Literature DB >> 138288

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.

W Löffelhardt.   

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 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.

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Year:  1976        PMID: 138288     DOI: 10.1515/znc-1976-11-1212

Source DB:  PubMed          Journal:  Z Naturforsch C Biosci        ISSN: 0341-0382


  2 in total

1.  Metabolism of l-Tyrosine to 4-Hydroxybenzaldehyde and 3-Bromo-4-Hydroxybenzaldehyde by Chloroplast-containing Fractions of Odonthalia floccosa (Esp.) Falk.

Authors:  S L Manley; D J Chapman
Journal:  Plant Physiol       Date:  1979-12       Impact factor: 8.340

2.  Biosynthesis of p-Hydroxybenzoate from p-Coumarate and p-Coumaroyl-Coenzyme A in Cell-Free Extracts of Lithospermum erythrorhizon Cell Cultures.

Authors:  R. Loscher; L. Heide
Journal:  Plant Physiol       Date:  1994-09       Impact factor: 8.340

  2 in total

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