Academic literature on the topic 'Sesquiterpene synthases'
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Journal articles on the topic "Sesquiterpene synthases"
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Yan, Xiaoguang, Yukun Li, Weiguo Li, Dongmei Liang, Shengxin Nie, Ruiqi Chen, Jianjun Qiao, Mingzhang Wen, and Qinggele Caiyin. "Transcriptome Analysis and Identification of Sesquiterpene Synthases in Liverwort Jungermannia exsertifolia." Bioengineering 10, no. 5 (May 9, 2023): 569. http://dx.doi.org/10.3390/bioengineering10050569.
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The liverwort Jungermannia exsertifolia is one of the oldest terrestrial plants and rich in structurally specific sesquiterpenes. There are several sesquiterpene synthases (STSs) with non-classical conserved motifs that have been discovered in recent studies on liverworts; these motifs are rich in aspartate and bind with cofactors. However, more detailed sequence information is needed to clarify the biochemical diversity of these atypical STSs. This study mined J. exsertifolia sesquiterpene synthases (JeSTSs) through transcriptome analysis using BGISEQ-500 sequencing technology. A total of 257,133 unigenes was obtained, and the average length was 933 bp. Among them, a total of 36 unigenes participated in the biosynthesis of sesquiterpenes. In addition, the in vitro enzymatic characterization and heterologous expression in Saccharomyces cerevisiae showed that JeSTS1 and JeSTS2 produced nerolidol as the major product, while JeSTS4 could produce bicyclogermacrene and viridiflorol, suggesting a specificity of J. exsertifolia sesquiterpene profiles. Furthermore, the identified JeSTSs had a phylogenetic relationship with a new branch of plant terpene synthases, the microbial terpene synthase-like (MTPSL) STSs. This work contributes to the understanding of the metabolic mechanism for MTPSL-STSs in J. exsertifolia and could provide an efficient alternative to microbial synthesis of these bioactive sesquiterpenes.
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Beran, Franziska, Peter Rahfeld, Katrin Luck, Raimund Nagel, Heiko Vogel, Natalie Wielsch, Sandra Irmisch, et al. "Novel family of terpene synthases evolved from trans-isoprenyl diphosphate synthases in a flea beetle." Proceedings of the National Academy of Sciences 113, no. 11 (March 2, 2016): 2922–27. http://dx.doi.org/10.1073/pnas.1523468113.
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Sesquiterpenes play important roles in insect communication, for example as pheromones. However, no sesquiterpene synthases, the enzymes involved in construction of the basic carbon skeleton, have been identified in insects to date. We investigated the biosynthesis of the sesquiterpene (6R,7S)-himachala-9,11-diene in the crucifer flea beetle Phyllotreta striolata, a compound previously identified as a male-produced aggregation pheromone in several Phyllotreta species. A (6R,7S)-himachala-9,11-diene–producing sesquiterpene synthase activity was detected in crude beetle protein extracts, but only when (Z,E)-farnesyl diphosphate [(Z,E)-FPP] was offered as a substrate. No sequences resembling sesquiterpene synthases from plants, fungi, or bacteria were found in the P. striolata transcriptome, but we identified nine divergent putative trans-isoprenyl diphosphate synthase (trans-IDS) transcripts. Four of these putative trans-IDSs exhibited terpene synthase (TPS) activity when heterologously expressed. Recombinant PsTPS1 converted (Z,E)-FPP to (6R,7S)-himachala-9,11-diene and other sesquiterpenes observed in beetle extracts. RNAi-mediated knockdown of PsTPS1 mRNA in P. striolata males led to reduced emission of aggregation pheromone, confirming a significant role of PsTPS1 in pheromone biosynthesis. Two expressed enzymes showed genuine IDS activity, with PsIDS1 synthesizing (E,E)-FPP, whereas PsIDS3 produced neryl diphosphate, (Z,Z)-FPP, and (Z,E)-FPP. In a phylogenetic analysis, the PsTPS enzymes and PsIDS3 were clearly separated from a clade of known coleopteran trans-IDS enzymes including PsIDS1 and PsIDS2. However, the exon–intron structures of IDS and TPS genes in P. striolata are conserved, suggesting that this TPS gene family evolved from trans-IDS ancestors.
