Project: Membrane protein enzymology

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Cells are surrounded by membranes that separates the cell from the outside world and allows a specific internal chemical environment. Membranes are also found in the cell interior. These membranes form a barrier in which many biochemical processes occur, such as energy conversion , transport, and signalling. These processes are relatively well studied. The membranes are also a compartment in the cell where lipophilic substances dissolve. Membrane processes where enzymes synthesize products by conjugating water soluble and membrane- dissolved components is less well investigated. Generally speaking, the detailed knowledge of membrane-bound enzymes mechanism is rare because these proteins represent a methodological challenge. In this project we will investigate two membrane-bound enzymes for which the crystal structure was determined and where tools have been developed for detailed mechanistic studies. We can thus contribute to new knowledge about a class of enzymes that have been very difficult to study in detail. Since the enzymes under study are involved in protection against toxic substances or participate in the synthesis of endogenous substances (such as fever, pain and inflammation signals) results will provide a better understanding of these processes. This can lead to better prevention strategies and the development of new and safer drugs.

Contact person


Ralf Morgenstern

Phone: +46-(0)8-524 875 74
Organizational unit: Biochemical toxicology


  • The Swedish Research Council (NT)
  • SSF-Vinnova


Structural basis for induced formation of the inflammatory mediator prostaglandin E2.
Jegerschöld C, Pawelzik S, Purhonen P, Bhakat P, Gheorghe K, Gyobu N, et al
Proc. Natl. Acad. Sci. U.S.A. 2008 Aug;105(32):11110-5

Characterization of new potential anticancer drugs designed to overcome glutathione transferase mediated resistance.
Johansson K, Ito M, Schophuizen C, Mathew Thengumtharayil S, Heuser V, Zhang J, et al
Mol. Pharm. 2011 Oct;8(5):1698-708

Synthesis and characterization of a series of highly fluorogenic substrates for glutathione transferases, a general strategy.
Zhang J, Shibata A, Ito M, Shuto S, Ito Y, Mannervik B, et al
J. Am. Chem. Soc. 2011 Sep;133(35):14109-19

Catalytic characterization of human microsomal glutathione S-transferase 2: identification of rate-limiting steps.
Ahmad S, Niegowski D, Wetterholm A, Haeggström J, Morgenstern R, Rinaldo-Matthis A
Biochemistry 2013 Mar;52(10):1755-64