ArticleCommunications biology2020
A GDSL lipase-like from Ipomoea batatas catalyzes efficient production of 3,5-diCQA when expressed in Pichia pastoris.
Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Completing the acylation landscape in plants: GDSL enzymes join the BAHD and SCPL acyltransferase families.Journal of experimental botany · 2026Review
- Recent Advances in Biosynthesis and Bioactivity of Plant Caffeoylquinic Acids.Current issues in molecular biology · 2025Review
- Graph-based pangenomes and pan-phenome provide a cornerstone for eggplant biology and breeding.Nature communications · 2025Article
- Identification of the first plant caffeoyl-quinate esterases inFrontiers in plant science · 2025Article
- Advances in Production of Hydroxycinnamoyl-Quinic Acids: From Natural Sources to Biotechnology.Antioxidants (Basel, Switzerland) · 2022Review
- Caffeoylquinic acids: chemistry, biosynthesis, occurrence, analytical challenges, and bioactivity.The Plant journal : for cell and molecular biology · 2021Review
- Sprout Caffeoylquinic Acid Profiles as Affected by Variety, Cooking, and Storage.Frontiers in nutrition · 2021Article
- Plant-Derived Compounds as Promising Therapeutics for Vitiligo.Frontiers in pharmacology · 2021Review
Corrections and comments
- Erratum issued
Authors and funding
16 authors at 6 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The synthesis of 3,5-dicaffeoylquinic acid (3,5-DiCQA) has attracted the interest of many researchers for more than 30 years. Recently, enzymes belonging to the BAHD acyltransferase family were shown to mediate its synthesis, albeit with notably low efficiency. In this study, a new enzyme belonging to the GDSL lipase-like family was identified and proven to be able to transform chlorogenic acid (5-O-caffeoylquinic acid, 5-CQA, CGA) in 3,5-DiCQA with a conversion rate of more than 60%. The enzyme has been produced in different expression systems but has only been shown to be active when transiently synthesized in Nicotiana benthamiana or stably expressed in Pichia pastoris. The synthesis of the molecule could be performed in vitro but also by a bioconversion approach beginning from pure 5-CQA or from green coffee bean extract, thereby paving the road for producing it on an industrial scale.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.