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Автор: Grafiati
Опубліковано: 7 липня 2024
Оновлено: 7 липня 2024

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1

Lee, Pyung Cheon, Christine Salomon, Benjamin Mijts, and Claudia Schmidt-Dannert. "Biosynthesis of Ubiquinone Compounds with Conjugated Prenyl Side Chains." Applied and Environmental Microbiology 74, no. 22 (September 26, 2008): 6908–17. http://dx.doi.org/10.1128/aem.01495-08.

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ABSTRACT Enzymatic steps from two different biosynthetic pathways were combined in Escherichia coli, directing the synthesis of a new class of biomolecules—ubiquinones with prenyl side chains containing conjugated double bonds. This was achieved by the activity of a C30 carotenoid desaturase, CrtN, from Staphylococcus aureus, which exhibited an inherent flexibility in substrate recognition compared to other carotenoid desaturases. By utilizing the known plasticity of E. coli's native ubiquinone biosynthesis pathway and the unusual activity of CrtN, modified ubiquinone structures with prenyl side chains containing conjugated double bonds were generated. The side chains of the new structures were confirmed to have different degrees of desaturation by mass spectrometry and nuclear magnetic resonance analysis. In vivo 14C labeling and in vitro activity studies showed that CrtN desaturates octaprenyl diphosphates but not the ubiquinone compounds directly. Antioxidant properties of conjugated side chain ubiquinones were analyzed in an in vitro β-carotene-linoleate model system and were found to be higher than the corresponding unmodified ubiquinones. These results demonstrate that by combining pathway steps from different branches of biosynthetic networks, classes of compounds not observed in nature can be synthesized and structural motifs that are functionally important can be combined or enhanced.
2

Wilton, D. C. "The effect of excess mevalonic acid on ubiquinone and tetrahymanol biosynthesis in Tetrahymena pyriformis." Biochemical Journal 229, no. 2 (July 15, 1985): 551–53. http://dx.doi.org/10.1042/bj2290551.

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When T. pyriformis is grown in the presence of 10(-2)M-mevalonic acid, the uptake exceeds the cell's requirement for this biosynthetic intermediate. The majority of the excess mevalonic acid is diverted into ubiquinone-8 biosynthesis whereas the biosynthesis of tetrahymanol, the major product of the mevalonic acid pathway, is unchanged. In the presence of excess external mevalonic acid, the biosynthesis of mevalonic acid by the cell is inhibited. It is proposed that ubiquinone biosynthesis is normally regulated by mevalonic acid availability, whereas tetrahymanol biosynthesis is regulated primarily at a later point in the pathway.
3

Szkopińska, A. "Ubiquinone. Biosynthesis of quinone ring and its isoprenoid side chain. Intracellular localization." Acta Biochimica Polonica 47, no. 2 (June 30, 2000): 469–80. http://dx.doi.org/10.18388/abp.2000_4027.

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Ubiquinone, known as coenzyme Q, was shown to be the part of the metabolic pathways by Crane et al. in 1957. Its function as a component of the mitochondrial respiratory chain is well established. However, ubiquinone has recently attracted increasing attention with regard to its function, in the reduced form, as an antioxidant. In ubiquinone synthesis the para-hydroxybenzoate ring (which is the derivative of tyrosine or phenylalanine) is condensed with a hydrophobic polyisoprenoid side chain, whose length varies from 6 to 10 isoprene units depending on the organism. para-Hydroxybenzoate (PHB) polyprenyltransferase that catalyzes the condensation of PHB with polyprenyl diphosphate has a broad substrate specificity. Most of the genes encoding (all-E)-prenyltransferases which synthesize polyisoprenoid chains, have been cloned. Their structure is either homo- or heterodimeric. Genes that encode prenyltransferases catalysing the transfer of the isoprenoid chain to para-hydroxybenzoate were also cloned in bacteria and yeast. To form ubiquinone, prenylated PHB undergoes several modifications such as hydroxylations, O-methylations, methylations and decarboxylation. In eukaryotes ubiquinones were found in the inner mitochondrial membrane and in other membranes such as the endoplasmic reticulum, Golgi vesicles, lysosomes and peroxisomes. Still, the subcellular site of their biosynthesis remains unclear. Considering the diversity of functions of ubiquinones, and their multistep biosynthesis, identification of factors regulating their cellular level remains an elusive task.
4

Meganathan, R. "Ubiquinone biosynthesis in microorganisms." FEMS Microbiology Letters 203, no. 2 (September 2001): 131–39. http://dx.doi.org/10.1111/j.1574-6968.2001.tb10831.x.

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5

Rötig, Agnès. "News in Ubiquinone Biosynthesis." Chemistry & Biology 17, no. 5 (May 2010): 415–16. http://dx.doi.org/10.1016/j.chembiol.2010.05.001.

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6

Kaneshiro, Edna S., Donggeun Sul, and Banasri Hazra. "Effects of Atovaquone and Diospyrin-Based Drugs on Ubiquinone Biosynthesis in Pneumocystis carinii Organisms." Antimicrobial Agents and Chemotherapy 44, no. 1 (January 1, 2000): 14–18. http://dx.doi.org/10.1128/aac.44.1.14-18.2000.

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ABSTRACT The naphthoquinone atovaquone is effective againstPlasmodium and Pneumocystis carinii carinii. InPlasmodium, the primary mechanism of drug action is an irreversible binding to the mitochondrial cytochromebc 1 complex as an analog of ubiquinone. Blockage of the electron transport chain ultimately inhibits de novo pyrimidine biosynthesis since dihydroorotate dehydrogenase, a key enzyme in pyrimidine biosynthesis, is unable to transfer electrons to ubiquinone. In the present study, the effect of atovaquone was examined on Pneumocystis carinii carinii coenzyme Q biosynthesis (rather than electron transport and respiration) by measuring its effect on the incorporation of radiolabeledp-hydroxybenzoate into ubiquinone in vitro. A triphasic dose-response was observed, with inhibition at 10 nM and then stimulation up to 0.2 μM, followed by inhibition at 1 μM. Since other naphthoquinone drugs may also act as analogs of ubiquinone, diospyrin and two of its derivatives were also tested for their effects on ubiquinone biosynthesis in P. carinii carinii. In contrast to atovaquone, these drugs did not inhibit the incorporation of p-hydroxybenzoate intoP. carinii carinii ubiquinone.
7

Bekker, Martijn, Svetlana Alexeeva, Wouter Laan, Gary Sawers, Joost Teixeira de Mattos, and Klaas Hellingwerf. "The ArcBA Two-Component System of Escherichia coli Is Regulated by the Redox State of both the Ubiquinone and the Menaquinone Pool." Journal of Bacteriology 192, no. 3 (November 20, 2009): 746–54. http://dx.doi.org/10.1128/jb.01156-09.

