, and enzymes involved in bacterial cell wall peptidoglycan biosynthesis, as targets for the development of novel antibacterial agents.

Selective inhibition of carotenoid cleavage dioxygenases: phenotypic effects on shoot branching. M.J. Sergeant, J-J. Li, C. Fox, N. Brookbank, D. Rea, T.D.H. Bugg, A.J. Thompson, J. Biol. Chem., 2009, 284, 5257-5264. Kinetic characterization of lipid II-Ala:alanyl-tRNA ligase MurN from Streptococcus pneumoniae using semi-synthetic aminoacyl-lipid II substrates. G. De Pascale, A.J. Lloyd, J.A. Schouten, A.M. Gilbey, D.I. Roper, C.G. Dowson, T.D.H. Bugg, J. Biol. Chem., 2008, 283, 34571-34579. Characterization of tRNA-dependent peptide bond formation by MurM in the synthesis of Streptococcus pneumoniae peptidoglycan. A.J. Lloyd, A.M. Gilbey, A.M. Blewett, G. De Pascale, A. de Zoeiby, R.C. Levesque, A.C. Catherwood, A. Tomasz, T.D.H. Bugg, D.I. Roper, C.G. Dowson, J. Biol. Chem., 2008, 283, 6402-6417. Evidence from mechanistic probes for distinct hydroperoxide rearrangement mechanisms in the intradiol and extradiol catechol dioxygenases. M. Xin, T.D.H. Bugg, J. Am. Chem. Soc., 2008, 130, 10422-10430.