Evidence map›Paper›PMID 40276033›Full record

ArticleFrontiers in bioengineering and biotechnology2025

Biosynthesis of novel cannabigerolic acid derivatives by engineering the substrate specificity of aromatic prenyltransferase.

Hoe-Suk Lee, Jisu Park, Taejung Kim, Huitae Min, Seongsu Na, Soon Young Park, Young-Tae Park, Young Joo Yeon, Jungyeob Ham

Abstract read
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

9 authors.

Hoe-Suk Lee *Department of Biochemical Engineering, Gangneung-Wonju National University, Gangneung, Republic of Korea.
Jisu Park *Department of Biochemical Engineering, Gangneung-Wonju National University, Gangneung, Republic of Korea.
Taejung KimNatural Product Research Center, Korea Institute of Science and Technology (KIST), Gangneung, Republic of Korea.
Huitae MinNatural Product Research Center, Korea Institute of Science and Technology (KIST), Gangneung, Republic of Korea.
Seongsu NaDepartment of Biochemical Engineering, Gangneung-Wonju National University, Gangneung, Republic of Korea.
Soon Young ParkNeoCannBio Co., Ltd., Seoul, Republic of Korea.
Young-Tae ParkNatural Product Research Center, Korea Institute of Science and Technology (KIST), Gangneung, Republic of Korea.
Young Joo YeonDepartment of Biochemical Engineering, Gangneung-Wonju National University, Gangneung, Republic of Korea.
Jungyeob HamNatural Product Research Center, Korea Institute of Science and Technology (KIST), Gangneung, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Introduction: Cannabinoids possess significant therapeutic potential, but their natural chemical diversity derived from plant biosynthesis is limited. Efficient biotransformation processes are required to expand the range of accessible cannabinoids. This study aimed to enhance the selective biosynthesis of cannabigerolic acid (CBGA) and its derivatives with varying aliphatic chain lengths, which serve as key precursors to various cannabinoids. Methods: We employed computational modeling and structure-guided mutagenesis to engineer the aromatic prenyltransferase NphB. Mutants were designed via Results: Engineered NphB variants exhibited significant improvements, with triple mutants achieving a 7-fold increase in CBGA production and a 4-fold increase in cannabigerovarinic acid production. Additionally, a single mutant also enhanced the synthesis of 3-geranyl orsellinic acid by 1.3-fold. Notably, novel enzymatic activity was identified that enabled the biosynthesis of 3-geranyl-2,4-dihydroxybenzoic acid. Structural analyses revealed that the mutations improved the spatial positioning of aromatic substrates relative to the co-substrate geranyl pyrophosphate. Discussion: This study demonstrates the feasibility of enzyme design to tailor prenyltransferase specificity for the production of diverse CBGA derivatives. These findings lay the groundwork for the microbial production of novel cannabinoids and offer promising potential for the development of scalable biocatalytic systems for therapeutic and industrial applications.

Indexed as

aromatic prenyltransferase NphBbiocatalytic systemcannabigerolic acid derivativecannabinoidcomputational enzyme designengineered E. coli whole cell

Identifiers

PMID40276033
PMCPMC12018323

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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.