Properties and Functional Analysis of Two Chorismate Mutases from Maritime Pine

• Published in: Cells (Basel, Switzerland) Vol. 13; no. 11; p. 929
• Main Authors: de la Torre, Fernando, Medina-Morales, Beatriz, Blanca-Reyes, Irene, Pascual, M Belén, Ávila, Concepción, Cánovas, Francisco M, Castro-Rodríguez, Vanessa
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 28.05.2024; MDPI
• Subjects: Algae; Amino acids; Angiosperms; aromatic amino acids; chloroplast; chorismate; Chorismate mutase; Chorismate Mutase - genetics; Chorismate Mutase - metabolism; Cloning; Conifers; Enzymes; Ethylenediaminetetraacetic acid; Flavonoids; Folic acid; Gene expression; Gene Expression Regulation, Plant; Gymnosperms; Isoenzymes; Localization; Metabolic flux; Metabolism; Metabolites; Pharmaceutical industry; Phenolic compounds; Phenylalanine; Phenylalanine - metabolism; Phylogenetics; Phylogeny; Pinus - enzymology; Pinus - genetics; Pinus - metabolism; Pinus pinaster; Plant Proteins - genetics; Plant Proteins - metabolism; Plastids - enzymology; Plastids - metabolism; Proteins; Salicylic acid; Seeds; shikimate pathway; Tryptophan; Tryptophan - metabolism; Tyrosine; Germany; California; United States > US; chorismate mutase; shikimate pathway; aromatic amino acids; conifers; chloroplast; chorismate
• ISSN: 2073-4409; 2073-4409
• DOI: 10.3390/cells13110929

Through the shikimate pathway, a massive metabolic flux connects the central carbon metabolism with the synthesis of chorismate, the common precursor of the aromatic amino acids phenylalanine, tyrosine, and tryptophan, as well as other compounds, including salicylate or folate. The alternative metabolic channeling of chorismate involves a key branch-point, finely regulated by aromatic amino acid levels. Chorismate mutase catalyzes the conversion of chorismate to prephenate, a precursor of phenylalanine and tyrosine and thus a vast repertoire of fundamental derived compounds, such as flavonoids or lignin. The regulation of this enzyme has been addressed in several plant species, but no study has included conifers or other gymnosperms, despite the importance of the phenolic metabolism for these plants in processes such as lignification and wood formation. Here, we show that maritime pine ( Aiton) has two genes that encode for chorismate mutase, and . Our investigations reveal that these genes encode plastidial isoenzymes displaying activities enhanced by tryptophan and repressed by phenylalanine and tyrosine. Using phylogenetic studies, we have provided new insights into the possible evolutionary origin of the cytosolic chorismate mutases in angiosperms involved in the synthesis of phenylalanine outside the plastid. Studies based on different platforms of gene expression and co-expression analysis have allowed us to propose that PpCM2 plays a central role in the phenylalanine synthesis pathway associated with lignification.