Title: | Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation |
Author(s): | Kaminaga Y; Schnepp J; Peel G; Kish CM; Ben-Nissan G; Weiss D; Orlova I; Lavie O; Rhodes D; Wood K; Porterfield DM; Cooper AJ; Schloss JV; Pichersky E; Vainstein A; Dudareva N; |
Address: | "Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, Indiana 47907-2010, USA" |
ISSN/ISBN: | 0021-9258 (Print) 0021-9258 (Linking) |
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" |
Keywords: | Acetaldehyde/*analogs & derivatives/chemistry/metabolism Amino Acid Sequence Catalysis Decarboxylation Molecular Sequence Data Multienzyme Complexes/*chemistry/genetics/isolation & purification Oxidation-Reduction Petunia/*enzymology/genetics Phenylalanin; |
Notes: | "MedlineKaminaga, Yasuhisa Schnepp, Jennifer Peel, Greg Kish, Christine M Ben-Nissan, Gili Weiss, David Orlova, Irina Lavie, Orly Rhodes, David Wood, Karl Porterfield, D Marshall Cooper, Arthur J L Schloss, John V Pichersky, Eran Vainstein, Alexander Dudareva, Natalia eng Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. 2006/06/13 J Biol Chem. 2006 Aug 18; 281(33):23357-66. doi: 10.1074/jbc.M602708200. Epub 2006 Jun 9" |