Relevant bibliographies by topics / Methylerythritol phosphate pathway (MEP pathway)

Academic literature on the topic 'Methylerythritol phosphate pathway (MEP pathway)'

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Published: 31 August 2024

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Journal articles on the topic "Methylerythritol phosphate pathway (MEP pathway)"

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Banerjee, A., and T. D. Sharkey. "Methylerythritol 4-phosphate (MEP) pathway metabolic regulation." Nat. Prod. Rep. 31, no. 8 (2014): 1043–55. http://dx.doi.org/10.1039/c3np70124g.

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The methylerythritol 4-phosphate pathway provides precursors for isoprenoids in bacteria, some eukaryotic parasites, and chloroplasts of plants. Metabolic regulatory mechanisms control flux through the pathway and the concentration of a central intermediate, methylerythritol cyclodiphosphate.
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Testa, Charles A., and L. Jeffrey Johnson. "A Whole-Cell Phenotypic Screening Platform for Identifying Methylerythritol Phosphate Pathway-Selective Inhibitors as Novel Antibacterial Agents." Antimicrobial Agents and Chemotherapy 56, no. 9 (July 9, 2012): 4906–13. http://dx.doi.org/10.1128/aac.00987-12.

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ABSTRACTIsoprenoid biosynthesis is essential for survival of all living organisms. More than 50,000 unique isoprenoids occur naturally, with each constructed from two simple five-carbon precursors: isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Two pathways for the biosynthesis of IPP and DMAPP are found in nature. Humans exclusively use the mevalonate (MVA) pathway, while most bacteria, including all Gram-negative and many Gram-positive species, use the unrelated methylerythritol phosphate (MEP) pathway. Here we report the development of a novel, whole-cell phenotypic screening platform to identify compounds that selectively inhibit the MEP pathway. Strains ofSalmonella entericaserovar Typhimurium were engineered to have separately inducible MEP (native) and MVA (nonnative) pathways. These strains, RMC26 and CT31-7d, were then used to differentiate MVA pathway- and MEP pathway-specific perturbation. Compounds that inhibit MEP pathway-dependent bacterial growth but leave MVA-dependent growth unaffected represent MEP pathway-selective antibacterials. This screening platform offers three significant results. First, the compound is antibacterial and is therefore cell permeant, enabling access to the intracellular target. Second, the compound inhibits one or more MEP pathway enzymes. Third, the MVA pathway is unaffected, suggesting selectivity for targeting the bacterial versus host pathway. The cell lines also display increased sensitivity to two reported MEP pathway-specific inhibitors, further biasing the platform toward inhibitors selective for the MEP pathway. We demonstrate development of a robust, high-throughput screening platform that combines phenotypic and target-based screening that can identify MEP pathway-selective antibacterials simply by monitoring optical density as the readout for cell growth/inhibition.
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Cassera, María B., Fabio C. Gozzo, Fabio L. D'Alexandri, Emilio F. Merino, Hernando A. del Portillo, Valnice J. Peres, Igor C. Almeida, et al. "The Methylerythritol Phosphate Pathway Is Functionally Active in All Intraerythrocytic Stages ofPlasmodium falciparum." Journal of Biological Chemistry 279, no. 50 (September 27, 2004): 51749–59. http://dx.doi.org/10.1074/jbc.m408360200.

