Worldwide, there are plants known as psychoactive plants that naturally contain psychedelic active components. They have a high concentration of neuroprotective substances that can interact with the nervous system to produce psychedelic effects. Despite these plants' hazardous potential, recreational use of them is on the rise because of their psychoactive properties. Early neuroscience studies relied heavily on psychoactive plants and plant natural products (NPs), and both recreational and hazardous NPs have contributed significantly to the understanding of almost all neurotransmitter systems. Worldwide, there are many plants that contain psychoactive properties, and people have been using them for ages. Psychoactive plant compounds may significantly alter how people perceive the world.
1. Org Lett. 2024 Feb 16;26(6):1233-1237. doi: 10.1021/acs.orglett.4c00042. Epub 2024 Feb 3. A Secreted BBE-Like Enzyme Acting as a Drug-Binding Efflux Carrier Confers Microbial Self-Resistance to Mitomycin C. Chen X(1), He R(1), Sun A(1), Pu J(1), Pan HX(1)(2), Tang GL(1)(2). Author information: (1)School of Chemistry and Materials Science, Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences, Hangzhou 310024, China. (2)State Key Laboratory of Chemical Biology, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China. The berberine bridge enzyme (BBE)-like flavoproteins have attracted continuous attention for their capability to catalyze various oxidative reactions. Here we demonstrate that MitR, a secreted BBE-like enzyme, functions as a special drug-binding efflux protein evolved from quinone reductase. Moreover, this protein provides self-resistance to its hosts toward the DNA-alkylating agent mitomycin C with a distinctive strategy, featured by independently performing drug binding and efflux. DOI: 10.1021/acs.orglett.4c00042 PMID: 38308850 [Indexed for MEDLINE] 2. Org Lett. 2024 Jan 26;26(3):642-646. doi: 10.1021/acs.orglett.3c03966. Epub 2024 Jan 12. A Berberine Bridge Enzyme-like Oxidase Mediates the Cage-like Acresorbicillinol C Biosynthesis. Wang S(1)(2), Wang M(3), Duan C(1)(2), Yao Y(1), Ren J(1), Liu L(1)(2), Pan Y(1), Liu G(1)(2). Author information: (1)State Key Laboratory of Mycology, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China. (2)University of Chinese Academy of Sciences, Beijing 100049, China. (3)School of Biotechnology and Health Sciences, Wuyi University, Jiangmen 529020, China. Oxosorbicillinol and cage-like acresorbicillinol C are bioactive sorbicillinoids produced by Acremonium chrysogenum. We found that a berberine bridge enzyme-like oxidase AcsorD was responsible for their biosynthesis by gene deletion and heterologous expression. AcsorD catalyzed oxidation of sorbicillinol to form oxosorbicillinol in in vitro assays, which was successively condensed with sorbicillinol to form acresorbicillinol C spontaneously. Finally, site-directed mutation revealed that Tyr525 was the key residue in the catalysis of the oxidation reaction and unlocking cage-like acresorbicillinol C production. DOI: 10.1021/acs.orglett.3c03966 PMID: 38214302 [Indexed for MEDLINE] 3. J Agric Food Chem. 2023 Dec 20;71(50):19986-19999. doi: 10.1021/acs.jafc.3c06280. Epub 2023 Dec 8. Genome-Wide Characterization of Berberine Bridge Enzyme Gene Family in Wheat (Triticum aestivum L.) and the Positive Regulatory Role of TaBBE64 in Response to Wheat Stripe Rust. Yu L(1), Wang X(1), Tang C(1), Wang H(2), Rabbani Nasab H(3), Kang Z(1), Wang J(1). Author information: (1)State Key Laboratory of Crop Stress Biology for Arid Areas and College of Plant Protection, Northwest A & F University, Yangling 712100, P. R. China. (2)Plant Protection Station of Xinjiang Uygur Autonomous Region, Urumqi 830006, Xinjiang, P. R. China. (3)Plant Protection Research Department, Agricultural and Natural Resources Research and Education Centre of Golestan Province, Agricultural Research Education and Extension Organization (AREEO), Gorgan 999067, Iran. Berberine bridge enzymes (BBEs), functioning as carbonate oxidases, enhance disease resistance in Arabidopsis and tobacco. However, the understanding of BBEs' role in monocots against pathogens remains limited. This study identified 81 TaBBEs with FAD_binding_4 and BBE domains. Phylogenetic analysis revealed a separation of the BBE gene family between monocots and dicots. Notably, RNA-seq showed TaBBE64's significant induction by both pathogen-associated molecular pattern treatment and Puccinia striiformis f. sp. tritici (Pst) infection at early stages. Subcellular localization revealed TaBBE64 at the cytoplasmic membrane. Knocking down TaBBE64 compromised wheat's Pst resistance, reducing reactive oxygen species and promoting fungal growth, confirming its positive role. Molecular docking and enzyme activity assays confirmed TaBBE64's glucose oxidation to produce H2O2. Since Pst relies on living wheat cells for carbohydrate absorption, TaBBE64's promotion of glucose oxidation limits fungal growth and resists pathogen infection. This study sheds light on BBEs' role in wheat resistance against biotrophic fungi. DOI: 10.1021/acs.jafc.3c06280 PMID: 38063491 [Indexed for MEDLINE] 4. Plant Physiol. 