Plant Physiol BiochemJClub
Vanillin aminotransferase-like homologues from Solanaceae beyond Capsicum species show differential capacity to support vanillylamine accumulation in planta.
Plant Physiology and Biochemistry · · Journal Article · Open access
Akhgari, Klepper + 1 more
Abstract ↗AI summary
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Tomato VAMT-like homologues SlVAMT1 and SlVAMT2 supported substantially higher vanillylamine accumulation than the Capsicum reference enzyme in transient Nicotiana benthamiana leaves after vanillin feeding.
- Why it matters: It was unclear whether VAMT-like vanillylamine-forming activity is functionally restricted to Capsicum or broadly retained across related Solanaceae homologues in a plant context.
- What they did: The study built an LC-MS/MS workflow to quantify vanillin, vanillylamine, and vanillyl alcohol, then used transient N. benthamiana leaf assays with vanillin feeding to test Capsicum, tomato, and tobacco VAMT-like proteins.
- The result: SlVAMT3 produced no detectable vanillylamine above empty vector, while NtVAMT1 increased accumulation but NtVAMT2 and tested N. benthamiana homologues did not, showing strong functional divergence among closely related enzymes.
The findingWhy it mattersWhat they didThe result
- Open access