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Two genes encoding the enzymes 1-deoxy-d-xylulose-5-phosphate synthase and 1-deoxy-d-xylulose-5-phosphate reductoisomerase have been recently identified, suggesting that isoprenoid biosynthesis inPlasmodium falciparumdepends on the methylerythritol phosphate (MEP) pathway, and that fosmidomycin could inhibit the activity of 1-deoxy-d-xylulose-5-phosphate reductoisomerase. The metabolite 1-deoxy-d-xylulose-5-phosphate is not only an intermediate of the MEP pathway for the biosynthesis of isopentenyl diphosphate but is also involved in the biosynthesis of thiamin (vitamin B1) and pyridoxal (vitamin B6) in plants and many microorganisms. Herein we report the first isolation and characterization of most downstream intermediates of the MEP pathway in the three intraerythrocytic stages ofP. falciparum. These include, 1-deoxy-d-xylulose-5-phosphate, 2-C-methyl-d-erythritol-4-phosphate, 4-(cytidine-5-diphospho)-2-C-methyl-d-erythritol, 4-(cytidine-5-diphospho)-2-C-methyl-d-erythritol-2-phosphate, and 2-C-methyl-d-erythritol-2,4-cyclodiphosphate. These intermediates were purified by HPLC and structurally characterized via biochemical and electrospray mass spectrometric analyses. We have also investigated the effect of fosmidomycin on the biosynthesis of each intermediate of this pathway and isoprenoid biosynthesis (dolichols and ubiquinones). For the first time, therefore, it is demonstrated that the MEP pathway is functionally active in all intraerythrocytic forms ofP. falciparum, andde novobiosynthesis of pyridoxal in a protozoan is reported. Its absence in the human host makes both pathways very attractive as potential new targets for antimalarial drug development.
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Chen, Lijia, Hui Tong, Mingxuan Wang, Jianhua Zhu, Jiachen Zi, Liyan Song, and Rongmin Yu. "Effect of Enzyme Inhibitors on Terpene Trilactones Biosynthesis and Gene Expression Profiling in Ginkgo biloba Cultured Cells." Natural Product Communications 10, no. 12 (December 2015): 1934578X1501001. http://dx.doi.org/10.1177/1934578x1501001205.

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The biosynthetic pathway of terpene trilactones of Ginkgo biloba is unclear. In this present study, suspension cultured cells of G. biloba were used to explore the regulation of the mevalonic acid (MVA) and methylerythritol 4-phosphate (MEP) pathways in response to specific enzyme inhibitors (lovastatin and clomazone). The results showed that the biosynthesis of bilobalide was more highly correlated with the MVA pathway, and the biosynthesis of ginkgolides was more highly correlated with the MEP pathway. Meanwhile, according to the results, it could be speculated that bilobalide might be a product of ginkgolide metabolism.
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Zeidler, J., J. Schwender, C. Mueller, and H. K. Lichtenthaler. "The non-mevalonate isoprenoid biosynthesis of plants as a test system for drugs against malaria and pathogenic bacteria." Biochemical Society Transactions 28, no. 6 (December 1, 2000): 796–98. http://dx.doi.org/10.1042/bst0280796.

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Two plant test systems are presented in the search for new inhibitors of the non-mevalonate isoprenoid pathway. A derivative of clomazone appears to be an inhibitor of the deoxyxylulose 5-phosphate/methylerythritol 4-phosphate (DOXP/MEP) pathway of isoprenoid formation.
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Kadian, Kavita, Yash Gupta, Harsh Vardhan Singh, Prakasha Kempaiah, and Manmeet Rawat. "Apicoplast Metabolism: Parasite’s Achilles’ Heel." Current Topics in Medicinal Chemistry 18, no. 22 (January 10, 2019): 1987–97. http://dx.doi.org/10.2174/1568026619666181130134742.

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Malaria continues to impinge heavily on mankind, with five continents still under its clasp. Widespread and rapid emergence of drug resistance in the Plasmodium parasite to current therapies accentuate the quest for novel drug targets and antimalarial compounds. Plasmodium parasites, maintain a non-photosynthetic relict organelle known as Apicoplast. Among the four major pathways of Apicoplast, biosynthesis of isoprenoids via Methylerythritol phosphate (MEP) pathway is the only indispensable function of Apicoplast that occurs during different stages of the malaria parasite. Moreover, the human host lacks MEP pathway. MEP pathway is a validated repertoire of novel antimalarial and antibacterial drug targets. Fosmidomycin, an efficacious antimalarial compound against IspC enzyme of MEP pathway is already in clinical trials as a combination drugs. Exploitation of other enzymes of MEP pathway would provide a much-needed impetus to the antimalarial drug discovery programs for the elimination of malaria. We outline the cardinal features of the MEP pathway enzymes and progress made towards the characterization of new inhibitors.
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Cornish, Rita M., John R. Roth, and C. Dale Poulter. "Lethal Mutations in the Isoprenoid Pathway of Salmonella enterica." Journal of Bacteriology 188, no. 4 (February 15, 2006): 1444–50. http://dx.doi.org/10.1128/jb.188.4.1444-1450.2006.