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Cong, Zhanren, Qiang Yin, Kunhong Tian, Njeru Joe Mukoma, Liming Ouyang, Tom Hsiang, Lixin Zhang, Lan Jiang, and Xueting Liu. "Genome Mining of Fungal Unique Trichodiene Synthase-like Sesquiterpene Synthases." Journal of Fungi 10, no. 5 (May 13, 2024): 350. http://dx.doi.org/10.3390/jof10050350.
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Sesquiterpenoids served as an important source for natural product drug discovery. Although genome mining approaches have revealed numerous novel sesquiterpenoids and biosynthetic enzymes, the comprehensive landscape of fungal sesquiterpene synthases (STSs) remains elusive. In this study, 123 previously reported fungal STSs were subjected to phylogenetic analysis, resulting in the identification of a fungi-specific STS family known as trichodiene synthase-like sesquiterpene synthases (TDTSs). Subsequently, the application of hidden Markov models allowed the discovery of 517 TDTSs from our in-house fungi genome library of over 400 sequenced genomes, and these TDTSs were defined into 79 families based on a sequence similarity network. Based on the novelty of protein sequences and the completeness of their biosynthetic gene clusters, 23 TDTS genes were selected for heterologous expression in Aspergillus oryzae. In total, 10 TDTSs were active and collectively produced 12 mono- and sesquiterpenes, resulting in the identification of the first chamipinene synthase, as well as the first fungi-derived cedrene, sabinene, and camphene synthases. Additionally, with the guidance of functionally characterized TDTSs, we found that TDTSs in Family 1 could produce bridged-cyclic sesquiterpenes, while those in Family 2 could synthesize spiro- and bridged-cyclic sesquiterpenes. Our research presents a new avenue for the genome mining of fungal sesquiterpenoids.
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Silva, Waldeyr M. C. da, Jakob L. Andersen, Maristela T. Holanda, Maria Emília M. T. Walter, Marcelo M. Brigido, Peter F. Stadler, and Christoph Flamm. "Exploring Plant Sesquiterpene Diversity by Generating Chemical Networks." Processes 7, no. 4 (April 25, 2019): 240. http://dx.doi.org/10.3390/pr7040240.
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Plants produce a diverse portfolio of sesquiterpenes that are important in their response to herbivores and the interaction with other plants. Their biosynthesis from farnesyl diphosphate depends on the sesquiterpene synthases that admit different cyclizations and rearrangements to yield a blend of sesquiterpenes. Here, we investigate to what extent sesquiterpene biosynthesis metabolic pathways can be reconstructed just from the knowledge of the final product and the reaction mechanisms catalyzed by sesquiterpene synthases. We use the software package MedØlDatschgerl (MØD) to generate chemical networks and to elucidate pathways contained in them. As examples, we successfully consider the reachability of the important plant sesquiterpenes β -caryophyllene, α -humulene, and β -farnesene. We also introduce a graph database to integrate the simulation results with experimental biological evidence for the selected predicted sesquiterpenes biosynthesis.
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Ker, De-Sheng, Sze Lei Pang, Noor Farhan Othman, Sekar Kumaran, Ee Fun Tan, Thiba Krishnan, Kok Gan Chan, Roohaida Othman, Maizom Hassan, and Chyan Leong Ng. "Purification and biochemical characterization of recombinant Persicaria minor β-sesquiphellandrene synthase." PeerJ 5 (February 28, 2017): e2961. http://dx.doi.org/10.7717/peerj.2961.
