Atypical phenylalanine ammonia-lyases that enhance phenylpropanoid production in plants.

PALnc atypical phenylalanine ammonia-lyases from Elaeis guineensis and Piper methysticum enhance phenylpropanoid accumulation in Nicotiana benthamiana leaves.

• Why it matters: PAL activity is tightly regulated and limits phenylpropanoid output, yet how different plant species control PAL enzymes remains unclear.
• What they did: Phylogeny-guided biochemical screening across 14 plant species mapped complex feedback regulation and identified a PALnc clade with in vitro activation by p-coumaric acid, caffeic acid, and 4-hydroxyphenylpyruvic acid. Transient expression of EgPALnc and PmPALnc2 in N. benthamiana leaves tested in planta effects.
• The result: EgPALnc and PmPALnc2 increased phenylpropanoid content, supported by higher in planta PALnc protein stability versus canonical PALs; in contrast, overexpressing Arabidopsis thaliana PAL1 produced very low AtPAL1 protein and minor metabolic changes. EgPALnc enabled hyperaccumulation of hydroxycinnamate derivatives, suggesting PALnc enzymes can debottleneck phenylpropanoid biosynthesis in planta.

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