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ABSTRACT Essential isoprenoid compounds are synthesized using the 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway in many gram-negative bacteria, some gram-positive bacteria, some apicomplexan parasites, and plant chloroplasts. The alternative mevalonate pathway is found in archaea and eukaryotes, including cytosolic biosynthesis in plants. The existence of orthogonal essential pathways in eukaryotes and bacteria makes the MEP pathway an attractive target for the development of antimicrobial agents. A system is described for identifying mutations in the MEP pathway of Salmonella enterica serovar Typhimurium. Using this system, point mutations induced by diethyl sulfate were found in the all genes of the essential MEP pathway and also in genes involved in uptake of methylerythritol. Curiously, none of the MEP pathway genes could be identified in the same parent strain by transposon mutagenesis, despite extensive searches. The results complement the biochemical and bioinformatic approaches to the elucidation of the genes involved in the MEP pathway and also identify key residues for activity in the enzymes of the pathway.
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Pérez-Gil, Jordi, and Manuel Rodríguez-Concepción. "Metabolic plasticity for isoprenoid biosynthesis in bacteria." Biochemical Journal 452, no. 1 (April 25, 2013): 19–25. http://dx.doi.org/10.1042/bj20121899.

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Isoprenoids are a large family of compounds synthesized by all free-living organisms. In most bacteria, the common precursors of all isoprenoids are produced by the MEP (methylerythritol 4-phosphate) pathway. The MEP pathway is absent from archaea, fungi and animals (including humans), which synthesize their isoprenoid precursors using the completely unrelated MVA (mevalonate) pathway. Because the MEP pathway is essential in most bacterial pathogens (as well as in the malaria parasites), it has been proposed as a promising new target for the development of novel anti-infective agents. However, bacteria show a remarkable plasticity for isoprenoid biosynthesis that should be taken into account when targeting this metabolic pathway for the development of new antibiotics. For example, a few bacteria use the MVA pathway instead of the MEP pathway, whereas others possess the two full pathways, and some parasitic strains lack both the MVA and the MEP pathways (probably because they obtain their isoprenoids from host cells). Moreover, alternative enzymes and metabolic intermediates to those of the canonical MVA or MEP pathways exist in some organisms. Recent work has also shown that resistance to a block of the first steps of the MEP pathway can easily be developed because several enzymes unrelated to isoprenoid biosynthesis can produce pathway intermediates upon spontaneous mutations. In the present review, we discuss the major advances in our knowledge of the biochemical toolbox exploited by bacteria to synthesize the universal precursors for their essential isoprenoids.
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Banerjee, Aparajita, Yan Wu, Rahul Banerjee, Yue Li, Honggao Yan, and Thomas D. Sharkey. "Feedback Inhibition of Deoxy-d-xylulose-5-phosphate Synthase Regulates the Methylerythritol 4-Phosphate Pathway." Journal of Biological Chemistry 288, no. 23 (April 23, 2013): 16926–36. http://dx.doi.org/10.1074/jbc.m113.464636.

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The 2-C-methyl-d-erythritol 4-phosphate (MEP) pathway leads to the biosynthesis of isopentenyl diphosphate (IDP) and dimethylallyl diphosphate (DMADP), the precursors for isoprene and higher isoprenoids. Isoprene has significant effects on atmospheric chemistry, whereas other isoprenoids have diverse roles ranging from various biological processes to applications in commercial uses. Understanding the metabolic regulation of the MEP pathway is important considering the numerous applications of this pathway. The 1-deoxy-d-xylulose-5-phosphate synthase (DXS) enzyme was cloned from Populus trichocarpa, and the recombinant protein (PtDXS) was purified from Escherichia coli. The steady-state kinetic parameters were measured by a coupled enzyme assay. An LC-MS/MS-based assay involving the direct quantification of the end product of the enzymatic reaction, 1-deoxy-d-xylulose 5-phosphate (DXP), was developed. The effect of different metabolites of the MEP pathway on PtDXS activity was tested. PtDXS was inhibited by IDP and DMADP. Both of these metabolites compete with thiamine pyrophosphate for binding with the enzyme. An atomic structural model of PtDXS in complex with thiamine pyrophosphate and Mg2+ was built by homology modeling and refined by molecular dynamics simulations. The refined structure was used to model the binding of IDP and DMADP and indicated that IDP and DMADP might bind with the enzyme in a manner very similar to the binding of thiamine pyrophosphate. The feedback inhibition of PtDXS by IDP and DMADP constitutes an important mechanism of metabolic regulation of the MEP pathway and indicates that thiamine pyrophosphate-dependent enzymes may often be affected by IDP and DMADP.
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Killiny, Nabil. "Silencing Phytoene Desaturase Causes Alteration in Monoterpene Volatiles Belonging to the Methylerythritol Phosphate Pathway." Plants 11, no. 3 (January 20, 2022): 276. http://dx.doi.org/10.3390/plants11030276.

