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 (∼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.
| Original language | English |
|---|---|
| Pages (from-to) | 23357-23366 |
| Number of pages | 10 |
| Journal | Journal of Biological Chemistry |
| Volume | 281 |
| Issue number | 33 |
| DOIs | |
| State | Published - 18 Aug 2006 |
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