Relevant bibliographies by topics / Tetrahydrofolate dehydrogenase

Academic literature on the topic 'Tetrahydrofolate dehydrogenase'

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Published: 4 June 2021
Last updated: 12 February 2022

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Journal articles on the topic "Tetrahydrofolate dehydrogenase"

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Invernizzi, R., R. Nano, O. Perugini, P. Fazio, L. Nespoli, G. Gerzeli, and E. Ascari. "Tetrahydrofolate dehydrogenase cytochemistry in acute lymphoblastic leukemia." European Journal of Haematology 41, no. 2 (April 24, 2009): 109–14. http://dx.doi.org/10.1111/j.1600-0609.1988.tb00879.x.

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Brosnan, Margaret E., Garrett Tingley, Luke MacMillan, Brian Harnett, Theerawat Pongnopparat, Jenika D. Marshall, and John T. Brosnan. "Plasma Formate Is Greater in Fetal and Neonatal Rats Compared with Their Mothers." Journal of Nutrition 150, no. 5 (January 7, 2020): 1068–75. http://dx.doi.org/10.1093/jn/nxz329.

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ABSTRACT Background Formate can be incorporated into 10-formyl-tetrahydrofolate (10-formyl-THF), which is a substrate for purine synthesis, and after further reduction of the one-carbon group, may be used as a substrate for thymidylate synthesis and for homocysteine remethylation. Objective We examined plasma formate concentrations and the expression of genes involved in the production and utilization of formate in fetal and neonatal rats and in pregnant and virgin female rats. Methods In 1 experiment, plasma formate was measured by GC-MS in rats aged 1–56 d. In a second experiment, virgin female (adult) rats, 19-d pregnant rats (P) and their male and female fetuses (F), and 3-d-old (N) and 7-d-old (J) offspring had plasma and amniotic fluid analyzed for formate by GC-MS, mRNA abundance in liver and placenta by qPCR, and several plasma amino acids by HPLC. Results The plasma formate concentration was significantly higher in fetuses at embryonic day 19 than in the mothers. It was also significantly higher in neonatal rats but slowly returned to adult concentrations by ∼3 wk. The abundance of mitochondrial monofunctional 10-formyl-tetrahydrofolate synthetase (Mthfd1l) mRNA was significantly higher in placenta (PP) and F liver than in liver of N or J. Expression of mitochondrial bifunctional NAD-dependent methylene-tetrahydrofolate dehydrogenase/methenyl-tetrahydrofolate cyclohydrolase (Mthfd2) was significantly enriched in PP and liver of P, intermediate in F liver, and much lower in liver of N and J, relative to PP. Serine hydroxymethyltransferase 2 (Shmt2), methylenetetrahydrofolate dehydrogenase 1 (Mthfd1), and glycine decarboxylase protein of the glycine cleavage system (Gldc) mRNA expression was significantly lower in PP compared with other groups. Cytoplasmic NAD(P)-dependent 10-formyl-tetrahydrofolate dehydrogenase (Aldh1/1) and mitochondrial NAD(P)-dependent 10-formyl-tetrahydrofolate dehydrogenase (Aldh1/2) , genes responsible for the catabolism of 10-formylTHF, were very weakly expressed in PP, low in livers of F and N, and reached the significantly higher adult levels in J. Serine, glycine, and methionine concentrations in plasma of F were significantly higher than in plasma of P. Conclusions Formate metabolism is highly active in fetuses and in placenta of pregnant rats.
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Krupenko, S. A., C. Wagner, and R. J. Cook. "Recombinant 10-formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate." Biochemical Journal 306, no. 3 (March 15, 1995): 651–55. http://dx.doi.org/10.1042/bj3060651.