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Volatile organic compounds (VOCs) are a large group of lipophilic hydrocarbon compounds derived from different biosynthetic pathways in plants. VOCs are produced and released from plants as a defense mechanism against biotic and abiotic stresses. They are involved in communication with the surrounding environment including plant-to-plant interactions and attracting or repelling insects. In citrus, phytoene desaturase (PDS), a precursor of the carotenoid biosynthetic pathway has been silenced using the Citrus tristeza virus-induced gene silencing technique. Silencing PDS resulted in a reduction of carotenoid contents and in the photobleaching phenotype in leaves. Interestingly, the strength of the phenotype was varied within the plants due to the unequal distribution of virus particles. Using solid-phase microextraction (SPME), fibers released VOCs from leaves with gradient degrees of the photobleaching phenotype were collected and analyzed in gas chromatography-mass spectrophotometry (GC-MS). Overall, 47 VOCs belonging to 12 chemically distinguished groups were detected and identified using authentic standards. Simple linear regression showed that monoterpenes belonging to methylerythritol phosphate (MEP) were significantly corrected with the degrees of photobleaching (carotenoid content). Both carotenoids and MEP biosynthetic pathways occurred in the plastid. Thus, we provide preliminary evidence for a potential role of carotenoids in supporting the MEP pathway and/or the production of monoterpenes.
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Dissertations / Theses on the topic "Methylerythritol phosphate pathway (MEP pathway)"

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Bianchino, Gabriella ines. "La métalloenzyme IspH, une source pour la découverte de nouveaux agents antimicrobiens." Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAF016.

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L'un des moyens de lutter contre la résistance aux antimicrobiens est de se concentrer sur des séries d'enzymes cibles sous-exploitées. Dans la plupart des bactéries et certains parasites, les précurseurs isoprénoïdes sont synthétisés par la voie du 2C-méthyl-d-érythritol 4-phosphate (MEP), absente chez l'homme, et qui représente donc une cible intéressante pour le développement de nouveaux anti-infectieux. IspH est une oxydoréductase contenant un cluster [4Fe-4S]2+ sensible à l'oxygène qui catalyse la dernière étape de la voie du MEP en convertissant l’HMBPP en IPP et DMAPP. Une stratégie pluridisciplinaire a été appliquée pour découvrir de nouvelles classes d'inhibiteurs contre l'IspH de Pseudomonas aeruginosa, Mycobacterium tuberculosis et Plasmodium falciparum. Une méthode a été mise au point pour produire les différents orthologues de l'IspH sous forme d'holoenzymes, suivie par le développement d'un test enzymatique qui a été utilisé pour un criblage in vitro de différentes chimiothèques. Cette dernière a conduit à la découverte d'un puissant nouvel inhibiteur ciblant les trois orthologues. En outre, une approche de prodrogue a été exploitée pour un inhibiteur d'IspH d'E. coli déjà connu ((E)-4-amino-3-méthylbut-2-en-1-yl diphosphate) dans le but d'obtenir une activité antibactérienne, antituberculeuse et antipaludéenne
One way to tackle the arising antimicrobial resistance is to focus on underexploited series of target enzymes. In most bacteria and some parasites, the isoprenoid precursors are synthesized via the 2C-methyl-d-erythritol 4-phosphate (MEP) pathway, which is absent in humans, and it thus represents an interesting target for the development of novel anti-infectives. IspH is an oxidoreductase containing an oxygen-sensitive [4Fe-4S]2+ cluster that catalyzes the last step of the MEP pathway converting HMBPP into IPP and DMAPP. A multidisciplinary strategy has been applied for the discovery of new classes of inhibitors against IspH from Pseudomonas aeruginosa, Mycobacterium tuberculosis and Plasmodium falciparum. A method was developed to produce the IspH orthologs as holoenzymes, followed by the development of the enzymatic assay which was used for an in vitro screening campaign of different chemical libraries. The latter led to the discovery of a novel potent inhibitor targeting the three orthologs object of this study. Moreover, a prodrug approach has been exploited for an already known E. coli IspH inhibitor ((E)-4-amino-3-methylbut-2-en-1-yl diphosphate) with the goal of reaching antibacterial, antitubercular, and antimalarial activity
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Baatarkhuu, Zoljargal. "Metabolic labelling of bacterial isoprenoids produced by the methylerythritol phosphate pathway : a starting point towards a new inhibitor." Thesis, Strasbourg, 2017. http://www.theses.fr/2017STRAF029/document.

