Overexpression and characterization of medium-chain-length polyhydroxyalkanoate granule bound polymerases from Pseudomonas putida GPo1 |
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Authors: | Qun Ren Guy de Roo Bernard Witholt Manfred Zinn Linda Thöny-Meyer |
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Affiliation: | (1) Laboratory for Biomaterials, Swiss Federal Laboratories for Materials Testing and Research (Empa), CH-9014 St., Gallen, Switzerland;(2) Synthon BV, P.O. BOX 7071, 6503 GN Nijmegen, the Netherlands;(3) Institute of Molecular Systems Biology, Swiss Federal Institute of Technology, CH-8093 Zurich, Switzerland |
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Abstract: | Background Polyhydroxyalkanoates (PHA) are synthesized by many bacteria in the cytoplasm as storage compounds for energy and carbon. The key enzymes for PHA biosynthesis are PHA polymerases, which catalyze the covalent linkage of 3-hydroxyacyl coenzymeA thioesters by transesterification with concomitant release of CoA. Pseudomonas putida GPo1 and many other Pseudomonas species contain two different class II polymerases, encoded by phaC1 and phaC2. Although numerous studies have been carried out on PHA polymerases and they are well characterized at the molecular level, the biochemical properties of the class II polymerases have not been studied in detail. Previously we and other groups purified the polymerases, however, the activities of the purified enzymes were several magnitude lower than the granule-bound enzymes. It is problematic to study the intrinsic properties of these enzymes with such low activities, although they are pure. |
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