Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation

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Abstract

We have isolated and characterized Petunia hybrida cv. Mitchell phenylacetaldehyde synthase (PAAS), which catalyzes the formation of phenylacetaldehyde, a constituent of floral scent. PAAS is a cytosolic homotetrameric enzyme that belongs to group II pyridoxal 5′-phosphate- dependent amino-acid decarboxylases and shares extensive amino acid identity (∼65%) with plant L-tyrosine/3,4-dihydroxy-L-phenylalanine and L-tryptophan decarboxylases. It displays a strict specificity for phenylalanine with an apparent Km of 1.2 mM. PAAS is a bifunctional enzyme that catalyzes the unprecedented efficient coupling of phenylalanine decarboxylation to oxidation, generating phenylacetaldehyde, CO2, ammonia, and hydrogen peroxide in stoichiometric amounts. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

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Kaminaga, Y., Schnepp, J., Peel, G., Kish, C. M., Ben-Nissan, G., Weiss, D., … Dudareva, N. (2006). Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation. Journal of Biological Chemistry, 281(33), 23357–23366. https://doi.org/10.1074/jbc.M602708200

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