Sandra Schlee

Summary

Affiliation: University of Regensburg
Country: Germany

Publications

  1. doi request reprint 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 request reprint 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. doi request reprint Evidence for the existence of elaborate enzyme complexes in the Paleoarchean era
    Bernd Reisinger
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, D 93053 Regensburg, Germany
    J Am Chem Soc 136:122-9. 2014
  4. doi request reprint 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
  5. pmc Molecular engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template
    Monika M Meier
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Regensburg, Germany
    J Am Chem Soc 135:11670-7. 2013

Collaborators

Detail Information

Publications5

  1. doi request reprint 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 request reprint 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. doi request reprint Evidence for the existence of elaborate enzyme complexes in the Paleoarchean era
    Bernd Reisinger
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Universitätsstraße 31, D 93053 Regensburg, Germany
    J Am Chem Soc 136:122-9. 2014
    ..5 billion years ago. ..
  4. doi request reprint 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...
  5. pmc Molecular engineering of organophosphate hydrolysis activity from a weak promiscuous lactonase template
    Monika M Meier
    Institute of Biophysics and Physical Biochemistry, University of Regensburg, Regensburg, Germany
    J Am Chem Soc 135:11670-7. 2013
    ....