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• "Exploiting Protein Symmetry To Design Light-Controllable Enzyme Inhibitors", Reisinger, Kuzmanovic, Löffler, Merkl, König, Sterner, 2014

  Publikation

  The activity of the metabolic branch-point enzyme PriA from Mycobacterium tuberculosis (mtPriA) can be controlled reversibly by light. Two-pronged...

  Publikation auf epub.uni-regensburg.de: "Exploiting Protein Symmetry To Design Light-Controllable Enzyme Inhibitors" (externer Link, öffnet neues Fenster)

• "A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase enzyme family identifies novel members and reveals mechanisms of substrate specificity and quaternary structure organization", Peterhoff, Beer, Rajendran, Kumpula, Kapetaniou, Guldan, Wierenga, Sterner, Babinger, 2014

  Publikation

  Geranylgeranylglyceryl phosphate synthase (GGGPS) family enzymes catalyse the formation of an ether bond between glycerol-1-phosphate and polyprenyl...

  Publikation auf epub.uni-regensburg.de: "A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase enzyme family identifies novel members and reveals mechanisms of substrate specificity and quaternary structure organization" (externer Link, öffnet neues Fenster)

• "TrpB2 Enzymes are O-Phospho-l-serine Dependent Tryptophan Synthases", Busch, Rajendran, Mayans, Löffler, Merkl, Sterner, 2014

  Publikation

  The rapid increase of the number of sequenced genomes asks for the functional annotation of the encoded enzymes. We used a combined...

  Publikation auf epub.uni-regensburg.de: "TrpB2 Enzymes are O-Phospho-l-serine Dependent Tryptophan Synthases" (externer Link, öffnet neues Fenster)

• "Activation of a chimeric Rpb5/RpoH subunit using library selection", Sommer, Waege, Pöllmann, Seitz, Thomm, Sterner, Hausner, 2014

  Publikation

  Rpb5 is a general subunit of all eukaryotic RNA polymerases which consists of a N-terminal and a C-terminal domain. The corresponding archaeal subunit...

  Publikation auf epub.uni-regensburg.de: "Activation of a chimeric Rpb5/RpoH subunit using library selection" (externer Link, öffnet neues Fenster)

• "Conversion of Anthranilate Synthase into Isochorismate Synthase: Implications for the Evolution of Chorismate‐Utilizing Enzymes", Plach, Löffler, Merkl, Sterner, 2015

  Publikation

  Chorismate-utilizing enzymes play a vital role in the biosynthesis of metabolites in plants as well as free-living and infectious microorganisms....

  Publikation auf epub.uni-regensburg.de: "Conversion of Anthranilate Synthase into Isochorismate Synthase: Implications for the Evolution of Chorismate‐Utilizing Enzymes" (externer Link, öffnet neues Fenster)

• "Improving thermal and detergent stability of Bacillus stearothermophilus neopullulanase by rational enzyme design", Ece, Evran, Janda, Merkl, Sterner, 2015

  Publikation

  Neopullulanase, a glycosyl hydrolase from Bacillus stearothermophilus (bsNpl), is a potentially valuable enzyme for starch and detergent industries....

  Publikation auf epub.uni-regensburg.de: "Improving thermal and detergent stability of Bacillus stearothermophilus neopullulanase by rational enzyme design" (externer Link, öffnet neues Fenster)

• "Identification and Characterization of Heptaprenylglyceryl Phosphate Processing Enzymes inBacillus subtilis", Linde, Peterhoff, Sterner, Babinger, 2016

  Publikation

  In Archaea, ether lipids play an essential role as the main building blocks of the cellular membrane. Recently, ether lipids have also been discovered...

  Publikation auf epub.uni-regensburg.de: "Identification and Characterization of Heptaprenylglyceryl Phosphate Processing Enzymes inBacillus subtilis" (externer Link, öffnet neues Fenster)

• "Ancestral Tryptophan Synthase Reveals Functional Sophistication of Primordial Enzyme Complexes", Busch, Rajendran, Heyn, Schlee, Merkl, Sterner, 2016

  Publikation

  Modern enzyme complexes are characterized by a high catalytic efficiency and allosteric communication between the constituting protein subunits. We...

  Publikation auf epub.uni-regensburg.de: "Ancestral Tryptophan Synthase Reveals Functional Sophistication of Primordial Enzyme Complexes" (externer Link, öffnet neues Fenster)