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Doctor of Philosophy, (Chemistry)
Study Completed: 2009
College of Sciences
Synthesis of substrate analogues and inhibitors of phosphoribosyl anthranilate isomerase and indole-3-glycorolphosphate synthase
Mr Mulchin developed organic-synthetic methodology to synthesise molecules to probe two key steps in the biosynthetic pathway of the amino acid tryptophan as there is little information on how the substrates and enzymes interact. In these key enzymatic steps, 5-phosphoribosylanthranilate is converted into indole-3-glycerolphosphate (IGP), via the intermediate species 1-(O-carboxyphenylamino)-1-deoxyribulose-5-phosphate (CdRP). Mr Mulchin undertook the first systematic attempt to develop synthetic methodology to produce a plethora of substrate and product analogues of CdRP. The methodology developed focused on secondary aryl amine formation, using a variety of techniques, and led to the synthesis of CdRP analogues. Mr Mulchin has shown that synthesis of CdRP analogues via nucleophilic substitution of good leaving groups and epoxide ring opening proved consistently reproducible. This methodology allows for future synthesis of a range of CdRP-like target compounds, which can then be used to gain information on how substrates and enzymes interact.
Associate Professor Emily Parker
Professor Geoff Jameson
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Last updated on Tuesday 04 April 2017