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10-Formyltetrahydrofolate dehydrogenase (EC 1.5.1.6) is a bifunctional enzyme, displaying both NADP(+)-dependent dehydrogenase activity for the formation of tetrahydrofolate and CO2, and NADP(+)-independent hydrolase activity for the formation of tetrahydrofolate and formate. A previous report [Case, Kaisaki and Steele (1988) J. Biol. Chem. 263, 1024-1027] claimed that dehydrogenase and hydrolase activities were products of separate cytosolic and mitochondrial forms of this enzyme. Here we report that recombinant 10-formyltetrahydrofolate dehydrogenase carries out both enzymic reactions, proving that a product of a single gene, i.e. one protein, not two, has both activities. The stable synthetic analogue 10-formyl-5,8-dideazafolate can substitute for the labile natural substrate, 10-formyltetrahydrofolate, in both reactions. This was shown with both native and recombinant rat liver enzyme. The Km values for 10-formyl-5,8-dideazafolate were half of those for 10-formyltetrahydrofolate in both the dehydrogenase and hydrolytic reactions. The Vmax, values were similar for both substrates. Both dehydrogenase and hydrolase reactions were dependent on the presence of 2-mercaptoethanol. The pH optima were 7.8 and 5.6 for the dehydrogenase and hydrolase reactions respectively, consistent with the presence of two active sites in the enzyme.
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Hattori, Satoshi, Alexander S. Galushko, Yoichi Kamagata, and Bernhard Schink. "Operation of the CO Dehydrogenase/Acetyl Coenzyme A Pathway in both Acetate Oxidation and Acetate Formation by the Syntrophically Acetate-Oxidizing Bacterium Thermacetogenium phaeum." Journal of Bacteriology 187, no. 10 (May 15, 2005): 3471–76. http://dx.doi.org/10.1128/jb.187.10.3471-3476.2005.

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ABSTRACT Thermacetogenium phaeum is a homoacetogenic bacterium that can grow on various substrates, such as pyruvate, methanol, or H2/CO2. It can also grow on acetate if cocultured with the hydrogen-consuming methanogenic partner Methanothermobacter thermautotrophicus. Enzyme activities of the CO dehydrogenase/acetyl coenzyme A (CoA) pathway (CO dehydrogenase, formate dehydrogenase, formyl tetrahydrofolate synthase, methylene tetrahydrofolate dehydrogenase) were detected in cell extracts of pure cultures and of syntrophic cocultures. Mixed cell suspensions of T. phaeum and M. thermautotrophicus oxidized acetate rapidly and produced acetate after addition of H2/CO2 after a short time lag. CO dehydrogenase activity staining after native polyacrylamide gel electrophoresis exhibited three oxygen-labile bands which were identical in pure culture and coculture. Protein profiles of T. phaeum cells after sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that the strain exhibited basically the same protein patterns in both pure and syntrophic culture. These results indicate that T. phaeum operates the CO dehydrogenase/acetyl-CoA pathway reversibly both in acetate oxidation and in reductive acetogenesis by using the same biochemical apparatus, although it has to couple this pathway to ATP synthesis in different ways.
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Vorholt, Julia A., Marina G. Kalyuzhnaya, Christoph H. Hagemeier, Mary E. Lidstrom, and Ludmila Chistoserdova. "MtdC, a Novel Class of Methylene Tetrahydromethanopterin Dehydrogenases." Journal of Bacteriology 187, no. 17 (September 1, 2005): 6069–74. http://dx.doi.org/10.1128/jb.187.17.6069-6074.2005.

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ABSTRACT Novel methylene tetrahydromethanopterin (H4MPT) dehydrogenase enzymes, named MtdC, were purified after expressing in Escherichia coli genes from, respectively, Gemmata sp. strain Wa1-1 and environmental DNA originating from unidentified microbial species. The MtdC enzymes were shown to possess high affinities for methylene-H4MPT and NADP but low affinities for methylene tetrahydrofolate or NAD. The substrate range and the kinetic properties revealed by MtdC enzymes distinguish them from the previously characterized bacterial methylene-H4MPT dehydrogenases, MtdA and MtdB. While revealing higher sequence similarity to MtdA enzymes, MtdC enzymes appear to fulfill a function homologous to the function of MtdB, as part of the H4MPT-linked pathway for formaldehyde oxidation/detoxification.
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Vorholt, Julia A., Ludmila Chistoserdova, Mary E. Lidstrom, and Rudolf K. Thauer. "The NADP-Dependent Methylene Tetrahydromethanopterin Dehydrogenase in Methylobacterium extorquens AM1." Journal of Bacteriology 180, no. 20 (October 15, 1998): 5351–56. http://dx.doi.org/10.1128/jb.180.20.5351-5356.1998.

