|
type |
Journal Article |
authors |
Sakai M, Hirata H, Sayama H, Sekiguchi K, Itano H, Asai T, Dohra H, Hara M, Watanabe N. |
title |
Production of 2-phenylethanol in roses as the dominant floral scent compound from L-phenylalanine by two key enzymes, a PLP-dependent decarboxylase and a phenylacetaldehyde reductase |
journal |
Biosci Biotechnol Biochem |
Activity |
4.1.1.109 |
Family |
4.1.1.109.a |
sel |
unselected |
ui |
17928708 |
year |
(2007) |
volume |
71 |
number |
10 |
pages |
2408-19 |
| |
abstract |
We investigated the biosynthetic pathway for 2-phenylethanol, the dominant floral scent compound in roses, using enzyme assays. L-[(2)H8] Phenylalanine was converted to [(2)H8] phenylacetaldehyde and [(2)H8]-2-phenylethanol by two enzymes derived from the flower petals of R. 'Hoh-Jun,' these being identified as pyridoxal-5'-phosphate-dependent L-aromatic amino acid decarboxylase (AADC) and phenylacetaldehyde reductase (PAR). The activity of rose petal AADC to yield phenylacetaldehyde was nine times higher toward L-phenylalanine than toward its D-isomer, and this conversion was not inhibited by iproniazid, a specific inhibitor of monoamine oxidase. Under aerobic conditions, rose petal AADC stoichiometrically produced NH3 together with phenylacetaldehyde during the course of decarboxylation and oxidation, followed by the hydrolysis of L-phenylalanine. Phenylacetaldehyde was subsequently converted to 2-phenylethanol by the action of PAR. PAR showed specificity toward several volatile aldehydes. |
last changed |
2018/05/03 11:17 |
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