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Background Sesquiterpenes are 15-carbon terpenes synthesized by sesquiterpene synthases using farnesyl diphosphate (FPP) as a substrate. Recently, a sesquiterpene synthase gene that encodes a 65 kDa protein was isolated from the aromatic plant Persicaria minor. Here, we report the expression, purification and characterization of recombinant P. minor sesquiterpene synthase protein (PmSTS). Insights into the catalytic active site were further provided by structural analysis guided by multiple sequence alignment. Methods The enzyme was purified in two steps using affinity and size exclusion chromatography. Enzyme assays were performed using the malachite green assay and enzymatic product was identified using gas chromatography-mass spectrometry (GC-MS) analysis. Sequence analysis of PmSTS was performed using multiple sequence alignment (MSA) against plant sesquiterpene synthase sequences. The homology model of PmSTS was generated using I-TASSER server. Results Our findings suggest that the recombinant PmSTS is mainly expressed as inclusion bodies and soluble aggregate in the E. coli protein expression system. However, addition of 15% (v/v) glycerol to the protein purification buffer and removal of N-terminal 24 amino acids of PmSTS helped to produce homogenous recombinant protein. Enzyme assay showed that recombinant PmSTS is active and specific to the C15 substrate FPP. The optimal temperature and pH for the recombinant PmSTS are 30 °C and pH 8.0, respectively. The GC-MS analysis further showed that PmSTS produces β-sesquiphellandrene as a major product and β-farnesene as a minor product. MSA analysis revealed that PmSTS adopts a modified conserved metal binding motif (NSE/DTE motif). Structural analysis suggests that PmSTS may binds to its substrate similarly to other plant sesquiterpene synthases. Discussion The study has revealed that homogenous PmSTS protein can be obtained with the addition of glycerol in the protein buffer. The N-terminal truncation dramatically improved the homogeneity of PmSTS during protein purification, suggesting that the disordered N-terminal region may have caused the formation of soluble aggregate. We further show that the removal of the N-terminus disordered region of PmSTS does not affect the product specificity. The optimal temperature, optimal pH, Km and kcat values of PmSTS suggests that PmSTS shares similar enzyme characteristics with other plant sesquiterpene synthases. The discovery of an altered conserved metal binding motif in PmSTS through MSA analysis shows that the NSE/DTE motif commonly found in terpene synthases is able to accommodate certain level of plasticity to accept variant amino acids. Finally, the homology structure of PmSTS that allows good fitting of substrate analog into the catalytic active site suggests that PmSTS may adopt a sesquiterpene biosynthesis mechanism similar to other plant sesquiterpene synthases.
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Ee, Su-Fang, Zeti-Azura Mohamed-Hussein, Roohaida Othman, Noor Azmi Shaharuddin, Ismanizan Ismail, and Zamri Zainal. "Functional Characterization of Sesquiterpene Synthase fromPolygonum minus." Scientific World Journal 2014 (2014): 1–11. http://dx.doi.org/10.1155/2014/840592.
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Polygonum minusis an aromatic plant, which contains high abundance of terpenoids, especially the sesquiterpenes C15H24. Sesquiterpenes were believed to contribute to the many useful biological properties in plants. This study aimed to functionally characterize a full length sesquiterpene synthase gene fromP. minus.P. minussesquiterpene synthase (PmSTS) has a complete open reading frame (ORF) of 1689 base pairs encoding a 562 amino acid protein. Similar to other sesquiterpene synthases, PmSTS has two large domains: the N-terminal domain and the C-terminal metal-binding domain. It also consists of three conserved motifs: the DDXXD, NSE/DTE, and RXR. A three-dimensional protein model for PmSTS built clearly distinguished the two main domains, where conserved motifs were highlighted. We also constructed a phylogenetic tree, which showed that PmSTS belongs to the angiosperm sesquiterpene synthase subfamily Tps-a. To examine the function ofPmSTS, we expressed this gene inArabidopsis thaliana. Two transgenic lines, designated asOE3andOE7, were further characterized, both molecularly and functionally. The transgenic plants demonstrated smaller basal rosette leaves, shorter and fewer flowering stems, and fewer seeds compared to wild type plants. Gas chromatography-mass spectrometry analysis of the transgenic plants showed that PmSTS was responsible for the production ofβ-sesquiphellandrene.
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Yamada, Yuuki, Tomohisa Kuzuyama, Mamoru Komatsu, Kazuo Shin-ya, Satoshi Omura, David E. Cane, and Haruo Ikeda. "Terpene synthases are widely distributed in bacteria." Proceedings of the National Academy of Sciences 112, no. 3 (December 22, 2014): 857–62. http://dx.doi.org/10.1073/pnas.1422108112.
