The Arabidopsis PAL3 is a carboxy-tyrosine ammonia lyase
Van Beirs, C.; Van der Vaet, A.; Goeman, J.; Almeida-Silva, F.; Xie, C.; Meinert, H.; Desmet, S.; Vandersyppe, S.; Vanholme, R.; Van der Eycken, J.; Devreese, B.; Bayer, T.; Bornscheuer, U.; Boerjan, W.; Vanholme, B.
Show abstract
Phenylalanine ammonia lyase (PAL) catalyses the deamination of L-phenylalanine, which is the first step of the plant-specific phenylpropanoid pathway. Its position at the intersection of primary and specialized metabolism, combined with its important role in plant growth and adaptive stress response, has made it a subject of extensive studies. We identified key amino acids in the catalytic pocket of several PAL enzymes, including PAL3 of Arabidopsis, that are different from the canonical PAL sites, suggesting these enzymes have a different substrate specificity and have been miscategorised for decades. By combining untargeted metabolomics with enzyme assays, we discovered that PAL3 converts 3-carboxy-tyrosine into carboxy-p-coumaric acid. Based on this specific function, we propose to denote it as a 3-carboxy-tyrosine ammonia lyase (CAL). In addition to its discovery as a novel enzyme class, paving the way for biotechnological applications, we introduce the carboxy-phenylpropanoids as a new class of specialised metabolites.
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