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

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Abstract

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. © 1976, Walter de Gruyter. All rights reserved.

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Löffelhardt, W., & Kindl, H. (1976). 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. Zeitschrift Fur Naturforschung - Section C Journal of Biosciences, 31(11–12), 693–699. https://doi.org/10.1515/znc-1976-11-1212

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