苯乙醛
脱羧
苯丙氨酸
酶
磷酸果糖激酶2
化学
生物化学
ATP合酶
氨基酸
催化作用
作者
Yasuhisa Kaminaga,Jennifer Schnepp,Greg Peel,Christine M. Kish,Gili Ben‐Nissan,David Weiss,Irina Orlova,Orly Lavie,David Rhodes,Karl V. Wood,D. Marshall Porterfield,Arthur J.L. Cooper,John V. Schloss,Eran Pichersky,Alexander Vainstein,Natalia Dudareva
标识
DOI:10.1074/jbc.m602708200
摘要
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.
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