Ms. Carolin Bisterfeld








Carolin Bisterfeld M.Sc.

Institute of Bioorganic Chemistry
Pietruszka Group
Research Center Jülich GmbH
Building: 15.8
Floor/Room: 212
52426 Jülich
Phone +492461-613745
Fax +492461-616196

Mini Academic CV

University degrees:

First degree or intermediate examination:

  • B.Sc. 2010, HHU

Second degree and/or intermediate examination:

  • M.Sc. 2012, HHU


  • Scholarship of Studienstiftung des deutschen Volkes, 2009-2012
  • Paticipation of the 59th Nobel Laureate Meeting dedicated to chemistry, 2009

Structure Based Design of Acetaldehyde-dependent Aldolases
There are 4 different (natural) donors in aldolase catalyzed transformations. While all possible enantio- and/or diastereoisomers are accessible for pyruvate-, DHAP- or glycine depending aldolases, the acetaldehyde-depending enzymes (DERA) do all just lead to one enantiomer. The aim is to change the selectivity of the catalyst by rational design. Thereby (in silico) docking experiments (Gohlke) based on the X-ray structure should allow suggesting sites for mutagenesis. While the DERA from E. coli is well described and understood, we noted that the corresponding aldolase from R. erythropolis (see our paper in press J. Biotechnol.) might have superior properties. We would like to apply the findings to this enzyme as well. Therefore we have to find the most appropriate expression system. Cristal Structures would be highly desirable (Groth).


Topic Supervisor:

undefinedProf. Dr. Jörg Pietruszka, Institute for Biochemistry, Smits Group

Complementary Supervisor:
undefinedProf. Dr. Georg Groth, Institute for Biochemistry, Groth Group

Third Supervisor:
undefinedProf. Dr. Holger Gohlke, Institute for Biochemistry, Gohlke Group

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