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ABSTRACT ArcBA is a two-component regulatory system of Escherichia coli involved in sensing oxygen availability and the concomitant transcriptional regulation of oxidative and fermentative catabolism. Based on in vitro data, it has been postulated that the redox state of the ubiquinone pool is the determinant for ArcB kinase activity. Here we report on the in vivo regulation of ArcB activation, as determined using a lacZ reporter specifically responsive to phosphorylated ArcA. Our results indicate that upon deletion of a ubiquinone biosynthetic enzyme, regulation of ArcB in the anaerobic-aerobic transition is not affected. In contrast, interference with menaquinone biosynthesis leads to inactivation of ArcB during anaerobic growth; this phenotype is fully rescued by addition of a menaquinone precursor. This clearly demonstrates that the menaquinones play a major role in ArcB activation. ArcB shows a complex pattern of regulation when E. coli is titrated through the entire aerobiosis range; ArcB is activated under anaerobic and subaerobic conditions and is much less active under fully aerobic and microaerobic conditions. Furthermore, there is no correlation between ArcB activation and the redox state of the ubiquinone pool, but there is a restricted correlation between the total cellular ubiquinone content and ArcB activity due to the considerable increase in the size of the ubiquinone pool with increasing degrees of aerobiosis. These results lead to the working hypothesis that the in vivo activity of ArcB in E. coli is modulated by the redox state of the menaquinone pool and that the ubiquinone/ubiquinol ratio in vivo surely is not the only determinant of ArcB activity.
8

Wang, Ying, and Siegfried Hekimi. "Mitochondrial respiration without ubiquinone biosynthesis." Human Molecular Genetics 22, no. 23 (July 11, 2013): 4768–83. http://dx.doi.org/10.1093/hmg/ddt330.

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9

Soubeyrand, Eric, Megan Kelly, Shea A. Keene, Ann C. Bernert, Scott Latimer, Timothy S. Johnson, Christian Elowsky, Thomas A. Colquhoun, Anna K. Block, and Gilles J. Basset. "Arabidopsis 4-COUMAROYL-COA LIGASE 8 contributes to the biosynthesis of the benzenoid ring of coenzyme Q in peroxisomes." Biochemical Journal 476, no. 22 (November 27, 2019): 3521–32. http://dx.doi.org/10.1042/bcj20190688.

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Plants have evolved the ability to derive the benzenoid moiety of the respiratory cofactor and antioxidant, ubiquinone (coenzyme Q), either from the β-oxidative metabolism of p-coumarate or from the peroxidative cleavage of kaempferol. Here, isotopic feeding assays, gene co-expression analysis and reverse genetics identified Arabidopsis 4-COUMARATE-COA LIGASE 8 (4-CL8; At5g38120) as a contributor to the β-oxidation of p-coumarate for ubiquinone biosynthesis. The enzyme is part of the same clade (V) of acyl-activating enzymes than At4g19010, a p-coumarate CoA ligase known to play a central role in the conversion of p-coumarate into 4-hydroxybenzoate. A 4-cl8 T-DNA knockout displayed a 20% decrease in ubiquinone content compared with wild-type plants, while 4-CL8 overexpression boosted ubiquinone content up to 150% of the control level. Similarly, the isotopic enrichment of ubiquinone's ring was decreased by 28% in the 4-cl8 knockout as compared with wild-type controls when Phe-[Ring-13C6] was fed to the plants. This metabolic blockage could be bypassed via the exogenous supply of 4-hydroxybenzoate, the product of p-coumarate β-oxidation. Arabidopsis 4-CL8 displays a canonical peroxisomal targeting sequence type 1, and confocal microscopy experiments using fused fluorescent reporters demonstrated that this enzyme is imported into peroxisomes. Time course feeding assays using Phe-[Ring-13C6] in a series of Arabidopsis single and double knockouts blocked in the β-oxidative metabolism of p-coumarate (4-cl8; at4g19010; at4g19010 × 4-cl8), flavonol biosynthesis (flavanone-3-hydroxylase), or both (at4g19010 × flavanone-3-hydroxylase) indicated that continuous high light treatments (500 µE m−2 s−1; 24 h) markedly stimulated the de novo biosynthesis of ubiquinone independently of kaempferol catabolism.
10

Kalén, A., E. L. Appelkvist, G. Dallner, Bertil Andersson, and Hans-Erik Åkerlund. "Biosynthesis of Ubiquinone in Rat Liver." Acta Chemica Scandinavica 41b (1987): 70–72. http://dx.doi.org/10.3891/acta.chem.scand.41b-0070.

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11

Ranganathan, Gouri, and Antony J. Mukkada. "Ubiquinone biosynthesis in Leishmania major promastigotes." International Journal for Parasitology 25, no. 3 (March 1995): 279–84. http://dx.doi.org/10.1016/0020-7519(94)00131-7.

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12

Tekle, Michael, Magnus Bentinger, Tomas Nordman, Eeva-Liisa Appelkvist, Tadeusz Chojnacki, and Jerker M. Olsson. "Ubiquinone Biosynthesis in Rat Liver Peroxisomes." Biochemical and Biophysical Research Communications 291, no. 5 (March 2002): 1128–33. http://dx.doi.org/10.1006/bbrc.2002.6537.

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13

Pravst, Igor, Juan Carlos Rodríguez Aguilera, Ana Belen Cortes Rodriguez, Janja Jazbar, Igor Locatelli, Hristo Hristov, and Katja Žmitek. "Comparative Bioavailability of Different Coenzyme Q10 Formulations in Healthy Elderly Individuals." Nutrients 12, no. 3 (March 16, 2020): 784. http://dx.doi.org/10.3390/nu12030784.

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Coenzyme Q10 (CoQ10) plays a central role in mitochondrial oxidative phosphorylation. Several studies have shown the beneficial effects of dietary CoQ10 supplementation, particularly in relation to cardiovascular health. CoQ10 biosynthesis decreases in the elderly, and consequently, the beneficial effects of dietary supplementation in this population are of greater significance. However, most pharmacokinetic studies have been conducted on younger populations. The aim of this study was to investigate the single-dose bioavailability of different formulations of CoQ10 in a healthy geriatric population. A randomized, three-period, crossover bioavailability study was conducted on 21 healthy older adults (aged 65–74). The treatment was a single dose with a one-week washout period. Three different formulations containing the equivalent of 100 mg of CoQ10 were used: Q10Vital® water-soluble CoQ10 syrup (the investigational product—IP); ubiquinol capsules (the comparative product—CP); and ubiquinone capsules (the standard product—SP). Ubiquinone/ubiquinol was followed in the plasma for 48 h. An analysis of the ratio of the area under the baseline-corrected concentration curve (ΔAUC48) for total CoQ10 and a comparison to SP yielded the following: The bioavailability of CoQ10 in the IP was 2.4-fold higher (95% CI: 1.3–4.5; p = 0.002), while the bioavailability of ubiquinol (CP) was not significantly increased (1.7-fold; 95% CI: 0.9–3.1, p = 0.129). No differences in the redox status of the absorbed coenzyme Q10 were observed between formulations, showing that CoQ10 appeared in the blood mostly as ubiquinol, even if consumed as ubiquinone.
14

Brajcich, Brian C., Andrew L. Iarocci, Lindsey A. G. Johnstone, Rory K. Morgan, Zachary T. Lonjers, Matthew J. Hotchko, Jordan D. Muhs, et al. "Evidence that Ubiquinone Is a Required Intermediate for Rhodoquinone Biosynthesis in Rhodospirillum rubrum." Journal of Bacteriology 192, no. 2 (November 20, 2009): 436–45. http://dx.doi.org/10.1128/jb.01040-09.

