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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Acetaldehyde / analogs & derivatives*
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Acetaldehyde / chemistry
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Acetaldehyde / metabolism
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Amino Acid Sequence
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Catalysis
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Decarboxylation
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Molecular Sequence Data
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Multienzyme Complexes / chemistry*
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Multienzyme Complexes / genetics
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Multienzyme Complexes / isolation & purification
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Oxidation-Reduction
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Petunia / enzymology*
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Petunia / genetics
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Phenylalanine / chemistry*
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Phenylalanine / metabolism
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Plant Proteins / chemistry
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Plant Proteins / genetics
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Plant Proteins / isolation & purification
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Rosa / enzymology*
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Rosa / genetics
Substances
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Multienzyme Complexes
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Plant Proteins
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phenylacetaldehyde synthase, Pentunia hybrida
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Phenylalanine
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Acetaldehyde
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phenylacetaldehyde
Associated data
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GENBANK/DQ192639
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GENBANK/DQ243784