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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti.

The sesquiterpene cyclase, aristolochene synthase, has been purified from Penicillium roqueforti by gel filtration and anion-exchange chromatography. Isolation was facilitated by a change in the elution behavior of the enzyme during gel filtration at different steps in the purification. The purified enzyme had a specific activity of 70 nmol/min/mg protein. The molecular weight as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was Mr 37,000. The native molecular weight as determined by gel filtration chromatography was Mr 48,000. The requirement for Mg2+ could be partially substituted with 0.01 mM Mn2+, but higher concentrations were inhibitory. Pyrophosphate, a competitive inhibitor of most terpene cyclases, had no effect on enzyme activity up to a concentration of 5.0 mM. The maximum activity was observed between pH 6.25 and pH 7.50, and the Km for farnesyl pyrophosphate was 0.55 +/- 0.06 microM.[1]

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