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ABSTRACT Rhodoquinone (RQ) is an important cofactor used in the anaerobic energy metabolism of Rhodospirillum rubrum. RQ is structurally similar to ubiquinone (coenzyme Q or Q), a polyprenylated benzoquinone used in the aerobic respiratory chain. RQ is also found in several eukaryotic species that utilize a fumarate reductase pathway for anaerobic respiration, an important example being the parasitic helminths. RQ is not found in humans or other mammals, and therefore inhibition of its biosynthesis may provide a parasite-specific drug target. In this report, we describe several in vivo feeding experiments with R. rubrum used for the identification of RQ biosynthetic intermediates. Cultures of R. rubrum were grown in the presence of synthetic analogs of ubiquinone and the known Q biosynthetic precursors demethylubiquinone, demethoxyubiquinone, and demethyldemethoxyubiquinone, and assays were monitored for the formation of RQ3. Data from time course experiments and S-adenosyl-l-methionine-dependent O-methyltransferase inhibition studies are discussed. Based on the results presented, we have demonstrated that Q is a required intermediate for the biosynthesis of RQ in R. rubrum.
15

Muraki, Ayako, Kazutoshi Miyashita, Masanori Mitsuishi, Masanori Tamaki, Kumiko Tanaka, and Hiroshi Itoh. "Coenzyme Q10 reverses mitochondrial dysfunction in atorvastatin-treated mice and increases exercise endurance." Journal of Applied Physiology 113, no. 3 (August 1, 2012): 479–86. http://dx.doi.org/10.1152/japplphysiol.01362.2011.

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Statins are cholesterol-lowering drugs widely used in the prevention of cardiovascular diseases; however, they are associated with various types of myopathies. Statins inhibit 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase and thus decrease biosynthesis of low-density lipoprotein cholesterol and may also reduce ubiquinones, essential coenzymes of a mitochondrial electron transport chain, which contain isoprenoid residues, synthesized through an HMG-CoA reductase-dependent pathway. Therefore, we hypothesized that statin treatment might influence physical performance through muscular mitochondrial dysfunction due to ubiquinone deficiency. The effect of two statins, atorvastatin and pravastatin, on ubiquinone content, mitochondrial function, and physical performance was examined by using statin-treated mice. Changes in energy metabolism in association with statin treatment were studied by using cultured myocytes. We found that atorvastatin-treated mice developed muscular mitochondrial dysfunction due to ubiquinone deficiency and a decrease in exercise endurance without affecting muscle mass and strength. Meanwhile, pravastatin at ten times higher dose of atorvastatin had no such effects. In cultured myocytes, atorvastatin-related decrease in mitochondrial activity led to a decrease in oxygen utilization and an increase in lactate production. Conversely, coenzyme Q10 treatment in atorvastatin-treated mice reversed atorvastatin-related mitochondrial dysfunction and a decrease in oxygen utilization, and thus improved exercise endurance. Atorvastatin decreased exercise endurance in mice through mitochondrial dysfunction due to ubiquinone deficiency. Ubiquinone supplementation with coenzyme Q10 could reverse atorvastatin-related mitochondrial dysfunction and decrease in exercise tolerance.
16

Coskun, Abdurrahman, Mustafa Serteser, and Ibrahim Unsal. "Inhibition of Cholesterol Biosynthesis in Hypercholesterolemia – Is It the Right Choice? / Inhibicija Biosinteze Holesterola u Hiperholesterolemiji – Da Li Je Pravi Izbor?" Journal of Medical Biochemistry 32, no. 1 (January 1, 2013): 16–19. http://dx.doi.org/10.2478/v10011-012-0020-3.

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Summary Cholesterol biosynthesis is a complex pathway comprising more than 20 biochemical reactions. Although the final product created in the pathway is cholesterol, the intermediate products, such as ubiquinone and dolichol, also provide vital metabolic functions. Statins are HGM-CoA reductase inhibitors that stop the production of cholesterol by directly inhibiting the mevalonate production. Mevalonate is a precursor of two additional vital molecules, squalene and ubiquinone (coenzyme Q10). We hypothesized that inhibiting the cholesterol biosynthesis with statins for an extended duration may potentiate the oxidative stress, neurodegenerative disease and cancer. Our recommendation was to measure muscle enzymes, antioxidant capacity, and ubiquinone to monitor patients receiving the statins for prolonged periods of time.
17

Ohara, Kazuaki, Ayumu Muroya, Nobuhiro Fukushima, and Kazufumi Yazaki. "Functional characterization of LePGT1, a membrane-bound prenyltransferase involved in the geranylation of p-hydroxybenzoic acid." Biochemical Journal 421, no. 2 (June 26, 2009): 231–41. http://dx.doi.org/10.1042/bj20081968.

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The AS-PT (aromatic substrate prenyltransferase) family plays a critical role in the biosynthesis of important quinone compounds such as ubiquinone and plastoquinone, although biochemical characterizations of AS-PTs have rarely been carried out because most members are membrane-bound enzymes with multiple transmembrane α-helices. PPTs [PHB (p-hydroxybenzoic acid) prenyltransferases] are a large subfamily of AS-PTs involved in ubiquinone and naphthoquinone biosynthesis. LePGT1 [Lithospermum erythrorhizon PHB geranyltransferase] is the regulatory enzyme for the biosynthesis of shikonin, a naphthoquinone pigment, and was utilized in the present study as a representative of membrane-type AS-PTs to clarify the function of this enzyme family at the molecular level. Site-directed mutagenesis of LePGT1 with a yeast expression system indicated three out of six conserved aspartate residues to be critical to the enzymatic activity. A detailed kinetic analysis of mutant enzymes revealed the amino acid residues responsible for substrate binding were also identified. Contrary to ubiquinone biosynthetic PPTs, such as UBIA in Escherichia coli which accepts many prenyl substrates of different chain lengths, LePGT1 can utilize only geranyl diphosphate as its prenyl substrate. Thus the substrate specificity was analysed using chimeric enzymes derived from LePGT1 and UBIA. In vitro and in vivo analyses of the chimeras suggested that the determinant region for this specificity was within 130 amino acids of the N-terminal. A 3D (three-dimensional) molecular model of the substrate-binding site consistent with these biochemical findings was generated.
18

Uchida, Naonori, Kengo Suzuki, Ryoichi Saiki, Tomohiro Kainou, Katsunori Tanaka, Hideyuki Matsuda, and Makoto Kawamukai. "Phenotypes of Fission Yeast Defective in Ubiquinone Production Due to Disruption of the Gene for p-Hydroxybenzoate Polyprenyl Diphosphate Transferase." Journal of Bacteriology 182, no. 24 (December 15, 2000): 6933–39. http://dx.doi.org/10.1128/jb.182.24.6933-6939.2000.