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ABSTRACT An NADP-dependent methylene tetrahydromethanopterin (H4MPT) dehydrogenase has recently been proposed to be involved in formaldehyde oxidation to CO2 inMethylobacterium extorquens AM1. We report here on the purification of this novel enzyme to apparent homogeneity. Via the N-terminal amino acid sequence, it was identified to be themtdA gene product. The purified enzyme catalyzed the dehydrogenation of methylene H4MPT with NADP+rather than with NAD+, with a specific activity of approximately 400 U/mg of protein. It also catalyzed the dehydrogenation of methylene tetrahydrofolate (methylene H4F) with NADP+. With methylene H4F as the substrate, however, the specific activity (26 U/mg) and the catalytic efficiency (V max/Km ) were approximately 20-fold lower than with methylene H4MPT. Whereas the dehydrogenation of methylene H4MPT (E0 = −390 mV) with NADP+ (E0 = −320 mV) proceeded essentially irreversibly, the dehydrogenation of methylene H4F (E0 = −300 mV) was fully reversible. Comparison of the primary structure of the NADP-dependent dehydrogenase fromM. extorquens AM1 with those of methylene H4F dehydrogenases from other bacteria and eucarya and with those of methylene H4MPT dehydrogenases from methanogenic archaea revealed only marginally significant similarity (<15%).
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Dimri, G. P., G. F. Ames, L. D'Ari, and J. C. Rabinowitz. "Physical map location of the Escherichia coli gene encoding the bifunctional enzyme 5,10-methylene-tetrahydrofolate dehydrogenase/5,10-methenyl-tetrahydrofolate cyclohydrolase." Journal of Bacteriology 173, no. 17 (1991): 5251. http://dx.doi.org/10.1128/jb.173.17.5251-.1991.

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Dimri, G. P., G. F. Ames, L. D'Ari, and J. C. Rabinowitz. "Physical map location of the Escherichia coli gene encoding the bifunctional enzyme 5,10-methylene-tetrahydrofolate dehydrogenase/5,10-methenyl-tetrahydrofolate cyclohydrolase.:." Journal of Bacteriology 173, no. 17 (September 1991): 5251. http://dx.doi.org/10.1128/jb.173.17.5251.1991.

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Wilquet, Valérie, Mark Van de Casteele, Daniel Gigot, Christianne Legrain, and Nicolas Glansdorff. "Dihydropteridine Reductase as an Alternative to Dihydrofolate Reductase for Synthesis of Tetrahydrofolate in Thermus thermophilus." Journal of Bacteriology 186, no. 2 (January 15, 2004): 351–55. http://dx.doi.org/10.1128/jb.186.2.351-355.2004.

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ABSTRACT A strategy devised to isolate a gene coding for a dihydrofolate reductase from Thermus thermophilus DNA delivered only clones harboring instead a gene (the T. thermophilus dehydrogenase [DH Tt ] gene) coding for a dihydropteridine reductase which displays considerable dihydrofolate reductase activity (about 20% of the activity detected with 6,7-dimethyl-7,8-dihydropterine in the quinonoid form as a substrate). DH Tt appears to account for the synthesis of tetrahydrofolate in this bacterium, since a classical dihydrofolate reductase gene could not be found in the recently determined genome nucleotide sequence (A. Henne, personal communication). The derived amino acid sequence displays most of the highly conserved cofactor and active-site residues present in enzymes of the short-chain dehydrogenase/reductase family. The enzyme has no pteridine-independent oxidoreductase activity, in contrast to Escherichia coli dihydropteridine reductase, and thus appears more similar to mammalian dihydropteridine reductases, which do not contain a flavin prosthetic group. We suggest that bifunctional dihydropteridine reductases may be responsible for the synthesis of tetrahydrofolate in other bacteria, as well as archaea, that have been reported to lack a classical dihydrofolate reductase but for which possible substitutes have not yet been identified.
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Wang, Hongchao, Qizai Wang, Chen Zhang, Haiqin Chen, Wenwei Lu, Zhennan Gu, Jianxin Zhao, Hao Zhang, Yong Q. Chen, and Wei Chen. "The role of MTHFDL in mediating intracellular lipogenesis in oleaginous Mortierella alpina." Microbiology 166, no. 7 (July 1, 2020): 617–23. http://dx.doi.org/10.1099/mic.0.000897.

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The oleaginous fungus Mortierella alpina can synthesize a variety of polyunsaturated fatty acids, which are used extensively in industry for the production of arachidonic acid (AA). NADPH is the limiting factor and critical reducing agent in lipid biosynthesis. In the folate cycle, methylenetetrahydrofolate dehydrogenase (MTHFDL) catalyzes the conversion of methylene tetrahydrofolate into 10-formyl-tetrahydrofolate with the reduction of NADP+ to NADPH. MTHFDL RNAi was used to investigate the role of the folate cycle in lipogenesis. Gene knockdown decreased the transcript levels of MTHFDL by about 50 % and attenuated cell fatty acid synthesis. The observation of decreased NADPH levels and downregulated NADPH-producing genes in response to MTHFDL RNAi indicates a novel aspect of the NADPH regulatory mechanism. Thus, our study demonstrates that MTHFDL plays key role in the mediation of NADPH in lipogenesis in M. alpina.
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Dissertations / Theses on the topic "Tetrahydrofolate dehydrogenase"

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Hastings, Michele Dawn. "Analysis of dihydrofolate reductase variations in relation to antifolate resistance in Plasmodium vivax /." Thesis, Connect to this title online; UW restricted, 2004. http://hdl.handle.net/1773/10269.