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Les isoprénoïdes, présents dans tous les organismes vivants, sont synthétisés selon deux processus: la voie du Mevalonate et la voie Méthylérythritol phosphate (MEP). Cette dernière, absente chez l’humain, est très étudiée car elle représente une cible pour le développement de nouveaux antimicrobiens. Le ME-N3, un analogue du méthylérythritol portant un azoture, a été synthétisé et exploité dans des expériences de marquage métabolique de la voie MEP en utilisant un couplage bioorthogonale suivi d’une analyse par LC/MS. De façon intéressante, nous avons découvert que le MEP-N3, un analogue du MEP, inhibe l'enzyme IspD d’ E. coli (3ème enzyme de la voie MEP). Les études cinétiques ont révélé que le MEP-N3 possède la meilleure activité inhibitrice sur IspD d’ E.coli en comparaison avec les inhibiteurs connus, et que le mécanisme d'inhibition est de type mixte. Une étude détaillée du mécanisme de la réaction catalysée par IspD a été réalisée pour la première fois, en utilisant une analyse cinétique à deux substrats
Isoprenoids, present in all living organisms, are synthesised according to two routes: the Mevalonate and the Methylerythritol phosphate (MEP) pathways. The MEP pathway, absent in humans, is extensively investigated as it is a target for the development of new antimicrobials. ME-N3 an azide tagged analogue of methylerythritol was synthesised and utilised for metabolic labelling studies of the MEP pathway using bioorthogonal ligation followed by LC-MS analysis. Interestingly, we found that MEP-N3, an analogue of MEP, inhibits E.coli IspD (3rd enzyme of the MEP pathway). Further inhibition kinetic studies revealed that MEP-N3 possesses the highest inhibitory activity on E.coli ispD when compared to known inhibitors. In addition, the mechanism of inhibition of E.coli ispD by MEP-N3 was found to be best described using a mixed type model. Moreover, determination of the IspD reaction mechanism has been carried out for the first time, by virtue of a bisubstrate steady state kinetic analysis
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Henriksson, Lena M. "Structural and Functional Studies of Peptidyl-prolyl cis-trans isomerase A and 1-deoxy-D-xylulose- 5-phosphate reductoisomerase from Mycobacterium tuberculosis." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis Acta Universitatis Upsaliensis, 2007. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-8253.

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Giménez, Oya Víctor. "Molecular studies of two methylerythritol 4-phosphate pathway enzymes of isoprenoid biosynthesis : the 4-diphosphocytidyl-2C-methyl-D-erythritol kinase and the 1-deoxy-D-xylulose 5-phosphate synthase = Estudios moleculares de dos enzimas de la ruta del metileritritol 4-fosfato de biosíntesis de isoprenoides : la 4-difosfocitidil-2C-metil-D-eritritol quinasa y la 1-dexosi-D-xilulosa 5-fosfato sintasa." Doctoral thesis, Universitat de Barcelona, 2009. http://hdl.handle.net/10803/665005.