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ABSTRACT Ubiquinone is an essential component of the electron transfer system in both prokaryotes and eukaryotes and is synthesized from chorismate and polyprenyl diphosphate by eight steps.p-Hydroxybenzoate (PHB) polyprenyl diphosphate transferase catalyzes the condensation of PHB and polyprenyl diphosphate in ubiquinone biosynthesis. We isolated the gene (designated ppt1) encoding PHB polyprenyl diphosphate transferase from Schizosaccharomyces pombe and constructed a strain with a disrupted ppt1 gene. This strain could not grow on minimal medium supplemented with glucose. Expression ofCOQ2 from Saccharomyces cerevisiae in the defective S. pombe strain restored growth and enabled the cells to produce ubiquinone-10, indicating that COQ2 andppt1 are functional homologs. Theppt1-deficient strain required supplementation with antioxidants, such as cysteine, glutathione, and α-tocopherol, to grow on minimal medium. This suggests that ubiquinone can act as an antioxidant, a premise supported by our observation that theppt1-deficient strain is sensitive to H2O2 and Cu2+. Interestingly, we also found that the ppt1-deficient strain produced a significant amount of H2S, which suggests that oxidation of sulfide by ubiquinone may be an important pathway for sulfur metabolism in S. pombe. Ppt1-green fluorescent protein fusion proteins localized to the mitochondria, indicating that ubiquinone biosynthesis occurs in the mitochondria in S. pombe. Thus, analysis of the phenotypes of S. pombe strains deficient in ubiquinone production clearly demonstrates that ubiquinone has multiple functions in the cell apart from being an integral component of the electron transfer system.
19

Shepherd, Jennifer A., Wayne W. Poon, David C. Myles, and Catherine F. Clarke. "The biosynthesis of ubiquinone: Synthesis and enzymatic modification of biosynthetic precursors." Tetrahedron Letters 37, no. 14 (April 1996): 2395–98. http://dx.doi.org/10.1016/0040-4039(96)00324-3.

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20

Wang, Ying, and Siegfried Hekimi. "Molecular genetics of ubiquinone biosynthesis in animals." Critical Reviews in Biochemistry and Molecular Biology 48, no. 1 (November 29, 2012): 69–88. http://dx.doi.org/10.3109/10409238.2012.741564.

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21

Cheng, W., and W. Li. "Structural Insights into Ubiquinone Biosynthesis in Membranes." Science 343, no. 6173 (February 20, 2014): 878–81. http://dx.doi.org/10.1126/science.1246774.

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22

Kawamukai, Makoto. "Biosynthesis, bioproduction and novel roles of ubiquinone." Journal of Bioscience and Bioengineering 94, no. 6 (December 2002): 511–17. http://dx.doi.org/10.1016/s1389-1723(02)80188-8.

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23

KAWAMUKAI, MAKOTO. "Biosynthesis, Bioproduction and Novel Roles of Ubiquinone." Journal of Bioscience and Bioengineering 94, no. 6 (2002): 511–17. http://dx.doi.org/10.1263/jbb.94.511.

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24

Sadre, Radin, Christian Pfaff, and Stephan Buchkremer. "Plastoquinone-9 biosynthesis in cyanobacteria differs from that in plants and involves a novel 4-hydroxybenzoate solanesyltransferase." Biochemical Journal 442, no. 3 (February 24, 2012): 621–29. http://dx.doi.org/10.1042/bj20111796.

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PQ-9 (plastoquinone-9) has a central role in energy transformation processes in cyanobacteria by mediating electron transfer in both the photosynthetic as well as the respiratory electron transport chain. The present study provides evidence that the PQ-9 biosynthetic pathway in cyanobacteria differs substantially from that in plants. We identified 4-hydroxybenzoate as being the aromatic precursor for PQ-9 in Synechocystis sp. PCC6803, and in the present paper we report on the role of the membrane-bound 4-hydroxybenzoate solanesyltransferase, Slr0926, in PQ-9 biosynthesis and on the properties of the enzyme. The catalytic activity of Slr0926 was demonstrated by in vivo labelling experiments in Synechocystis sp., complementation studies in an Escherichia coli mutant with a defect in ubiquinone biosynthesis, and in vitro assays using the recombinant as well as the native enzyme. Although Slr0926 was highly specific for the prenyl acceptor substrate 4-hydroxybenzoate, it displayed a broad specificity with regard to the prenyl donor substrate and used not only solanesyl diphosphate, but also a number of shorter-chain prenyl diphosphates. In combination with in silico data, our results indicate that Slr0926 evolved from bacterial 4-hydroxybenzoate prenyltransferases catalysing prenylation in the course of ubiquinone biosynthesis.
25

Fernández-del-Río, Lucía, and Catherine F. Clarke. "Coenzyme Q Biosynthesis: An Update on the Origins of the Benzenoid Ring and Discovery of New Ring Precursors." Metabolites 11, no. 6 (June 14, 2021): 385. http://dx.doi.org/10.3390/metabo11060385.

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Coenzyme Q (ubiquinone or CoQ) is a conserved polyprenylated lipid essential for mitochondrial respiration. CoQ is composed of a redox-active benzoquinone ring and a long polyisoprenyl tail that serves as a membrane anchor. A classic pathway leading to CoQ biosynthesis employs 4-hydroxybenzoic acid (4HB). Recent studies with stable isotopes in E. coli, yeast, and plant and animal cells have identified CoQ intermediates and new metabolic pathways that produce 4HB. Stable isotope labeling has identified para-aminobenzoic acid as an alternate ring precursor of yeast CoQ biosynthesis, as well as other natural products, such as kaempferol, that provide ring precursors for CoQ biosynthesis in plants and mammals. In this review, we highlight how stable isotopes can be used to delineate the biosynthetic pathways leading to CoQ.
26

Henry, A., P. W. Stacpoole, and C. M. Allen. "Dolichol biosynthesis in human malignant cells." Biochemical Journal 278, no. 3 (September 15, 1991): 741–47. http://dx.doi.org/10.1042/bj2780741.

