Purification and Properties of Acridone Synthase from Cell Suspension Cultures of Ruta gvaveolens L.

Author:

Baumert Alfred,Maier Walter,Gröger Detlef,Deutzmann Rainer

Abstract

Acridone synthase has been purified from cell suspension cultures of Ruta graveolens using a combination of gel filtration and ion exchange chromatography. The purified enzyme has an apparent molecular weight of 69 kDa on gel filtration and a subunit structure on SDS-PAGE of 40 kDa. The apparent Km-values are 10.64 μM and 32.8 μM for N-methylanthraniloyl-CoA and malonyl-CoA, respectively. Tryptic digestion of the homogeneous acridone synthase was performed. Seven of the peptides were chosen for microsequencing. The homology of the amino acid sequences from this particular polypeptide and corresponding peptides from chalcone synthase 3 from garden pea amounted to 76%.

Publisher

Walter de Gruyter GmbH

Subject

General Biochemistry, Genetics and Molecular Biology

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