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Odoriferous terpene metabolites of bacterial origin have been known for many years. In genome-sequencedStreptomycetaceaemicroorganisms, the vast majority produces the degraded sesquiterpene alcohol geosmin. Two minor groups of bacteria do not produce geosmin, with one of these groups instead producing other sesquiterpene alcohols, whereas members of the remaining group do not produce any detectable terpenoid metabolites. Because bacterial terpene synthases typically show no significant overall sequence similarity to any other known fungal or plant terpene synthases and usually exhibit relatively low levels of mutual sequence similarity with other bacterial synthases, simple correlation of protein sequence data with the structure of the cyclized terpene product has been precluded. We have previously described a powerful search method based on the use of hidden Markov models (HMMs) and protein families database (Pfam) search that has allowed the discovery of monoterpene synthases of bacterial origin. Using an enhanced set of HMM parameters generated using a training set of 140 previously identified bacterial terpene synthase sequences, a Pfam search of 8,759,463 predicted bacterial proteins from public databases and in-house draft genome data has now revealed 262 presumptive terpene synthases. The biochemical function of a considerable number of these presumptive terpene synthase genes could be determined by expression in a specially engineered heterologousStreptomyceshost and spectroscopic identification of the resulting terpene products. In addition to a wide variety of terpenes that had been previously reported from fungal or plant sources, we have isolated and determined the complete structures of 13 previously unidentified cyclic sesquiterpenes and diterpenes.
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Sun, Xiang, You-Sheng Cai, Yujie Yuan, Guangkai Bian, Ziling Ye, Zixin Deng, and Tiangang Liu. "Genome mining in Trichoderma viride J1-030: discovery and identification of novel sesquiterpene synthase and its products." Beilstein Journal of Organic Chemistry 15 (August 28, 2019): 2052–58. http://dx.doi.org/10.3762/bjoc.15.202.
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Sesquiterpene synthases in Trichoderma viride have been seldom studied, despite the efficiency of filamentous fungi for terpenoid production. Using the farnesyl diphosphate-overexpressing Saccharomyces cerevisiae platform to produce diverse terpenoids, we herein identified an unknown sesquiterpene synthase from T. viride by genome mining and determined the structure of its corresponding products. One new 5/6 bicyclic sesquiterpene and its esterified derivative were characterised by GC–MS and 1D and 2D NMR spectroscopy. To the best of our knowledge, this is the first well-identified sesquiterpene synthase from T. viride to date.
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Liang, Dongmei, Weiguo Li, Xiaoguang Yan, Qinggele Caiyin, Guangrong Zhao, and Jianjun Qiao. "Molecular and Functional Evolution of the Spermatophyte Sesquiterpene Synthases." International Journal of Molecular Sciences 22, no. 12 (June 14, 2021): 6348. http://dx.doi.org/10.3390/ijms22126348.
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Sesquiterpenes are important defense and signal molecules for plants to adapt to the environment, cope with stress, and communicate with the outside world, and their evolutionary history is closely related to physiological functions. In this study, the information of plant sesquiterpene synthases (STSs) with identified functions were collected and sorted to form a dataset containing about 500 members. The phylogeny of spermatophyte functional STSs was constructed based on the structural comparative analysis to reveal the sequence–structure–function relationships. We propose the evolutionary history of plant sesquiterpene skeletons, from chain structure to small rings, followed by large rings for the first time and put forward a more detailed function-driven hypothesis. Then, the evolutionary origins and history of spermatophyte STSs are also discussed. In addition, three newly identified STSs CaSTS2, CaSTS3, and CaSTS4 were analyzed in this functional evolutionary system, and their germacrene D products were consistent with the functional prediction. This demonstrates an application of the structure-based phylogeny in predicting STS function. This work will help us to understand evolutionary patterns and dynamics of plant sesquiterpenes and STSs and screen or design STSs with specific product profiles as functional elements for synthetic biology application.
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Manczak, Tom, and Henrik Toft Simonsen. "Insight into Biochemical Characterization of Plant Sesquiterpene Synthases." Analytical Chemistry Insights 11s1 (January 2016): ACI.S40292. http://dx.doi.org/10.4137/aci.s40292.
