TY - JOUR
T1 - Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation
AU - Kaminaga, Yasuhisa
AU - Schnepp, Jennifer
AU - Peel, Greg
AU - Kish, Christine M.
AU - Ben-Nissan, Gili
AU - Weiss, David
AU - Orlova, Irina
AU - Lavie, Orly
AU - Rhodes, David
AU - Wood, Karl
AU - Porterfield, D. Marshall
AU - Cooper, Arthur J.L.
AU - Schloss, John V.
AU - Pichersky, Eran
AU - Vainstein, Alexander
AU - Dudareva, Natalia
PY - 2006/8/18
Y1 - 2006/8/18
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=33747646883&partnerID=8YFLogxK
U2 - 10.1074/jbc.M602708200
DO - 10.1074/jbc.M602708200
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C2 - 16766535
AN - SCOPUS:33747646883
SN - 0021-9258
VL - 281
SP - 23357
EP - 23366
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 33
ER -