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Cholesterol, ubiquinone and dolichol biosynthesis from mevalonic acid was measured in non-malignant and malignant cultured human lymphocytes, freshly isolated human mononuclear leucocytes and in cultured human hepatoma cells. The relative flux of mevalonate into ubiquinone, dilichol and cholesterol was not significantly different between malignant and non-malignant cells, although the extent of labelling of each product was an order of magnitude greater in the malignant cultured cells. The most prominent dolichol isolated from total cellular lipid and synthesized in short-term labelling of cultured leukaemic cells had a chain length one isoprene unit shorter than that observed in normal human cells. Cultured human hepatoma cells and mononuclear leucocytes isolated from the peripheral blood of individuals with lymphoblastic and myelogenic leukaemia similarly synthesized shorter-chain dolichols. The dolichols made in cultured non-tumorigenic cells, freshly isolated mononuclear leucocytes from a normal individual or a patient with non-haematological malignancy had normal chain length.
27

Kazemzadeh, Katayoun, Sophie-Carole Chobert, Mahmoud Hajj Chehade, Nelle Varoquaux, John Willison, Ivan Junier, Sophie Abby, Ludovic Pelosi, and Fabien Pierrel. "Biosynthesis and Physiology of Ubiquinone under anaerobic conditions." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1863 (September 2022): 148694. http://dx.doi.org/10.1016/j.bbabio.2022.148694.

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28

Heide, L., and H. Floss. "Ubiquinone Biosynthesis inE. coli: Origin ofp-Hydroxybenzoic Acid." Planta Medica 55, no. 07 (December 1989): 592–93. http://dx.doi.org/10.1055/s-2006-962127.

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29

Zhu, Xufen, Mihoko Yuasa, Kazunori Okada, Kengo Suzuki, Tsuyoshi Nakagawa, Makoto Kawamukai, and Hideyuki Matsuda. "Production of ubiquinone in Escherichia coli by expression of various genes responsible for ubiquinone biosynthesis." Journal of Fermentation and Bioengineering 79, no. 5 (January 1995): 493–95. http://dx.doi.org/10.1016/0922-338x(95)91268-a.

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30

Shams, Somayeh, Ahmad Ismaili, Farhad Nazarian Firouzabadi, Hasan Mumivand, and Karim Sorkheh. "Comparative transcriptome analysis to identify putative genes involved in carvacrol biosynthesis pathway in two species of Satureja, endemic medicinal herbs of Iran." PLOS ONE 18, no. 7 (July 7, 2023): e0281351. http://dx.doi.org/10.1371/journal.pone.0281351.

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Satureja is rich in phenolic monoterpenoids, mainly carvacrol, that is of interest due to diverse biological activities including antifungal and antibacterial. However, limited information is available regarding the molecular mechanisms underlying carvacrol biosynthesis and its regulation for this wonderful medicinal herb. To identify the putative genes involved in carvacrol and other monoterpene biosynthesis pathway, we generated a reference transcriptome in two endemic Satureja species of Iran, containing different yields (Satureja khuzistanica and Satureja rechingeri). Cross-species differential expression analysis was conducted between two species of Satureja. 210 and 186 transcripts related to terpenoid backbone biosynthesis were identified for S. khuzistanica and S. rechingeri, respectively. 29 differentially expressed genes (DEGs) involved in terpenoid biosynthesis were identified, and these DEGs were significantly enriched in monoterpenoid biosynthesis, diterpenoid biosynthesis, sesquiterpenoid and triterpenoid biosynthesis, carotenoid biosynthesis and ubiquinone and other terpenoid-quinone biosynthesis pathways. Expression patterns of S. khuzistanica and S. rechingeri transcripts involved in the terpenoid biosynthetic pathway were evaluated. In addition, we identified 19 differentially expressed transcription factors (such as MYC4, bHLH, and ARF18) that may control terpenoid biosynthesis. We confirmed the altered expression levels of DEGs that encode carvacrol biosynthetic enzymes using quantitative real-time PCR (qRT-PCR). This study is the first report on de novo assembly and transcriptome data analysis in Satureja which could be useful for an understanding of the main constituents of Satureja essential oil and future research in this genus.
31

Poon, Wayne W., Diana E. Davis, Huan T. Ha, Tanya Jonassen, Philip N. Rather, and Catherine F. Clarke. "Identification of Escherichia coli ubiB, a Gene Required for the First Monooxygenase Step in Ubiquinone Biosynthesis." Journal of Bacteriology 182, no. 18 (September 15, 2000): 5139–46. http://dx.doi.org/10.1128/jb.182.18.5139-5146.2000.

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ABSTRACT It was recently discovered that the aarF gene inProvidencia stuartii is required for coenzyme Q (CoQ) biosynthesis. Here we report that yigR, theEscherichia coli homologue of aarF, isubiB, a gene required for the first monooxygenase step in CoQ biosynthesis. Both the P. stuartii aarF and E. coli ubiB (yigR) disruption mutant strains lack CoQ and accumulate octaprenylphenol. Octaprenylphenol is the CoQ biosynthetic intermediate found to accumulate in the E. coli strain AN59, which contains the ubiB409 mutant allele. Analysis of the mutation in the E. coli strain AN59 reveals no mutations within the ubiB gene, but instead shows the presence of an IS1 element at position +516 of the ubiE gene. The ubiE gene encodes aC-methyltransferase required for the synthesis of both CoQ and menaquinone, and it is the 5′ gene in an operon containingubiE, yigP, and ubiB. The data indicate that octaprenylphenol accumulates in AN59 as a result of a polar effect of the ubiE::IS1mutation on the downstream ubiB gene. AN59 is complemented by a DNA segment containing the contiguous ubiE,yigP, and ubiB genes. Although transformation of AN59 with a DNA segment containing the ubiB coding region fails to restore CoQ biosynthesis, transformation with theubiE coding region results in a low-frequency but significant rescue attributed to homologous recombination. In addition, the fre gene, previously considered to correspond toubiB, was found not to be involved in CoQ biosynthesis. TheubiB gene is a member of a predicted protein kinase family of which the Saccharomyces cerevisiae ABC1 gene is the prototypic member. The possible protein kinase function of UbiB and Abc1 and the role these polypeptides may play in CoQ biosynthesis are discussed.
32

Marbois, B. Noelle, and Catherine F. Clarke. "TheCOQ7Gene Encodes a Protein inSaccharomyces cerevisiaeNecessary for Ubiquinone Biosynthesis." Journal of Biological Chemistry 271, no. 6 (February 9, 1996): 2995–3004. http://dx.doi.org/10.1074/jbc.271.6.2995.

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33

Kalén, A., B. Norling, E. L. Appelkvist, and G. Dallner. "Ubiquinone biosynthesis by the microsomal fraction from rat liver." Biochimica et Biophysica Acta (BBA) - General Subjects 926, no. 1 (October 1987): 70–78. http://dx.doi.org/10.1016/0304-4165(87)90183-8.