2023 Dec 30;194(1):296-313. doi: 10.1093/plphys/kiad457. Berberine bridge enzyme-like oxidases of cellodextrins and mixed-linked β-glucans control seed coat formation. Costantini S(1), Benedetti M(2), Pontiggia D(1)(3), Giovannoni M(2), Cervone F(1), Mattei B(2), De Lorenzo G(1). Author information: (1)Department of Biology and Biotechnology "C. Darwin", Sapienza University of Rome, 00185 Rome, Italy. (2)Department of Life, Health and Environmental Sciences, University of L'Aquila, 67100 L'Aquila, Italy. (3)Research Center for Applied Sciences to the Safeguard of Environment and Cultural Heritage (CIABC), Sapienza University of Rome, 00185 Rome, Italy. Plants have evolved various resistance mechanisms to cope with biotic stresses that threaten their survival. The BBE23 member (At5g44360/BBE23) of the Arabidopsis berberine bridge enzyme-like (BBE-l) protein family (Arabidopsis thaliana) has been characterized in this paper in parallel with the closely related and previously described CELLOX (At4g20860/BBE22). In addition to cellodextrins, both enzymes, renamed here as CELLODEXTRIN OXIDASE 2 and 1 (CELLOX2 and CELLOX1), respectively, oxidize the mixed-linked β-1→3/β-1→4-glucans (MLGs), recently described as capable of activating plant immunity, reinforcing the view that the BBE-l family includes members that are devoted to the control of the homeostasis of potential cell wall-derived damage-associated molecular patterns (DAMPs). The 2 putatively paralogous genes display different expression profiles. Unlike CELLOX1, CELLOX2 is not expressed in seedlings or adult plants and is not involved in immunity against Botrytis cinerea. Both are instead expressed in a concerted manner in the seed coat during development. Whereas CELLOX2 is expressed mainly during the heart stage, CELLOX1 is expressed at the immediately later stage, when the expression of CELLOX2 decreases. Analysis of seeds of cellox1 and cellox2 knockout mutants shows alterations in the coat structure: the columella area is smaller in cellox1, radial cell walls are thicker in both cellox1 and cellox2, and the mucilage halo is reduced in cellox2. However, the coat monosaccharide composition is not significantly altered, suggesting an alteration of the organization of the cell wall, thus reinforcing the notion that the architecture of the cell wall in specific organs is determined not only by the dynamics of the synthesis/degradation of the main polysaccharides but also by its enzymatic oxidation. © American Society of Plant Biologists 2023. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com. DOI: 10.1093/plphys/kiad457 PMID: 37590952 [Indexed for MEDLINE] Conflict of interest statement: Conflict of interest statement. The authors declare no conflict of interest. 5. Sci Rep. 2023 Mar 13;13(1):4123. doi: 10.1038/s41598-023-31335-y. Radical cation scavenging activity of berberine bridge enzyme-like oligosaccharide oxidases acting on short cell wall fragments. Scortica A(#)(1), Scafati V(#)(1), Giovannoni M(#)(1), Benedetti M(2), Mattei B(1). Author information: (1)Department of Life, Health and Environmental Sciences, University of L'Aquila, 67100, L'Aquila, Italy. (2)Department of Life, Health and Environmental Sciences, University of L'Aquila, 67100, L'Aquila, Italy. manuel.benedetti@univaq.it. (#)Contributed equally Oligogalacturonide-oxidases (OGOXs) and cellodextrin-oxidase (CELLOX) are plant berberine bridge enzyme-like oligosaccharide-oxidases (OSOXs) that oxidize, respectively, oligogalacturonides (OGs) and cellodextrins (CDs), thereby inactivating their elicitor nature and concomitantly releasing H2O2. Little is known about the physiological role of OSOX activity. By using an ABTS·+-reduction assay, we identified a novel reaction mechanism through which the activity of OSOXs on cell wall oligosaccharides scavenged the radical cation ABTS·+ with an efficiency dependent on the type and length of the oxidized oligosaccharide. In contrast to the oxidation of longer oligomers such as OGs (degree of polymerization from 10 to 15), the activity of OSOXs on short galacturonan- and cellulose-oligomers (degree of polymerization ≤ 4) successfully counteracted the radical cation-generating activity of a fungal laccase, suggesting that OSOXs can generate radical cation scavenging activity in the apoplast with a power proportional to the extent of degradation of the plant cell wall, with possible implications for redox homeostasis and defense against oxidative stress. © 2023. The Author(s). DOI: 10.1038/s41598-023-31335-y PMCID: PMC10011498 PMID: 36914850 [Indexed for MEDLINE] Conflict of interest statement: The authors declare no competing interests.