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A fast and reproducible protocol was established for enzymatic characterization of plant sesquiterpene synthases that can incorporate radioactivity in their products. The method utilizes the 96-well format in conjunction with cluster tubes and enables processing of >200 samples a day. Along with reduced reagent usage, it allows further reduction in the use of radioactive isotopes and flammable organic solvents. The sesquiterpene synthases previously characterized were expressed in yeast, and the plant-derived Thapsia garganica kunzeaol synthase TgTPS2 was tested in this method. KM for TgTPS2 was found to be 0.55 μM; the turnover number, kcat, was found to be 0.29 s−1, kcat for TgTPS2 is in agreement with that of terpene synthases of other plants, and kcat/ KM was found to be 0.53 s−1 μM−1 for TgTPS2. The kinetic parameters were in agreement with previously published data.
Dissertations / Theses on the topic "Sesquiterpene synthases"
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Li, Amang. "Investigations into the function of two plant sesquiterpene synthases : d-cadinene synthase and (e)-beta-farnesene synthase." Thesis, Cardiff University, 2011. http://orca.cf.ac.uk/55131/.
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Terpenoids represent the most structurally and stereochemically diverse family of natural products with more than 55,000 terpenoid structures discovered to date from all life forms. Sesquiterpenes are a class of the terpenoid family, and their formation from farnesyl diphosphate is catalyzed by sesquiterpene synthases. This project focuses on trying to decipher the reaction mechanisms of two sesquiterpene synthases, 6-cadinene synthase from Gossypium arboreum and (2
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Greenhagen, Bryan T. "ORIGINS OF ISOPRENOID DIVERSITY: A STUDY OF STRUCTURE-FUNCTION RELATIONSHIPS IN SESQUITERPENE SYNTHASES." UKnowledge, 2003. http://uknowledge.uky.edu/gradschool_diss/440.
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Plant sesquiterpene synthases catalyze the conversion of the linear substrate farnesyl diphosphate, FPP, into a remarkable array of secondary metabolites. These secondary metabolites in turn mediate a number of important interactions between plants and their environment, such as plant-plant, plant-insect and plant-pathogen interactions. Given the relative biological importance of sesquiterpenes and their use in numerous practical applications, the current thesis was directed towards developing a better understanding of the mechanisms employed by sesquiterpene synthases in the biosynthesis of such a diverse class of compounds. Substrate preference for sesquiterpene synthases initially isolated from Nicotiana tabacum (TEAS), Hyoscyamus muticus (HPS) and Artemisia annuna (ADS) were optimized with regards to a divalent metal ion requirement. Surprisingly, careful titration with manganese stimulated bona fide synthase activity with the native 15-carbon substrate farnesyl diphopshate (FPP) as well as with the 10-carbon substrate geranyl diphosphate (GPP). Reaction product analysis suggested that the GPP could be used to investigate early steps in the catalytic cascade of these enzymes. To investigate how structural features of the sesquiterpene synthases translate into enzymatic traits, a series of substrate and active site residue contacts maps were developed and used in a comparative approach to identify residues that might direct product specificity. The role and contribution of several of these residues to catalysis and product specificity were subsequently tested by the creation of site-directed mutants. One series of mutants was demonstrated to change the reaction product to a novel sesquiterpene, 4-epi-eremophilene, and while another series successfully transmutated TEAS into a HPS-like enzyme. This is the first report of a rational redesign of product specificity for any terpene synthase. The contact map provides a basis for the prediction of specific configurations of amino acids that might be necessary for as yet uncharacterized sesquiterpene synthases from natural sources. This prediction was tested by the subsequent isolation and validation that valencene synthase, a synthase from citrus, did indeed have the amino acid configuration as predicted. Lastly, an in vitro system was developed for analyzing the interaction between sesquiterpene synthases and the corresponding terpene hydroxylase. Development of this in vitro system is presented as a new important tool in further defining those biochemical features giving rise to the biological diversity of sesquiterpenes.
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Couillaud, Julie. "The terpene mini-path : nouvel accès aux terpènes et exploration de l'espace chimique par une cascade enzymatique originale." Electronic Thesis or Diss., Aix-Marseille, 2021. http://www.theses.fr/2021AIXM0188.
