ArticlePlanta2019
A BAHD hydroxycinnamoyltransferase from Actaea racemosa catalyses the formation of fukinolic and cimicifugic acids.
Article in Planta, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 9 citations in OpenAlex.
- Article
- Genome-wide identification and expression analysis of the BAHD gene family inFrontiers in genetics · 2024Article
- Complete biosynthesis of the phenylethanoid glycoside verbascoside.Plant communications · 2023Article
- Chemical Synthesis ofMolecules (Basel, Switzerland) · 2022Article
- Characterization of Two BAHD Acetyltransferases Highly Expressed in the Flowers ofPlants (Basel, Switzerland) · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MAIN
conclusionThe nucleotide sequence of a BAHD hydroxycinnamoyltransferase was amplified from Actaea racemosa (Ranunculaceae) and expressed in E. coli. The protein catalysed the formation of cimicifugic acids and thus is named hydroxycinnamoyl-CoA:piscidic acid hydroxycinnamoyltransferase (ArHPT1; cimicifugic acid synthase). Actaea racemosa (syn. Cimicifuga racemosa) is known to contain triterpene lactone glycosides and cimicifugic acids. The latter are esters of various hydroxycinnamic or benzoic acids with piscidic or fukiic acid. Amplification of a nucleotide sequence from A. racemosa, that was already known as HCT1 from an EST approach, and its expression in E. coli resulted in a protein that was able to catalyse the formation of several cimicifugic acids. For the characterisation of this hydroxycinnamoyltransferase (hydroxy)cinnamoyl-coenzyme A thioesters were synthesised as donor substrates and piscidic acid isolated as acceptor substrate. The lowest K
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Registered trials
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