Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: "The allosteric modulation of lipases and its possible biological relevance | Theoretical Biology and Medical Modelling BioMed Central Research Open Access The allosteric modulation of lipases and its possible biological relevance Jens Kohler and Bernhard Wunsch Address Institut fur Pharmazeutische und Medizinische Chemie Westfalische Wilhelms-Universitat Munster Hittorfstrafie 58-62 D-48149 Munster Germany Email Jens Kohler - jenskoeh@ Bernhard Wunsch - wuensch@ Corresponding author Published 7 September 2007 Received 10 May 2007 Theoretical Biology and Medical Modelling 2007 4 34 doi 1742-4682-4-34 Accepted 7 September 2007 This article is available from http content 4 1 34 2007 Kohler and Wunsch licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background During the development of an enantioselective synthesis using the lipase from Mucor miehei an unusual reaction course was observed which was analyzed precisely. For the first time an allosteric modulation of a lipase changing its selectivity was shown. Theory Considering the biological relevance of the discovered regulation mechanism we developed a theory that describes the regulation of energy homeostasis and fat metabolism. Conclusion This theory represents a new approach to explain the cause of the metabolic syndrome and provides an innovative basis for further research activity. Background Introduction Asymmetric syntheses are investigated to produce chiral organic compounds with high enantiomeric purity. Their development has been an expending task of research during the last years. Valuable tools to perform the required chemical reactions are enzymes which work as catalysts. The substrate to be transformed binds to the chiral binding site of the employed enzyme and is modified .