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34

Abby, Sophie Saphia, Katayoun Kazemzadeh, Charles Vragniau, Ludovic Pelosi, and Fabien Pierrel. "Advances in bacterial pathways for the biosynthesis of ubiquinone." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1861, no. 11 (November 2020): 148259. http://dx.doi.org/10.1016/j.bbabio.2020.148259.

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35

Awad, Agape M., Michelle C. Bradley, Lucía Fernández-del-Río, Anish Nag, Hui S. Tsui, and Catherine F. Clarke. "Coenzyme Q10 deficiencies: pathways in yeast and humans." Essays in Biochemistry 62, no. 3 (July 6, 2018): 361–76. http://dx.doi.org/10.1042/ebc20170106.

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Coenzyme Q (ubiquinone or CoQ) is an essential lipid that plays a role in mitochondrial respiratory electron transport and serves as an important antioxidant. In human and yeast cells, CoQ synthesis derives from aromatic ring precursors and the isoprene biosynthetic pathway. Saccharomyces cerevisiae coq mutants provide a powerful model for our understanding of CoQ biosynthesis. This review focusses on the biosynthesis of CoQ in yeast and the relevance of this model to CoQ biosynthesis in human cells. The COQ1–COQ11 yeast genes are required for efficient biosynthesis of yeast CoQ. Expression of human homologs of yeast COQ1–COQ10 genes restore CoQ biosynthesis in the corresponding yeast coq mutants, indicating profound functional conservation. Thus, yeast provides a simple yet effective model to investigate and define the function and possible pathology of human COQ (yeast or human gene involved in CoQ biosynthesis) gene polymorphisms and mutations. Biosynthesis of CoQ in yeast and human cells depends on high molecular mass multisubunit complexes consisting of several of the COQ gene products, as well as CoQ itself and CoQ intermediates. The CoQ synthome in yeast or Complex Q in human cells, is essential for de novo biosynthesis of CoQ. Although some human CoQ deficiencies respond to dietary supplementation with CoQ, in general the uptake and assimilation of this very hydrophobic lipid is inefficient. Simple natural products may serve as alternate ring precursors in CoQ biosynthesis in both yeast and human cells, and these compounds may act to enhance biosynthesis of CoQ or may bypass certain deficient steps in the CoQ biosynthetic pathway.
36

Roberts Buceta, Paloma M., Laura Romanelli-Cedrez, Shannon J. Babcock, Helen Xun, Miranda L. VonPaige, Thomas W. Higley, Tyler D. Schlatter, et al. "The kynurenine pathway is essential for rhodoquinone biosynthesis in Caenorhabditis elegans." Journal of Biological Chemistry 294, no. 28 (June 7, 2019): 11047–53. http://dx.doi.org/10.1074/jbc.ac119.009475.

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A key metabolic adaptation of some species that face hypoxia as part of their life cycle involves an alternative electron transport chain in which rhodoquinone (RQ) is required for fumarate reduction and ATP production. RQ biosynthesis in bacteria and protists requires ubiquinone (Q) as a precursor. In contrast, Q is not a precursor for RQ biosynthesis in animals such as parasitic helminths, and most details of this pathway have remained elusive. Here, we used Caenorhabditis elegans as a model animal to elucidate key steps in RQ biosynthesis. Using RNAi and a series of C. elegans mutants, we found that arylamine metabolites from the kynurenine pathway are essential precursors for RQ biosynthesis de novo. Deletion of kynu-1, encoding a kynureninase that converts l-kynurenine (KYN) to anthranilic acid (AA) and 3-hydroxykynurenine (3HKYN) to 3-hydroxyanthranilic acid (3HAA), completely abolished RQ biosynthesis but did not affect Q levels. Deletion of kmo-1, which encodes a kynurenine 3-monooxygenase that converts KYN to 3HKYN, drastically reduced RQ but not Q levels. Knockdown of the Q biosynthetic genes coq-5 and coq-6 affected both Q and RQ levels, indicating that both biosynthetic pathways share common enzymes. Our study reveals that two pathways for RQ biosynthesis have independently evolved. Unlike in bacteria, where amination is the last step in RQ biosynthesis, in worms the pathway begins with the arylamine precursor AA or 3HAA. Because RQ is absent in mammalian hosts of helminths, inhibition of RQ biosynthesis may have potential utility for targeting parasitic infections that cause important neglected tropical diseases.
37

Tonhosolo, Renata, Fabio L. D'Alexandri, Fernando A. Genta, Gerhard Wunderlich, Fabio C. Gozzo, Marcos N. Eberlin, Valnice J. Peres, Emilia A. Kimura, and Alejandro M. Katzin. "Identification, molecular cloning and functional characterization of an octaprenyl pyrophosphate synthase in intra-erythrocytic stages of Plasmodium falciparum." Biochemical Journal 392, no. 1 (November 8, 2005): 117–26. http://dx.doi.org/10.1042/bj20050441.

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Isoprenoids play important roles in all living organisms as components of structural cholesterol, steroid hormones in mammals, carotenoids in plants, and ubiquinones. Significant differences occur in the length of the isoprenic side chains of ubiquinone between different organisms, suggesting that different enzymes are involved in the synthesis of these side chains. Whereas in Plasmodium falciparum the isoprenic side chains of ubiquinone contain 7–9 isoprenic units, 10-unit side chains are found in humans. In a search for the P. falciparum enzyme responsible for the biosynthesis of isoprenic side chains attached to the benzoquinone ring of ubiquinones, we cloned and expressed a putative polyprenyl synthase. Polyclonal antibodies raised against the corresponding recombinant protein confirmed the presence of the native protein in trophozoite and schizont stages of P. falciparum. The recombinant protein, as well as P. falciparum extracts, showed an octaprenyl pyrophosphate synthase activity, with the formation of a polyisoprenoid with eight isoprenic units, as detected by reverse-phase HPLC and reverse-phase TLC, and confirmed by electrospray ionization and tandem MS analysis. The recombinant and native versions of the enzyme had similar Michaelis constants with the substrates isopentenyl pyrophosphate and farnesyl pyrophosphate. The recombinant enzyme could be competitively inhibited in the presence of the terpene nerolidol. This is the first report that directly demonstrates an octaprenyl pyrophosphate synthase activity in parasitic protozoa. Given the rather low similarity of the P. falciparum enzyme to its human counterpart, decaprenyl pyrophosphate synthase, we suggest that the identified enzyme and its recombinant version could be exploited in the screening of novel drugs.
38

White, Mark D., Karl A. P. Payne, Karl Fisher, Stephen A. Marshall, David Parker, Nicholas J. W. Rattray, Drupad K. Trivedi, et al. "UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis." Nature 522, no. 7557 (June 17, 2015): 502–6. http://dx.doi.org/10.1038/nature14559.