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À ce jour, les terpénoïdes constituent la classe de produits naturels la plus abondante et diversifiée avec plus de 80000 composés décrits et dont les propriétés structurales, biologiques (antibiotique, anticancéreux, antipaludique…) et physico-chimiques (arôme, parfum, colorant…) retiennent l’attention de la communauté scientifique. Cependant, leur accès est limité par une faible disponibilité par extraction à partir de sources naturelles ; une synthèse chimique souvent coûteuse et laborieuse; et des voies de biosynthèses longues. En combinant des approches bioinformatiques, statistiques, biochimiques et de biologie moléculaire, nous avons développé la « mini-voie des terpènes », à seulement deux étapes enzymatiques, comme alternative synthétique et biosourçable pour l’accès aux DMAPP et IPP, précurseurs universels des terpènes. Cette nouvelle voie artificielle a permis la synthèse de différents terpénoïdes naturels et également non-naturels tels que des dérivés cyclobutyliques, en l’absence d’ingénierie métabolique et enzymatique. Ainsi, la mini-voie offre un accès facilité à l’ensemble des terpénoïdes et constitue un nouvel outil biosynthétique attractif pour l’exploration de la diversité de l’espace chimique des terpènesTo date, terpenoids form the most abundant and diversified class of natural products with more than 80,000 compounds whose structural, biological (antibiotic, anticancer, antimalarial, etc.) and physicochemical (flavor, fragrance, dye, etc.) properties hold the attention of the scientific community. However, their access is limited because of the low available quantity by extraction from natural sources; an often expensive and laborious chemical synthesis; and long biosynthetic pathways. By combining bioinformatic, statistical, biochemical and molecular biology approaches, we have developed the « Terpene mini-path », with only two enzymatic steps, as a synthetic and potentially bio-sourced alternative to access DMAPP and IPP, universal precursors of terpenes. This new artificial pathway allowed the synthesis of various natural and unnatural terpenoids, such as cyclobutylic derivatives, in the absence of any metabolic and enzymatic engineering. The mini-path provides thus an easy access to all terpenoids and represents an attractive new biosynthetic tool to explore the diversity of the terpene chemical space
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Adams, Racheal. "Cloning and characterisation of (#EPSILON#) β farnesene synthase genes." Thesis, University of Nottingham, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.289464.
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Köllner, Tobias G. "Molekulare und genetische Aspekte der Biosynthese von komplexen Sesquiterpengemischen in Mais." kostenfrei, 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972066292.
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Al-Lami, Naeemah. "Synthesis of nitrogen-containing bicyclic sesquiterpenes as potential transition state inhibitors of aristolochene synthase." Thesis, Cardiff University, 2013. http://orca.cf.ac.uk/53674/.
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Aristolochene synthase from Penicillium roqueforti(PR-AS) is sesquiterpene synthase that catalyses the Mg2+-dependent conversion of farnesyl diphosphate FDP to (+)-aristolochene. Through the use of site directed mutagenesis, fluorinated FDPs and an aza-analogue of the eudesmane cation, the reaction was previously shown to involve germacrene A and eudesmane cation as intermediates. The subsequent series of rearrangements that transform the eudesmane cation to (+)-aristolochene have not been investigated previously. To probe the carbocationic nature of these 1,2-hydride and methyl shifts, new aza-analogues were designed to mimic the geometric and electrostatic properties of postulated carbocation intermediates in the catalytic mechanism of PR-AS. Here is described the synthesis of both enantiomers of 10-aza-eremophilane in enantiomerically pure from the common precursor (4S)-limonene oxide and their analysis as inhibitors of PR-AS. The synthesis of (7R,4S,5S)-10-aza-eremophilane cation was accomplished in 8 steps, starting from a known keto ester that in turn was obtained by degradation of (-)-limonene oxide. An identical synthetic protocol was repeated from (4R)-limonene oxide to give the enantiomer of 10-aza-eremophilane cation. Inhibition studies with compound (7R,4S,5S)-10-aza-eremophilane indicated that this ammonium salt acted as a moderate competitive inhibitor of PR-AS (Ki = 38 μM), and showed that eremophilane cation is likely a true intermediate on the pathway from FDP to aristolochene during PR-AS catalysis. The inhibition potency of 10-aza-eremophilane was increased by the addition of diphosphate PPi (Ki = 2.9 μM). This synergetic kinetic effect suggests that the possible involvement of PPi as a stabilizing anion for the eremophilane carbocation in PR-AS biosynthesis. Inhibition studies of the enantiomer of (7R,4S,5S)-10-aza-eremophilane cation, (7S,4R,5R)-10-aza-eremophilane cation, which has incorrect stereocenteres, with PR-AS indicated that this ammonium salt was a poor inhibitor of PR-AS (Ki = 1.03 mM). The data obtained for this compound highlight the chiral environment of the active site of PR-AS, and more importantly supports the postulate that terpene synthases form a product-like contour at their active site that steers the carbocationic cascade catalyzed by PR-AS toward the production of a single enantiomer. iv In the second part of the present work, progress was made towards the stereoselective synthesis of 5-aza-eudesmane cation. This teriary amine is a structural mimic of the 5-eudesmane carbocation, another putative intermediate in the reaction cascade catalysed by PR-AS. However, this tertiary amine was not obtained with desired stereochemistry, nevertheless, two diastereoisomers of the desired compound were obtained.
