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

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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

241 Scopus citations

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.

Original languageAmerican English
Pages (from-to)23357-23366
Number of pages10
JournalJournal of Biological Chemistry
Volume281
Issue number33
DOIs
StatePublished - 18 Aug 2006

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