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39

Turunen, Mikael, Jeffrey M. Peters, Frank J. Gonzalez, Sophia Schedin та Gustav Dallner. "Influence of peroxisome proliferator-activated receptor α on ubiquinone biosynthesis". Journal of Molecular Biology 297, № 3 (березень 2000): 607–14. http://dx.doi.org/10.1006/jmbi.2000.3596.

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40

Chubiz, Lon M., and Christopher V. Rao. "Aromatic Acid Metabolites of Escherichia coli K-12 Can Induce the marRAB Operon." Journal of Bacteriology 192, no. 18 (July 16, 2010): 4786–89. http://dx.doi.org/10.1128/jb.00371-10.

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ABSTRACT MarR is a key regulator of the marRAB operon involved in antibiotic resistance and solvent stress tolerance in Escherichia coli. We show that two metabolic intermediates, 2,3-dihydroxybenzoate and anthranilate, involved in enterobactin and tryptophan biosynthesis, respectively, can activate marRAB transcription. We also found that a third intermediate involved in ubiquinone biosynthesis, 4-hydroxybenzoate, activates marRAB transcription in the absence of TolC. Of the three, however, only 2,3-dihydroxybenzoate directly binds MarR and affects its activity.
41

Hu, Mei, Yan Jiang, and Jing-Jing Xu. "Characterization of Arabidopsis thaliana Coq9 in the CoQ Biosynthetic Pathway." Metabolites 13, no. 7 (June 30, 2023): 813. http://dx.doi.org/10.3390/metabo13070813.

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Coenzyme Q, also known as ubiquinone, is a fat-soluble isoprene quinone that serves as a cofactor for numerous enzymes across all domains of life. However, the biosynthetic pathway for this important molecule in plants has been examined in only a limited number of studies. In yeast and mammals, Coq9, an isoprenoid-lipid-binding protein, is essential for CoQ biosynthesis. Previous studies showed that Arabidopsis thaliana Coq9 failed to complement the fission yeast Schizosaccharomyces pombe coq9 null mutant, and its function in plants remains unknown. In this study, we demonstrated that expression of Arabidopsis Coq9 rescued the growth of a yeast temperature-sensitive coq9 mutant and increased CoQ content. Phylogenetic analysis revealed that Coq9 is widely present in green plants. Green fluorescent protein (GFP) fusion experiments showed that Arabidopsis Coq9 is targeted to mitochondria. Disruption of the Coq9 gene in Arabidopsis results in lower amounts of CoQ. Our work suggests that plant Coq9 is required for efficient CoQ biosynthesis. These findings provide new insights into the evolution of CoQ biosynthesis in plants. The identification of Coq9 as a key player in CoQ biosynthesis in plants opens up new avenues for understanding the regulation of this important metabolic pathway.
42

Barker, Clive S., Irina V. Meshcheryakova, Toshio Sasaki, Michael C. Roy, Prem Kumar Sinha, Takao Yagi, and Fadel A. Samatey. "Randomly selected suppressor mutations in genes for NADH : quinone oxidoreductase-1, which rescue motility of a Salmonella ubiquinone-biosynthesis mutant strain." Microbiology 160, no. 6 (June 1, 2014): 1075–86. http://dx.doi.org/10.1099/mic.0.075945-0.

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The primary mobile electron-carrier in the aerobic respiratory chain of Salmonella is ubiquinone. Demethylmenaquinone and menaquinone are alternative electron-carriers involved in anaerobic respiration. Ubiquinone biosynthesis was disrupted in strains bearing deletions of the ubiA or ubiE genes. In soft tryptone agar both mutant strains swam poorly. However, the ubiA deletion mutant strain produced suppressor mutant strains with somewhat rescued motility and growth. Six independent suppressor mutants were purified and comparative genome sequence analysis revealed that they each bore a single new missense mutation, which localized to genes for subunits of NADH : quinone oxidoreductase-1. Four mutants bore an identical nuoG(Q297K) mutation, one mutant bore a nuoM(A254S) mutation and one mutant bore a nuoN(A444E) mutation. The NuoG subunit is part of the hydrophilic domain of NADH : quinone oxidoreductase-1 and the NuoM and NuoN subunits are part of the hydrophobic membrane-embedded domain. Respiration was rescued and the suppressed mutant strains grew better in Luria–Bertani broth medium and could use l-malate as a sole carbon source. The quinone pool of the cytoplasmic membrane was characterized by reversed-phase HPLC. Wild-type cells made ubiquinone and menaquinone. Strains with a ubiA deletion mutation made demethylmenaquinone and menaquinone and the ubiE deletion mutant strain made demethylmenaquinone and 2-octaprenyl-6-methoxy-1,4-benzoquinone; the total quinone pool was reduced. Immunoblotting found increased NADH : quinone oxidoreductase-1 levels for ubiquinone-biosynthesis mutant strains and enzyme assays measured electron transfer from NADH to demethylmenaquinone or menaquinone. Under certain growth conditions the suppressor mutations improved electron flow activity of NADH : quinone oxidoreductase-1 for cells bearing a ubiA deletion mutation.
43

Walker, Emma C., Rashmi Ramani, Sarah Javati, Elizabeth Todd, Pallavi Chandra, John-Paul Matlam, Edgar Anaya, William Pomat, and Sharon Celeste Morley. "A novel variant in ubiquinone biosynthesis highly prevalent in Papua New Guinea children increases mortality following bacterial pneumonia." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 231.5. http://dx.doi.org/10.4049/jimmunol.204.supp.231.5.

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Abstract To identify immune variants predisposing to severe pneumonia, we performed whole exome sequencing in a pediatric population highly susceptible to acute lower respiratory infections, identifying a candidate novel variant in the ubiquinone (CoQ10) biosynthetic pathway. To evaluate the effect of this variant on immune function during bacterial pneumonia, we generated a mouse line using CRISPR-Cas9 that expresses the homologous aspartate to tyrosine variant in the enzyme COQ6. Intra-tracheal S. pneumoniae infection leads to increased bacteremia and mortality in mice homozygous for the variant despite similar numbers of immune cells in the lung. Mechanistic studies show that macrophages expressing the variant have decreased mitochondrial activity at the ubiquinone-dependent reduction of cytochrome c by complex III, as well as decreased maximum respiratory capacity in response to acute stimulation. Variant-expressing macrophages also exhibit impaired generation of mitochondrial reactive oxygen species (mROS) causing a direct, intrinsic defect in intracellular killing of internalized bacteria. Thus, the novel variant in CoQ10 biosynthesis leads to changes in macrophage mitochondria and an intrinsic inability to kill internalized bacteria. As alveolar macrophages are the first responders in the lung to bacterial challenge, the inability of these macrophages to mount a sufficient immune response can explain the observed increase in mortality following bacterial pneumonia. Because variants in CoQ10 biosynthesis can be supplemented with CoQ10, a readily available therapy may be able to correct this defect and improve survival in children with this variant
44

Wang, Ying, Pan Chen, Qi Lin, Linzhi Zuo, and Lei Li. "Whole-Genome Sequencing of Two Potentially Allelopathic Strains of Bacillus from the Roots of C. equisetifolia and Identification of Genes Related to Synthesis of Secondary Metabolites." Microorganisms 12, no. 6 (June 20, 2024): 1247. http://dx.doi.org/10.3390/microorganisms12061247.

