Sandra Schlee

Summary

Affiliation: University of Regensburg
Country: Germany

Publications

  1. ncbi Kinetic mechanism of indole-3-glycerol phosphate synthase
    Sandra Schlee
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Universitatsstrasse 31, D 93053 Regensburg, Germany
    Biochemistry 52:132-42. 2013
  2. ncbi Experimental assessment of the importance of amino acid positions identified by an entropy-based correlation analysis of multiple-sequence alignments
    Susanne Dietrich
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Universitatsstrasse 31, D 93053 Regensburg, Germany
    Biochemistry 51:5633-41. 2012
  3. ncbi Activation of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus by removal of magnesium inhibition and acceleration of product release
    Sandra Schlee
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Germany
    Biochemistry 48:5199-209. 2009

Collaborators

Detail Information

Publications3

  1. ncbi Kinetic mechanism of indole-3-glycerol phosphate synthase
    Sandra Schlee
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Universitatsstrasse 31, D 93053 Regensburg, Germany
    Biochemistry 52:132-42. 2013
    ..The liberation of the product from the active site is the rate-limiting step of the overall reaction. Our results confirm the importance of flexible active loops for substrate binding and catalysis by sIGPS...
  2. ncbi Experimental assessment of the importance of amino acid positions identified by an entropy-based correlation analysis of multiple-sequence alignments
    Susanne Dietrich
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Universitatsstrasse 31, D 93053 Regensburg, Germany
    Biochemistry 51:5633-41. 2012
    ..Our findings demonstrate that positions with high conn(k) values have an increased probability of being important for enzyme function or stability...
  3. ncbi Activation of anthranilate phosphoribosyltransferase from Sulfolobus solfataricus by removal of magnesium inhibition and acceleration of product release
    Sandra Schlee
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Germany
    Biochemistry 48:5199-209. 2009
    ..This effect appears to be mainly caused by an increased conformational flexibility induced by the F149S mutation, a hypothesis which is supported by the reduced thermal stability of the ssAnPRT-F149S single mutant...