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

The Journal of biological chemistry (2006-06-13)
Yasuhisa Kaminaga, Jennifer Schnepp, Greg Peel, Christine M Kish, Gili Ben-Nissan, David Weiss, Irina Orlova, Orly Lavie, David Rhodes, Karl Wood, D Marshall Porterfield, Arthur J L Cooper, John V Schloss, Eran Pichersky, Alexander Vainstein, Natalia Dudareva
ABSTRAKT

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 (approximately 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.

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Sigma-Aldrich
Phenylacetaldehyde, ≥90%