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Differential metabolism of L–phenylalanine in the formation of aromatic volatiles in melon (Cucumis melo L.) fruit

Author:
Gonda, Itay, Davidovich-Rikanati, Rachel, Bar, Einat, Lev, Shery, Jhirad, Pliaa, Meshulam, Yuval, Wissotsky, Guy, Portnoy, Vitaly, Burger, Joseph, Schaffer, Arthur A., Tadmor, Yaakov, Giovannoni, James J., Fei, Zhangjun, Fait, Aaron, Katzir, Nurit, Lewinsohn, Efraim
Source:
Phytochemistry 2018 v.148 pp. 122-131
ISSN:
0031-9422
Subject:
Cucumis melo, NADP (coenzyme), adenosine triphosphate, biosynthesis, fruit peels, fruits, genes, magnesium sulfate, melons, methyltransferases, phenylalanine, phenylalanine ammonia-lyase, stable isotopes
Abstract:
Studies on the active pathways and the genes involved in the biosynthesis of L-phenylalanine-derived volatiles in fleshy fruits are sparse. Melon fruit rinds converted stable-isotope labeled L-phe into more than 20 volatiles. Phenylpropanes, phenylpropenes and benzenoids are apparently produced via the well-known phenylpropanoid pathway involving phenylalanine ammonia lyase (PAL) and being (E)-cinnamic acid a key intermediate. Phenethyl derivatives seemed to be derived from L-phe via a separate biosynthetic route not involving (E)-cinnamic acid and PAL. To explore for a biosynthetic route to (E)-cinnamaldehyde in melon rinds, soluble protein cell-free extracts were assayed with (E)-cinnamic acid, CoA, ATP, NADPH and MgSO4, producing (E)-cinnamaldehyde in vitro. In this context, we characterized CmCNL, a gene encoding for (E)-cinnamic acid:coenzyme A ligase, inferred to be involved in the biosynthesis of (E)-cinnamaldehyde. Additionally we describe CmBAMT, a SABATH gene family member encoding a benzoic acid:S-adenosyl-L-methionine carboxyl methyltransferase having a role in the accumulation of methyl benzoate. Our approach leads to a more comprehensive understanding of L-phe metabolism into aromatic volatiles in melon fruit.
Agid:
5906689