| Literature DB >> 16766535 |
Yasuhisa Kaminaga1, 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.
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 (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.Entities:
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Year: 2006 PMID: 16766535 DOI: 10.1074/jbc.M602708200
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157