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Andersson, Marie. "Elucidation of the product synthesis of the sesquiterpene synthase Cop6 isolated from Coprinus cinereus." Thesis, Linköpings universitet, Institutionen för fysik, kemi och biologi, 2009. http://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-17252.
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Mushrooms are believed to have a great potential for production of bioactive metabolites e. g. terpenes, a group of interesting compounds with diverse chemical properties such as antitumour and antibacterial activity. Cop6 is a terpene cyclase isolated from the mushroom Coprinus cinereus that catalyzes the cyclization of farnesyl diphosphate (FPP) to mainly α-cuprenene. In this study gas chromatography combined with mass spectroscopy (GC-MS) is used to analyze the product profile of Cop6 mutants created by PCR based site directed mutagenesis. The goal is to produce trichodiene, the parent hydrocarbon in the biosynthesis of trichothecene antibiotics and mycotoxins. Valine instead of tyrosine in amino acid position 195 resulted in cyclisation of (E)-β-Farnesene and (3Z,6E)-α-Farnesene besides the products of the wild type enzyme. Another mutant with aspartic acid instead of asparagine in position 224 resulted in the synthesis of β-Bisabolene except for α-cuprenene and methionine in position 74 instead of isoleucine killed the activity of the cyclase. Furthermore, an attempt to saturation of position 98 was made, resulting in four mutants. Two of them essentially killed the activity of the cyclase whereas two had minor effect of the product profile compared to the wild type.
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Huh, Jung-Hyun. "Biochemical, Molecular and Functional Analysis of Volatile Terpene Formation in Arabidopsis Roots." Diss., Virginia Tech, 2011. http://hdl.handle.net/10919/77151.
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Plants produce secondary (or specialized) metabolites to respond to a variety of environmental changes and threats. Especially, volatile compounds released by plants facilitate short and long distance interaction with both beneficial and harmful organisms. Comparatively little is known about the organization and role of specialized metabolism in root tissues. In this study, we have investigated the root-specific formation and function of volatile terpenes in the model plant Arabidopsis.
As one objective, we have characterized the two root-specific terpene synthases, TPS22 and TPS25. Both enzymes catalyze the formation of several volatile sesquiterpenes with (E)-β-farnesene as the major product. TPS22 and TPS25 are expressed in the root in distinct different cell type-specific patterns and both genes are induced by jasmonic acid. Unexpectedly, both TPS proteins are localized to mitochondria, demonstrating a subcellular localization of terpene specialized metabolism in compartments other than the cytosol and plastids. (E)-β-Farnesene is produced at low concentrations suggesting posttranslational modifications of the TPS proteins and/or limited substrate availability in mitochondria. We hypothesize that the mitochondrial localization of TPS22 and TPS25 reflects evolutionary plasticity in subcellular compartmentation of TPS proteins with emerging or declining activity. Since (E)-β-farnesene inhibits Arabidopsis root growth in vitro, mitochondrial targeting of both proteins may fine tune (E)-β-farnesene concentrations to prevent possible autotoxic or inhibitory effects of this terpene in vivo.
