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B6db references: 16766535

type Journal Article
authors 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.
title Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation
journal J. Biol. Chem.
sel selected
ui 16766535
year (2006)
volume 281
pages 23357-66
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
last changed 2008/01/30 19:12

B6db references