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Post anthesis, loquat flowers emit volatile benzenoids, including phenylacetaldehyde, phenylethyl alcohol, and 2-phenethyl benzoate. Previous studies have shown that pyridoxal phosphate-dependent aromatic L-amino acid decarboxylase (AADC) produces phenylacetaldehyde from L-phenylalanine. Here, two AADC genes ( EjAADC1 and EjAADC2 ) were isolated from loquat ( Eriobotrya japonica ) flowers. The EjAADC1 and EjAADC2 proteins showed approximately 72% and 55% identity, respectively, to a rose AADC homolog that has phenylacetaldehyde synthase activity. Transcript analyses indicated that EjAADC1 was specifically expressed in petals, with the highest level of expression in fully opened flowers; the petals showed high levels of volatile benzenoids, including phenylacetaldehyde. In contrast, EjAADC2 was expressed at a lower level than EjAADC1 in all tested tissues, including leaves and developing flowers. Functional characterization of a recombinant EjAADC1 protein expressed in Escherichia coli showed that it catalyzes the formation of phenylacetaldehyde from L-phenylalanine in a pyridoxal phosphate-dependent manner. Our results suggest that EjAADC1 is mainly responsible for the biosynthesis of volatile benzenoids in loquat flowers.

Aromatic amino acid decarboxylase is involved in volatile phenylacetaldehyde production in loquat (<i>Eriobotrya japonica</i>) flowers