We further investigated the role of volatile terpenes in Arabidopsis roots in interaction with the soil-borne oomycete, Pythium irregulare. Infection of roots with P. irregulare causes emission of the C11-homoterpene (or better called C4-norterpene) 4,8-dimethylnona-1,3,7-triene (DMNT), which is a common volatile induced by biotic stress in aerial parts of plants but was not previously known to be produced in plant roots. We demonstrate that DMNT is synthesized by a novel, root-specific pathway via oxidative degradation of the C30-triterpene, arabidiol. DMNT exhibits inhibitory effects on P. irregulare mycelium growth and oospore germination in vitro. Moreover, arabidiol and DMNT biosynthetic mutants were found to be more susceptible to P. irregulare infection and showed higher rates of Pythium colonization in comparison to wild type plants. Together, our studies demonstrate differences and plasticity in the metabolic organization and function of terpenes in roots in comparison to aboveground plant tissues.Ph. D.
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Singh, S. "Structural studies on sesquisabinene synthase 1: enzyme involved in terpene biosynthesis pathway." Thesis(Ph.D.), 2021. http://dspace.ncl.res.in:8080/xmlui/handle/20.500.12252/5995.
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Hsieh, Hui-Ling, and 謝慧玲. "Cloning and Expression of a Sesquiterpene Synthase Gene from Taiwania cryptomerioides Hayata." Thesis, 2010. http://ndltd.ncl.edu.tw/handle/82143189020621256157.
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碩士國立臺灣大學
森林環境暨資源學研究所
98
Taiwania (Taiwania cryptomerioides Hayata) is a native conifer species of Taiwan. Many studies have demonstrated the bioactivities of secondary metabolites extracted from Taiwania in recent years. To regulate the biosynthsis of metabolites in Taiwania, it should be illustrate the synthesis based on the molecular level. In this study, we focus on sesquiterpene synthase of Taiwania. First, a pair of degenerated primers was designed for reverse transcription-polymerase chain reaction (RT-PCR) using total RNA extracted from leaves of mature tree. A DNA fragment with the conserved region of the terpene synthases (TPSs) was obtained. After 5’ and 3’ Rapid Amplification of cDNA Ends (RACE), the full-length cDNA was obtained, and it contains an open reading frame of 1791 bp with a predicated molecular mass of 70.2 kDa. The gene was highly expressed in young leaves, female flowers and cones. The expression in leave was enhanced after the treatment of soaking in 100 μM salicylic acid (SA). To identify the function of the obtained TPS, the recombinant protein from Escherichia coli was incubated with farnesyl diphosphate (FPP). After GC/MS analysis and retention time as well as mass spectrum matching with authentic standards revealed that the major product of TPS was sesquiterpene α-Gurjunene. The gene was named as Tc-Gur. To investigate the synthesis of this TPS in plant system, α-Gurjunene is also synthesized in transgenic Arabidopsis. But another sesquiterpene, α-Muurolene, is synthesized in transgenic hairy root of Taiwania.
Books on the topic "Sesquiterpene synthases"
1
Crock, John Edward. Five sesquiterpene synthases. 1998.
Find full textBook chapters on the topic "Sesquiterpene synthases"
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Garrett, Steven R., Richard J. Morris, and Paul E. O'Maille. "Steady-State Kinetic Characterization of Sesquiterpene Synthases by Gas Chromatography–Mass Spectroscopy." In Natural Product Biosynthesis by Microorganisms and Plants, Part A, 3–19. Elsevier, 2012. http://dx.doi.org/10.1016/b978-0-12-394290-6.00001-x.
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Huynh, Florence, David J. Miller, and Rudolf K. Allemann. "Sesquiterpene Synthase-Catalyzed Conversion of a Farnesyl Diphosphate Analogue to a Nonnatural Terpenoid Ether." In Methods in Enzymology, 83–95. Elsevier, 2018. http://dx.doi.org/10.1016/bs.mie.2018.05.004.
Full textConference papers on the topic "Sesquiterpene synthases"
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Omar, Aimi Farehah, and Ismanizan Ismail. "Isolation of Persicaria minor sesquiterpene synthase promoter and its deletions for transgenic Arabidopsis thaliana." In THE 2016 UKM FST POSTGRADUATE COLLOQUIUM: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2016 Postgraduate Colloquium. Author(s), 2016. http://dx.doi.org/10.1063/1.4966730.
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