Professor Emily Parker

Position

Professor

Director of Research

Theme Leader, Biomolecular Interaction Centre

Qualifications

BSc(Hons) (UC), PhD (UK)

Field of Study

Bioorganic/Organic

Professional Awards

National Tertiary Teaching Excellence Award 2010
UC Teaching Award 2010

Room

758

Contact Details

DDI: +64 3 364 2871 (Internal 6871)
Fax: +64 3 364 2110
Email: emily.parker@canterbury.ac.nz

Background

Emily completed her BSc(Hons) degree in organic chemistry at the University of Canterbury . She was awarded a commonwealth scholarship to the University of Cambridge, UK, where she completed a PhD in bio-organic chemistry in 1997. After a brief period as a postdoctoral fellow at the University of Cambridge , she returned to New Zealand in 1998 to take up a lectureship at Massey University.

In 2005 she was awarded the New Zealand Institute of Chemistry Easterfield medal which is awarded biannually in recognition of significant contribution to research in the chemical sciences by a younger researcher. In 2006 Emily moved to the University of Canterbury to take up a position in the Chemistry Department. She was director of the TEC-funded Canterbury Biomolecular Interaction Centre which was established in 2007.

Undergraduate Courses

CHEM112
CHEM242/272
CHEM322/362
CHEM325/BCHM302
BCHM206

Graduate Courses

CHEM408
CHEM405
BCHM403

Research Interests

Emily's research team explores the evolution and molecular details of enzymic catalysis. This research area spans the areas of chemistry and biochemistry and involves a range of research techniques including small molecule synthesis, protein purification and manipulation, and molecular biology.

The group's focuses on the reaction chemistry of some key biosynthetic enzymes including 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAH7PS), 3-deoxy-D-manno-octulosonate 8-phosphate synthase (KDO8PS) and a-isopropylmalate synthase.

DAH7PS is the first enzyme of the shikimate pathway to aromatic compounds. As this pathway exists in plants and micro organisms but not in humans there has been a lot of interest in the enzymes of the pathway as potential targets form drug design. We have studied the enzyme from a variety of sources including the DAH7PSs from the pathogens Mycobacterium tuberculosis and Helicobacter pylori .

Structure of M. tuberculosis DAH7PS

Research Group Members

PhD
Aidan Harrison
David Tran
Penelope Cross
Wanting Jiao
Michael Hunter
Tim Allison
Frances Huisman
Tammie Cookson

Hons
Evan Nimmo
Dmitri Joseph

MSc
Benjamin Gloyne

Postdoctoral
Richard Hutton

Representative Publications

  • Phone: +64 3 364 2100
    Fax: +64 3 364 2110
    Email: chemistry@canterbury.ac.nz
  • Department of Chemistry
    University of Canterbury
    Private Bag 4800, Christchurch
    New Zealand
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