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Los isoprenoides son una de las mayores familias de compuestos descritos en la naturaleza. Estos compuestos están presentes en todos los organismos vivos y se sintetizan a partir de dos moléculas de 5 átomos de carbono: el isopentenil difosfato (IPP) y el dimetilalil difosfato (DMAPP). Actualmente se conoce que arqueobacterias, hongos y animales presentan la ruta del mevalonato de síntesis de estos precursores, mientras que eubacterias, algún protozoo (como el causante de la malaria) y protistas presentan la ruta del metileritritol 4-fosfato (MEP) de síntesis de IPP y DMAPP. Estas rutas coexisten separadas espacialmente en plantas, helechos y algunas algas. La ruta del MEP de biosíntesis de los precursores de isoprenoides se muestra como una atractiva diana para la búsqueda de nuevos compuestos antimaláricos, antibióticos y herbicidas debido a su presencia en los principales agentes patogénicos y su ausencia en animales, además del carácter esencial de los isoprenoides para la vida. En esta tesis se ha realizado la búsqueda asistida por ordenador de compuestos que puedan interferir en la formación del complejo homodimérico del cuarto paso enzimático de la ruta del MEP. La metodología utilizada es muy útil en la búsqueda de inhibidores específicos. Se han caracterizado la unión de diferentes compuestos obtenidos con la enzima. Además se ha caracterizado el estado de oligomerización de la enzima. Paralelamente también se ha caracterizado un homólogo del primer paso enzimático de la ruta del MEP de un organismo termofílico caracterizando sus principales parámetros cinéticos y residuos importantes para la actividad enzimática mediante mutagénesis dirigida. Como último punto, se ha caracterizado el proceso de proteólisis de diferentes homólogos de este primer paso enzimático de la ruta del MEP asociándolo a modificaciones postraduccionales intramoleculares de las mismas proteínas, abriendo la posibilidad de un proceso de regulación posttraduccional de la actividad enzimática en este tipo de enzimas.
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Jansson, Anna M. "Targeting Infectious Disease : Structural and functional studies of proteins from two RNA viruses and Mycobacterium tuberculosis." Doctoral thesis, Uppsala universitet, Struktur- och molekylärbiologi, 2013. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-196623.

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The recent emergence of a number of new viral diseases as well as the re-emergence of tuberculosis (TB), indicate an urgent need for new drugs against viral and bacterial infections. Coronavirus nsp1 has been shown to induce suppression of host gene expression and interfere with host immune response. However, the mechanism behind this is currently unknown. Here we present the first nsp1 structure from an alphacoronavirus, Transmissible gastroenteritis virus (TGEV) nsp1. Contrary to previous speculation, the TGEV nsp1 structure clearly shows that alpha- and betacoronavirus nsp1s have a common evolutionary origin. However, differences in conservation, shape and surface electrostatics indicate that the mechanism for nsp1-induced suppression of host mRNA translation is likely to be different in the alpha- and betacoronavirus genera. The Modoc virus is a neuroinvasive rodent virus with similar pathology as flavivirus encephalitis in humans. The flaviviral methyltransferase catalyses the two methylations required to complete 5´ mRNA capping, essential for mRNA stability and translation. The structure of the Modoc NS5 methyltransferase domain was determined in complex with its cofactor S-adenosyl-L-methionine. The observed methyltransferase conservation between Modoc and other flaviviral branches, indicates that it may be possible to identify drugs that target a range of flaviviruses and supports the use of Modoc virus as a model for general flaviviral studies. 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR) is part of the methylerythritol phosphate (MEP) pathway that produces essential precursors for isoprenoid biosynthesis. This pathway is used by a number of pathogens, including Mycobacterium tuberculosis and Plasmodium falciparum, but it is not present in humans. Using a structure-based approach, we designed a number of MtDXR inhibitors, including a novel fosmidomycin-analogue that exhibited improved activity against P.falciparum in an in vitro blood cell growth assay. The approach also allowed the first design of an inhibitor that bridge both DXR substrate and co-factor binding sites, providing a stepping-stone for further optimization.
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Book chapters on the topic "Methylerythritol phosphate pathway (MEP pathway)"

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Lichtenthaler, Hartmut K. "Chapter 7 The Non-mevalonate DOXP/MEP (Deoxyxylulose 5-Phosphate/Methylerythritol 4-Phosphate) Pathway of Chloroplast Isoprenoid and Pigment Biosynthesis." In The Chloroplast, 95–118. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-8531-3_7.

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Boronat, Albert. "Chapter 8 The Methylerythritol 4-Phosphate Pathway: Regulatory Role in Plastid Isoprenoid Biosynthesis." In The Chloroplast, 119–26. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-8531-3_8.

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Sathee, Lekshmy, M. K. Malini, Pramod Kumar, and Sudhir Kumar. "Terpenoid Production Through Mevalonate and Methylerythritol Phosphate Pathway and Regulation of Environmental Stress Tolerance." In Biology and Biotechnology of Environmental Stress Tolerance in Plants, 67–100. New York: Apple Academic Press, 2023. http://dx.doi.org/10.1201/9781003346173-4.

