Faculty - Kenneth Ng

Research Interests: Our research group primarily uses X-ray crystallography to define the three-dimensional shapes of protein complexes to shed light on the mechanisms underlying molecular processes important to living organisms. Structures often provide hints and suggest hypotheses for how changes in the primary sequences of proteins lead to changes in their functions. We test these ideas and hypotheses by creating site-directed mutants and comparing their binding and catalytic properties with the original protein. Our primary goal is to contribute towards understanding biomolecular structure and mechanism at the basic science level. In addition, we focus our attention on specific systems where our research attempts to provide new tools and approaches for creating new treatments for diseases and to expand the capabilities of biotechnology through protein and metabolic engineering.

• Viral RNA-dependent RNA Polymerases replicate the genomes of positive-strand RNA viruses, which cause many human diseases (e.g., polio, hepatitis A and C, dengue, viral encephalitis (West Nile virus), viral gastroenteritis (Norovirus) and Severe Acute Respiratory Syndrome (SARS and COVID-19). Our work provides the foundation for designing novel antiviral therapeutics.
• Biosynthetic enzymes in the benzylisoquinoline alkaloid (BIA) pathways lead to the production of powerful analgesics (morphine and codeine) and antimicrobial compounds (sanguinarine and berberine). Our studies on key enzymes open the door to producing novel medicinal compounds.
• Streptavidin muteins exploit the tight and specific binding of biotin and peptide tags in a controlled and switchable manner to provide powerful new tools for biotechnology.

 

RECENT PUBLICATIONS:

1. Engineering a disulfide-gated switch in streptavidin enables reversible binding without sacrificing binding affinity.
   Marangoni, J., S.-C. Wu, D. Fogen, S.-L. Wong, K.K.S. Ng Sci. Rep. (2020) 294, 14482-14498.
2. Structure function studies of tetrahydroprotoberberine N-methyltransferase reveal the molecular basis of stereoselective substrate recognition.
   Lang, D.E., J.S. Morris, M. Rowley, M.A. Torres, V.A. Maksimovich, P.J. Facchini, K.K.S. Ng J. Biol. Chem. (2019) 294, 14482-14498.
3. Codeinone reductase isoforms with differential stability, efficiency and product selectivity in opium poppy.
   Dastmalchi, M., L. Chang, M.A. Torres, K.K.S. Ng, P.J. Facchini Plant J. (2018) 95, 631-647.
4. Heterodimeric O-methyltransferases involved in the biosynthesis of noscapine in opium poppy.
   Park, M.R. X. Chen, D.E. Lang, K.K.S. Ng, P.J. Facchini Plant J. (2018) 95, 252-267.
5. Recognition of dual phosphorylated substrates by the tyrosine-specific PPP-family phosphatase Arabidopsis thaliana Rhizobiales-like phosphatase 2.
   Labandera, A., R.G. Uhrig, K. Colville, G.B. Moorhead, K.K.S. Ng Sci. Signal. (2018) 11(524). pii: eaan8804­.

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