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Membrane-Bound Enzyme Complexes, Anacystis nidulans, Thylakoids, Benzoate Synthase The photosynthetic procaryote Anacystis nidulans converts L-phenylalanine and L-tyrosine into benzoic acid and p-hydroxybenzoic acid, respectively. Results obtained with thylakoid fractions support the hypothesis that the reaction sequence is catalyzed by thylakoid-bound enzyme complexes consisting of phenylalanine ammonia-lyase and benzoate synthase or tyrosine ammonia-lyase and p-hydroxybenzoate synthase, respectively. Both complexes do not accept phenylacetic acids as substrates, and cinnamic acids only at a small extent. These properties suggest a striking similarity to a benzoic acid-synthesizing enzyme system from higher plants which is situated at the thylakoid membrane of chloroplasts. The respective complexes of Dunaliella marina and Porphyridium sp. were included in this comparison.

zeitschrift für naturforschung c

Formation of Benzoic Acid and p-Hydroxybenzoic Acid in the Blue Green Alga Anacystis nidulans: A Thylakoid-Bound Enzyme Complex Analogous to the Chloroplast System