Kaminaga 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
Department of Horticulture and Landscape Architecture, Purdue University, West Lafayette, Indiana 47907-2010, USA.
J Biol Chem. 2006 Aug 18;281(33):23357-66. doi: 10.1074/jbc.M602708200. Epub 2006 Jun 9.
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.
我们已经分离并鉴定了矮牵牛品种米切尔的苯乙醛合酶（PAAS），它催化花香成分苯乙醛的形成。PAAS是一种胞质同四聚体酶，属于II类依赖磷酸吡哆醛的氨基酸脱羧酶，与植物L-酪氨酸/3,4-二羟基-L-苯丙氨酸和L-色氨酸脱羧酶具有广泛的氨基酸同一性（约65%）。它对苯丙氨酸表现出严格的特异性，表观Km为1.2 mM。PAAS是一种双功能酶，催化苯丙氨酸脱羧与氧化的前所未有的高效偶联，以化学计量的量生成苯乙醛、二氧化碳、氨和过氧化氢。
