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J. Biol. Chem., Vol. 281, Issue 33, 23357-23366, August 18, 2006

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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, and Natalia Dudareva¹

From the Departments of Horticulture and Landscape Architecture, ^¶Chemistry, and ^||Agricultural and Biological Engineering, Purdue University, West Lafayette, Indiana 47907-2010, the Faculty of Agricultural, Food and Environmental Quality Sciences, The Hebrew University of Jerusalem, Rehovot 76100, Israel, the ^**Weil Medical College of Cornell University and the Burke Medical Research Institute, White Plains, New York 10605, NeuroSystec Corporation, Mann Biomedical Park, Valencia, California 91355, and the Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109

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 K_m 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.

Received for publication, March 22, 2006 , and in revised form, June 8, 2006.

^* This work was supported by United States-Israel Binational Agriculture Research and Development Grant US-3437-03 (to N. D., A. V., and D. W.) and Grant IS-3332-02 (to E. P.) and by a grant from the Fred C. Gloeckner Foundation (to N. D.). This is Contribution 2005-17814 from the Purdue University Agricultural Experimental Station. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the Gen-Bank^TM/EBI Data Bank with accession number(s) DQ243784 [GenBank] and DQ192639 [GenBank] for petunia and ros PAAS, respectively.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

¹ To whom correspondence should be addressed: Dept. of Horticulture and Landscape Architecture, Purdue University, 625 Agriculture Mall Dr., West Lafayette, IN 47907-2010. Tel.: 765-494-1325; Fax: 765-494-0391; E-mail: dudareva{at}purdue.edu.

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