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Dr Louis Luk

Dr Lousi LukLouis Luk is a research associate working under the supervision of Professor R. Allemann, on a BBSRC-funded project entitled “Protein-ligand coupled motions in DHFR catalysis”.  His past research experience includes his Ph.D. studies at the University of British Columbia and postdoctoral research at the University of Chicago. He has extensive experience in peptide synthesis and native chemical ligation, and has also provided evidence for the involvement of a Cope rearrangement in the biosynthesis of ergot alkaloids. His current research focuses on understanding the functional role(s) of protein dynamics in catalysis and designing novel inhibitors of dihydrofolate reductase, an enzyme that plays central role in DNA and amino acid biosynthesis.

Publications:

  • Luk, L.Y.P., Ruiz-Pernia, J.J., Dawson, W.M., Roca, M., Loveridge, E.J., Glowacki, D.R., Harvey, J.N., Mulholland, A.J., Tuñón, I., Moliner, V., Allemann, R.K. Differences in reactivity in dihydrofolate reductase are linked to dynamics. Proc. Natl. Acad. Science 2013, submitted.
  • Guo, J., Loveridge, E.J., Luk, L.Y.P., Allemann, R.K. Effect of dimerisation on catalysis by dihydrofolate reductase. Biochemistry 2013, accepted.
  • Mahmoodi, N., Qi, Q., Luk, L.Y.P., Tanner, M.E. Rearrangements in the mechanisms of the indole alkaloid prenyltransferases. Pure Appl. Chem. 2013, accepted.
  • Luk, L.Y.P., Qian, Q., Tanner, M.E. A Cope rearrangement in the reaction catalyzed by dimethylallyltryptophan synthase? J. Am. Chem. Soc. 2011, 133, 12342-12345; DOI: 10.1021/ja2034969.
  • Luk, L.Y.P., Tanner, M.E. Mechanism of dimethylallyltryptophan synthase: evidence for a dimethylallyl cation intermediate in an aromatic prenyltransferase reaction. J. Am. Chem. Soc. 2009, 131, 13932-13933; DOI: 10.1021/ja906485u.
  • Luk, L.Y.P., Bunn, S., Liscombe, D.K., Facchini, P.J., Tanner, M.E. Mechanistic studies on norcoclaurine synthase of benzylisoquinoline alkaloid biosynthesis: an enzymatic Pictet-Spengler reaction. Biochemistry. 2007, 46, 10153-10161; DOI: 10.1021/bi700752n.



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