Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation

被引:233
作者
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
机构
[1] Purdue Univ, Dept Hort & Landscape Architecture, W Lafayette, IN 47907 USA
[2] Purdue Univ, Dept Chem, W Lafayette, IN 47907 USA
[3] Purdue Univ, Dept Agr & Biol Engn, W Lafayette, IN 47907 USA
[4] Hebrew Univ Jerusalem, Fac Agr Food & Environm Qual Sci, IL-76100 Rehovot, Israel
[5] Cornell Univ, Weil Med Coll, White Plains, NY 10605 USA
[6] Cornell Univ, Coll Med, Burke Med Res Inst, White Plains, NY 10605 USA
[7] NeuroSystec Corp, Valencia, CA 91355 USA
[8] Univ Michigan, Dept Mol Cellular & Dev Biol, Ann Arbor, MI 48109 USA
关键词
D O I
10.1074/jbc.M602708200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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 (similar to 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.
引用
收藏
页码:23357 / 23366
页数:10
相关论文
共 61 条
[1]   OXYGENASE SIDE REACTIONS OF ACETOLACTATE SYNTHASE AND OTHER CARBANION-FORMING ENZYMES [J].
ABELL, LM ;
SCHLOSS, JV .
BIOCHEMISTRY, 1991, 30 (32) :7883-7887
[2]   Identification of an unusual [2Fe-2S]-binding motif in the CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase from Yersinia pseudoutberculosis:: Implication for C-3 deoxygenation in the biosynthesis of 3,6-dideoxyhexoses [J].
Agnihotri, G ;
Liu, YN ;
Paschal, BM ;
Liu, HW .
BIOCHEMISTRY, 2004, 43 (44) :14265-14274
[3]   PLP and PMP radicals:: A new paradigm in coenzyme B6 chemistry [J].
Agnihotri, G ;
Liu, HW .
BIOORGANIC CHEMISTRY, 2001, 29 (04) :234-257
[4]   ESTIMATION OF PHENYLALANINE AMMONIA-LYASE (PAL)-ACTIVITY IN INTACT-CELLS OF HIGHER PLANT-TISSUE .1. PARAMETERS OF ASSAY [J].
AMRHEIN, N ;
GODEKE, KH ;
GERHARDT, J .
PLANTA, 1976, 131 (01) :33-40
[5]   PEROXIDATION REACTIONS IN PLANT MEMBRANES - EFFECTS OF FREE FATTY-ACIDS [J].
BARCLAY, KD ;
MCKERSIE, BD .
LIPIDS, 1994, 29 (12) :877-882
[6]   Targeting detoxification pathways: an efficient approach to obtain plants with multiple stress tolerance? [J].
Bartels, D .
TRENDS IN PLANT SCIENCE, 2001, 6 (07) :284-286
[7]   Locking mechanism preventing radical damage in the absence of substrate,, as revealed by the x-ray structure of lysine 5,6-aminomutase [J].
Berkovitch, F ;
Behshad, E ;
Tang, KH ;
Enns, EA ;
Frey, PA ;
Drennan, CL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (45) :15870-15875
[8]   A quinonoid is an intermediate of oxidative deamination reaction catalyzed by Dopa decarboxylase [J].
Bertoldi, M ;
Cellini, B ;
Maras, B ;
Voltattorni, CB .
FEBS LETTERS, 2005, 579 (23) :5175-5180
[9]   Reaction and substrate specificity of recombinant pig kidney Dopa decarboxylase under aerobic and anaerobic conditions [J].
Bertoldi, M ;
Voltattorni, CB .
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2003, 1647 (1-2) :42-47
[10]   Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase [J].
Bertoldi, M ;
Gonsalvi, M ;
Contestabile, R ;
Voltattorni, CB .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (39) :36357-36362