Characterization of an Isoprene Synthase from Leaves of Quercus petraea (Mattuschka) Liebl.
Corresponding Author
J.-P. Schnitzler
Fraunhofer-Institut Atmosphärische Umweltforschung, Garmisch-Partenkirchen, Germany
Frauenhofer-Institut Atmosphärische Umweltforschung (IFU) Kreuzeckbahnstr. 19 D-82467 Garmisch-Partenkirchen Germany e-mail: [email protected]Search for more papers by this authorR. Arenz
Fraunhofer-Institut Atmosphärische Umweltforschung, Garmisch-Partenkirchen, Germany
Search for more papers by this authorR. Steinbrecher
Fraunhofer-Institut Atmosphärische Umweltforschung, Garmisch-Partenkirchen, Germany
Search for more papers by this authorAndrea Lehning
Fraunhofer-Institut Atmosphärische Umweltforschung, Garmisch-Partenkirchen, Germany
Search for more papers by this authorCorresponding Author
J.-P. Schnitzler
Fraunhofer-Institut Atmosphärische Umweltforschung, Garmisch-Partenkirchen, Germany
Frauenhofer-Institut Atmosphärische Umweltforschung (IFU) Kreuzeckbahnstr. 19 D-82467 Garmisch-Partenkirchen Germany e-mail: [email protected]Search for more papers by this authorR. Arenz
Fraunhofer-Institut Atmosphärische Umweltforschung, Garmisch-Partenkirchen, Germany
Search for more papers by this authorR. Steinbrecher
Fraunhofer-Institut Atmosphärische Umweltforschung, Garmisch-Partenkirchen, Germany
Search for more papers by this authorAndrea Lehning
Fraunhofer-Institut Atmosphärische Umweltforschung, Garmisch-Partenkirchen, Germany
Search for more papers by this authorAbstract:
Biogenic emission of isoprene (2-methyl-1,3-butadiene) by many plant species plays an important role in atmospheric chemistry. Its rapid breakdown in the atmosphere substantially affects the oxidation potential of the atmosphere. Leaves of Quercus petraea were found to contain an enzyme which catalyses the conversion of dimethylallyl pyrophosphate (DMAPP) to isoprene. A standard enzyme assay was established and the isoprene synthase activity was characterized in purified leaf extracts. Optimum enzyme activity was observed at pH 8.5. The enzyme had an apparent Km of 0.97 mM for its substrate DMAPP, but isopentenyl pyrophosphate (IPP), the isomeric form of DMAPP, was not converted to isoprene by the enzyme extract. The temperature optimum of the enzyme activity was 35 °C. Isoprene synthase activity was strictly dependent on the presence of bivalent cations, with magnesium being most effective. Molecular weight determination by FPLC revealed the presence of a single protein with a native molecular weight of approximately 90–100 kDa.
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