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The coastal Casuarina equisetifolia is the most common tree species in Hainan’s coastal protection forests. Sequencing the genomes of its allelopathic endophytes can allow the protective effects of these bacteria to be effectively implemented in protected forests. The goal of this study was to sequence the whole genomes of the endophytes Bacillus amyloliquefaciens and Bacillus aryabhattai isolated from C. equisetifolia root tissues. The results showed that the genome sizes of B. amyloliquefaciens and B. aryabhattai were 3.854 Mb and 5.508 Mb, respectively. The two strains shared 2514 common gene families while having 1055 and 2406 distinct gene families, respectively. The two strains had 283 and 298 allelochemical synthesis-associated genes, respectively, 255 of which were shared by both strains and 28 and 43 of which were unique to each strain, respectively. The genes were putatively involved in 11 functional pathways, including secondary metabolite biosynthesis, terpene carbon skeleton biosynthesis, biosynthesis of ubiquinone and other terpene quinones, tropane/piperidine and piperidine alkaloids biosynthesis, and phenylpropanoid biosynthesis. NQO1 and entC are known to be involved in the biosynthesis of ubiquinone and other terpenoid quinones, and rfbC/rmlC, rfbA/rmlA/rffH, and rfbB/rmlB/rffG are involved in the biosynthesis of polyketide glycan units. Among the B. aryabhattai-specific allelochemical synthesis-related genes, STE24 is involved in terpene carbon skeleton production, atzF and gdhA in arginine biosynthesis, and TYR in isoquinoline alkaloid biosynthesis. B. amyloliquefaciens and B. aryabhattai share the genes aspB, yhdR, trpA, trpB, and GGPS, which are known to be involved in the synthesis of carotenoids, indole, momilactones, and other allelochemicals. Additionally, these bacteria are involved in allelochemical synthesis via routes such as polyketide sugar unit biosynthesis and isoquinoline alkaloid biosynthesis. This study sheds light on the genetic basis of allelopathy in Bacillus strains associated with C. equisetifolia, highlighting the possible use of these bacteria in sustainable agricultural strategies for weed management and crop protection.
45

FORSGREN, Margareta, Anneli ATTERSAND, Staffan LAKE, Jacob GRÜNLER, Ewa SWIEZEWSKA, Gustav DALLNER, and Isabel CLIMENT. "Isolation and functional expression of human COQ2, a gene encoding a polyprenyl transferase involved in the synthesis of CoQ." Biochemical Journal 382, no. 2 (August 24, 2004): 519–26. http://dx.doi.org/10.1042/bj20040261.

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The COQ2 gene in Saccharomyces cerevisiae encodes a Coq2 (p-hydroxybenzoate:polyprenyl transferase), which is required in the biosynthetic pathway of CoQ (ubiquinone). This enzyme catalyses the prenylation of p-hydroxybenzoate with an all-trans polyprenyl group. We have isolated cDNA which we believe encodes the human homologue of COQ2 from a human muscle and liver cDNA library. The clone contained an open reading frame of length 1263 bp, which encodes a polypeptide that has sequence homology with the Coq2 homologues in yeast, bacteria and mammals. The human COQ2 gene, when expressed in yeast Coq2 null mutant cells, rescued the growth of this yeast strain in the absence of a non-fermentable carbon source and restored CoQ biosynthesis. However, the rate of CoQ biosynthesis in the rescued cells was lower when compared with that in cells rescued with the yeast COQ2 gene. CoQ formed when cells were incubated with labelled decaprenyl pyrophosphate and nonaprenyl pyrophosphate, showing that the human enzyme is active and that it participates in the biosynthesis of CoQ.
46

DISCH, Andrea, Andréa HEMMERLIN, Thomas J. BACH, and Michel ROHMER. "Mevalonate-derived isopentenyl diphosphate is the biosynthetic precursor of ubiquinone prenyl side chain in tobacco BY-2 cells." Biochemical Journal 331, no. 2 (April 15, 1998): 615–21. http://dx.doi.org/10.1042/bj3310615.

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Study of the incorporation of 13C-labelled glucose or pyruvate into the isoprenoids of tobacco BY-2 cells allowed the biosynthetic origin of isopentenyl diphosphate to be determined. Sterols synthesized in the cytoplasm and the prenyl chain of ubiquinone Q10 located in mitochondria were derived from the same isopentenyl diphosphate pool, synthesized from acetyl-CoA through mevalonate, whereas the prenyl chain of plastoquinone was obtained from the mevalonate-independent glyceraldehyde 3-phosphate/pyruvate route, like all chloroplast isoprenoids from higher plants. These results are in accord with the compartmentation and complete enzymic independence of the biosynthesis of long-chain all-trans polyprenols in mitochondria and chloroplasts.
47

Hekimi, Siegfried, and Bryan Hughes. "Phylogenetic ubiquity of the effects of altered ubiquinone biosynthesis on survival." Aging 3, no. 3 (March 17, 2011): 184–85. http://dx.doi.org/10.18632/aging.100310.

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48

KAWAHARA, Kazuyoshi, Naohisa KOIZUMI, Haruhiko KAWAJI, Kunio OISHI, Kô AIDA, and Kinya UCHIDA. "Partial Purification and Characterization of 4-Hydroxybenzoate-polyprenyltransferase in Ubiquinone Biosynthesis." Agricultural and Biological Chemistry 55, no. 9 (1991): 2307–11. http://dx.doi.org/10.1271/bbb1961.55.2307.

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49

Kang, Dongchon, Toshiyuki Fujiwara, and Koichiro Takeshige. "Ubiquinone Biosynthesis by Mitochondria, Sonicated Mitochondria and Mitoplasts of Rat Liver." Journal of Biochemistry 111, no. 3 (March 1992): 371–75. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a123764.

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50

Barkovich, Robert J., Andrey Shtanko, Jennifer A. Shepherd, Peter T. Lee, David C. Myles, Alexander Tzagoloff, and Catherine F. Clarke. "Characterization of theCOQ5Gene fromSaccharomyces cerevisiaeEVIDENCE FOR AC-METHYLTRANSFERASE IN UBIQUINONE BIOSYNTHESIS." Journal of Biological Chemistry 272, no. 14 (April 4, 1997): 9182–88. http://dx.doi.org/10.1074/jbc.272.14.9182.

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