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Aromatic amino acid decarboxylase is involved in volatile phenylacetaldehyde production in loquat (Eriobotrya japonica) flowers.


ABSTRACT: 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.

SUBMITTER: Koeduka T 

PROVIDER: S-EPMC6543696 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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

Koeduka Takao T   Fujita Yoshiyuki Y   Furuta Takumi T   Suzuki Hideyuki H   Tsuge Tomohiko T   Matsui Kenji K  

Plant biotechnology (Tokyo, Japan) 20171202 4


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 <i>AADC</i> genes (<i>EjAADC1</i> and <i>EjAADC2</i>) were isolated from loquat (<i>Eriobotrya japonica</i>) flowers. The EjAADC1 and EjAADC2 proteins showed approximately 72% and 55% identity, respect  ...[more]

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