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Keywords = bornyl diphosphate synthase

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14 pages, 2756 KB  
Article
Mechanistic Insights into the Bornyl Diphosphate Synthase from Lavandula angustifolia
by Dafeng Liu, Na Li, Feng Yu, Yanyan Du, Hongjun Song and Wenshuang Yao
Curr. Issues Mol. Biol. 2025, 47(7), 517; https://doi.org/10.3390/cimb47070517 - 4 Jul 2025
Cited by 3 | Viewed by 970
Abstract
Lavender species hold substantial economic importance due to their widespread cultivation for essential oils (EOs). Lavender EOs contain terpenes essential for industries such as cosmetics, personal care, and pharmaceuticals. In the biosynthetic pathway of EOs, Lavandula angustifolia bornyl diphosphate synthase (LaBPPS) catalyzes the [...] Read more.
Lavender species hold substantial economic importance due to their widespread cultivation for essential oils (EOs). Lavender EOs contain terpenes essential for industries such as cosmetics, personal care, and pharmaceuticals. In the biosynthetic pathway of EOs, Lavandula angustifolia bornyl diphosphate synthase (LaBPPS) catalyzes the conversion of geranyl diphosphate (GPP) to bornyl diphosphate (BPP). However, the functional mechanisms of LaBPPS remain poorly understood. Here, we conducted mutational experiments based on the molecular docking results, and found that mutations at positions D356A, D360A, R497A, D501A, or E508A led to a 50- to 100-fold reduction in the activity. Deletion of region 1–58 (∆1–58) did not affect activity compared to the wild-type (WT) protein, while deletions of regions 1–74 or 59–74 (∆1–74 or ∆59–74) significantly decreased the activity. Conversely, deletion of residues 578–602 (∆578–602) dramatically increased the activity. The LaBPPS gene showed dramatically higher expression levels in flowers compared to other tissues (stems, leaves and roots), peaking at 8:00. Our results provide valuable insights into EO biosynthesis in lavender and suggest potential strategies for genetic engineering aimed at improving EO quality. Full article
(This article belongs to the Section Molecular Plant Sciences)
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19 pages, 18021 KB  
Article
Biosynthesis of Camphane Volatile Terpenes in Amomum villosum Lour: Involved Genes and Enzymes
by Yuhua Guo, Yamei Li, Pengfei Zhang, Zuliang Luo, Junmei Yin, Xiaojun Ma and Chao Yuan
Plants 2025, 14(12), 1767; https://doi.org/10.3390/plants14121767 - 10 Jun 2025
Cited by 1 | Viewed by 1485
Abstract
Amomum villosum (A. villosum) Lour., a medicinal species of the Zingiberaceae family, is used for medical purposes. Bornyl acetate, camphor, and borneol are the main bioactive ingredients in A. villosum fruit, and the amount of bornyl acetate is regarded as a [...] Read more.
Amomum villosum (A. villosum) Lour., a medicinal species of the Zingiberaceae family, is used for medical purposes. Bornyl acetate, camphor, and borneol are the main bioactive ingredients in A. villosum fruit, and the amount of bornyl acetate is regarded as a measure of the fruit’s quality. In order to explore the major effective genes regulating the biosynthesis of camphane volatile terpenes in A. villosum, some DEGs involved in camphane volatile terpene biosynthesis and transcription factors were analyzed and summarized in this study. The result showed that the content of bornyl acetate was altered in the different growth stages. In particular, the significant change occurred from 7 to 30 DAP (days after pollination). The content of bornyl acetate at 30 DAP was 169.3% more than that at 7 DAP. In total, 4782 up-regulated and 5284 down-regulated unigenes were found in G2 vs. G1, as well as 3324 up-regulated and 5036 down-regulated unigenes in G3 vs. G1, and 3332 up-regulated and 4490 down-regulated unigenes in G3 vs. G2. A total of 323 up-regulated and 820 down-regulated unigenes were shared in three growth stage comparisons. We screened the genes that encode the enzymes most likely to inhibit bornyl diphosphate synthase, borneol dehydrogenase, and BAHD acyltransferases. Interestingly, we found that borneol dehydrogenase and bornyl diphosphate synthase displayed bi-substrate features, suggesting that a substrate of catalyzation is promiscuity in the biosynthesis downstream pathway, and the unknown bornyl pyrophosphate hydrolase may not be the specific enzyme for borneol formation. Additionally, the DXR, HDS, and IDS found in the PPI network would assist in the understanding of molecular regulation. The results of this study constructed DGE libraries and identified key genes related to camphane volatile terpenes, which laid a foundation for a deep investigation of the mechanism of volatile terpene biosynthesis, and provided a reference for mining other key genes in A. villosum fruits. Full article
(This article belongs to the Section Plant Molecular Biology)
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