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Nagegowda, Dinesh A., David Rhodes, and Natalia Dudareva. "Chapter 10 The Role of the Methyl-Erythritol-Phosphate (MEP)Pathway in Rhythmic Emission of Volatiles." In The Chloroplast, 139–54. Dordrecht: Springer Netherlands, 2010. http://dx.doi.org/10.1007/978-90-481-8531-3_10.

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Wright, Louwrance P., and Michael A. Phillips. "Measuring the Activity of 1-Deoxy-D-Xylulose 5-Phosphate Synthase, the First Enzyme in the MEP Pathway, in Plant Extracts." In Methods in Molecular Biology, 9–20. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0606-2_2.

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O. Bruce, Stella, and Felix A. Onyegbule. "Biosynthesis of Natural Products." In Biosynthesis [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97660.

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Natural products are in the form of primary and secondary metabolites and are isolated chemical compounds or substances from living organisms. Terpenes, Phenolic compounds, and Nitrogen-containing compounds are secondary metabolites. The biosyntheses of secondary metabolites are derived from primary metabolism pathways, which consist of a tricarboxylic acid cycle (TCA), methylerythritol phosphate pathway (MEP), mevalonic and shikimic acid pathway. This chapter provides an overview of the diversity of secondary metabolites in plants, their multiple biological functions, and multi-faceted cultural history.
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"Mevalonate and Methylerythritol Phosphate Pathways: Terpenoids and Steroids." In Chemical Diversity of Plant Specialized Metabolites, 77–162. Royal Society of Chemistry, 2023. http://dx.doi.org/10.1039/9781837671472-00077.

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Terpenes are naturally occurring metabolites with structural diversity based on the number of isoprene units (C5H8). They are biosynthesized following mevalonate (MVA) or methylerythritol phosphate (MEP) pathways. The MVA pathway occurs in the cytosol in plants to form sesquiterpenes (C15) and triterpenes (C30). The MEP pathway occurs in the plastids in plants to form monoterpenes (C10), diterpenes (C20) and tetraterpenes (C40). Depending on the structure, metabolites belonging to this group are essential for plants to interact with the environment for example, protecting plants against herbivores and pathogens and attracting pollinators. Some metabolites are involved in respiration (ubiquinone) and photosynthesis (chlorophylls, carotenoids, phylloquinones, and plastoquinone). Some of the metabolites are growth regulators (brassinosteroids, gibberellins, and strigolactones), and present as part of the membrane structure (sterols). They are also sources of flavours and fragrances (monoterpenes and sesquiterpenes), medicine (taxol for cancer, artemisinin for malaria), and commercial materials (rubber and gutta-percha).
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8

Bittencourt Fagundes, Mariane, and Roger Wagner. "Sterols Biosynthesis in Algae." In Biosynthesis [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96719.

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Sterols are secondary metabolites, they are considered bioactive, due to their recognized activity as antioxidants, anticarcinogenic, cardiovascular protectors, and antiviral capacity. These triterpenoids can be found in a wide range of concentrations in different algae strains, being the variations related to external factors. In the world, there are millions of algae, some strains have the ability to produce high-value phytosterols, like stigmasterol, and sitosterol, however, others could lead to cholesterol production. For this reason, understand the principal factors involved in sterols biosynthesis, allows us to appoint the algae strain for industrial application and escalating these specific compounds production. Some algae are capable to produce sterols from mevalonic acid pathway, other strains present the methylerythritol 4-phosphate (MEP), or 1-deoxy-D-xylulose-5-phosphate (DOXP) as the main pathway, each one is responsible for the production of plans of intermediary compounds. In this sense, this chapter summarizes current knowledge of the biosynthetic pathways responsible for different sterols formation, as well as, describe main sterols that could be isolated from algae metabolism.
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Rohmer, Michel. "Methylerythritol Phosphate Pathway." In Comprehensive Natural Products III, 560–90. Elsevier, 2010. http://dx.doi.org/10.1016/b978-0-08-102690-8.00702-8.

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10

Rohmer, Michel. "Methylerythritol Phosphate Pathway." In Comprehensive Natural Products II, 517–55. Elsevier, 2010. http://dx.doi.org/10.1016/b978-008045382-8.00702-4.

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