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.
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 of tyrosine ammonia-lyase and p-hydroxybenzoate synthase, respectively. Btoh 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.
D001565:Benzoates / Q000378:metabolism* / Q000494:pharmacology; D002455:Cell Division / Q000187:drug effects; D002462:Cell Membrane / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism*; D000458:Cyanobacteria / Q000187:drug effects / Q000378:metabolism*; D062385:Hydroxybenzoates / Q000378:metabolism* / Q000494:pharmacology; D009097:Multienzyme Complexes / Q000378:metabolism*; D010649:Phenylalanine / Q000378:metabolism; D013045:Species Specificity; D014443:Tyrosine / Q000378:metabolism
D001565:Benzoates; D062385:Hydroxybenzoates; D009097:Multienzyme Complexes; D014443:Tyrosine; D010649:Phenylalanine