Abstract
Although the crystal structures of prokaryotic 6-phosphofructokinase, a key enzyme of glycolysis, have been available for almost 25 years now, structural information about the more complex and highly regulated eukaryotic enzymes is still lacking until now. This review provides an overview of the current knowledge of eukaryotic 6-phosphofructokinase based on recent crystal structures, kinetic analyses and site-directed mutagenesis data with special focus on the molecular architecture and the structural basis of allosteric regulation.
About the authors
Torsten Schöneberg studied medicine at the University of Greifswald, is professor of Molecular Biochemistry and leads the Institute for Biochemistry at the Medical Faculty of the University of Leipzig, Germany. After completing his MD thesis at the Institute of Pharmacology at the Charité, Humboldt University of Berlin, he focused on GPCR and their signal transduction in the labs of J. Wess (NIDDK, NIH, Bethesda) and G. Schultz (Free University of Berlin) as a postdoc.
Marco Kloos studied biochemistry at the University of Greifswald. After completing his diploma thesis at the Friedrich-Loeffler-Institut Insel Riems and the Institute of Biochemistry at the University of Greifswald, he started his PhD thesis in the lab of N. Sträter (Center for Biotechnology and Biomedicine, University of Leipzig).
Antje Brüser studied biochemistry at the University of Leipzig. She completed her PhD thesis in the lab of Torsten Schöneberg. Her scientific work focused on the functional relevance of nucleotide binding sites in eukaryotic 6-phosphofructokinases. Antje Brüser is currently leading a group in the Institute of Biochemistry at University of Leipzig.
Jürgen Kirchberger studied biochemistry at the University of Leipzig, is member of the academic staff of the Molecular Biochemistry in the Institute for Biochemistry at the Medical Faculty of the University of Leipzig, Germany. Since 1999 he focused his scientific work in studying the structure-function-relationship including regulation of oligomeric, allosteric enzymes, especially eukaryotic 6-phosphofructokinases.
Norbert Sträter studied chemistry at the University of Münster, where he obtained his doctoral degree with B. Krebs for the structure analysis of purple acid phosphatase. As a postdoctoral fellow with W. N. Lipscomb at Harvard University and later for his habilitation thesis in the laboratory of Wolfram Saenger at the Free University of Berlin, he studied the structure and function of dinuclear metalloenzymes. Since 2002 he is Professor of Structural Analysis in the Institute of Bioanalytical Chemistry at the University of Leipzig.
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