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Gelling, Cristy Lee Biotechnology &amp Biomolecular Sciences Faculty of Science UNSW. "Tetrahydrofolate and iron-sulfur metabolism in Saccharomyces cerevisiae." Publisher:University of New South Wales. Biotechnology & Biomolecular Sciences, 2008. http://handle.unsw.edu.au/1959.4/43270.

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Tetrahydrofolate-mediated one-carbon metabolism is required for the biosynthesis of many central metabolites, including some amino acids, nucleobases, and nucleotides, and hence dysfunction of one-carbon metabolism is associated with many human diseases and disorders. The mitochondrial glycine decarboxylase complex (GDC) is an important component of one-carbon metabolism, generating 5,10-methylene-tetrahydrofolate (5,10-CH2-H??4folate) from glycine. Previous work has shown that the genes encoding the unique sub-units of the Saccharomyces cerevisiae GDC (GCV1, GCV2 and GCV3) are regulated in response to changes in the levels of cytosolic 5,10-CH2-H??4folate (Piper et al., 2000). Given the centrality of 5,10-CH2-H??4folate to many aspects of metabolism, it was hypothesised that other genes may be regulated by the same mechanism. Using microarray analysis of S. cerevisiae under a number of conditions that affect 5,10-CH2-H??4folate levels, the ??one-carbon regulon??, a group of genes that were co-regulated with the GCV genes was identified. The one-carbon regulon corresponds closely to genes whose promoters are bound by the purine biosynthesis regulator Bas1p, but not all one-carbon regulon members are significantly purine regulated. Genetic approaches demonstrated that the one-carbon unit response and the purine response are distinct, though both depend on the presence of Bas1p. This demonstrated that the close metabolic connections of one-carbon and purine metabolism are reflected in over-lapping, but separable regulatory mechanisms. The identity of the sensor of one-carbon unit depletion remains unknown, but in the course of investigation of the candidate regulator Caf17p, it was demonstrated that Caf17p is in fact involved in Fe/S cluster protein maturation. Examination of the effects of Caf17p depletion revealed that Caf17p is required for the function and maturation of the related mitochondrial Fe/S proteins aconitase and homoaconitase, as well as the function of, but not de novo iron incorporation into, the mitochondrial radical-SAM Fe/S protein biotin synthase. Because other Fe/S proteins were unaffected, Caf17p appears to be a specialised Fe/S maturation factor. The presence of a putative H4folate binding site indicates that Caf17p may constitute a metabolic link between one-carbon and iron metabolism.
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Wooden, Jason. "Analysis of resistance to inhibitors of Plasmodium falciparum dihydrofolate reductase in yeast /." Thesis, Connect to this title online; UW restricted, 1996. http://hdl.handle.net/1773/10261.

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Tu, Yongxue. "Etude physicochimique et biochimique des dihydrofolates reductases et de l'effet antifolate des thiosemicarbazones." Paris 7, 1988. http://www.theses.fr/1988PA077164.

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Hankins, Eleanor Gray. "Drug resistance in Plasmodium falciparum : the role of point mutations in dihydropteroate synthase and dihydrofolate reductase analyzed in a yeast model /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/10290.

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Brophy, Victoria Hertle. "Study of the Cryptosporidium parvum DHFR-TS in the model system Saccharomyces cerevisiae /." Thesis, Connect to this title online; UW restricted, 1998. http://hdl.handle.net/1773/10262.

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Ulmer, Jonathan Edward. "Analysis and studies of inhibition of the two divergent thymidine biosynthesis pathways in Mycobacterium tuberculosis /." Thesis, Connect to this title online; UW restricted, 2007. http://hdl.handle.net/1773/10297.

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Mousseau, Mireille. "Étude des mécanismes moléculaires de chimiorésistance intrinsèque des tumeurs cérébrales humaines." Grenoble 1, 1992. http://www.theses.fr/1992GRE10186.

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La chimiothérapie a une faible efficacité sur les tumeurs cérébrales humaines (taux de réponse objective allant de 13 a 33%). Nous avons étudié les mécanismes moléculaires de chimiorésistance intrinsèque sur une série de 66 tumeurs cérébrales humaines comportant 31 gliomes (1 gangliogliome grade 1, 9 astrocytomes grade 2 et 10 grade 3, 11 gliomes grade 4), 18 méningiomes, 12 métastases cérébrales (de 2 cancers bronchiques épidermoïdes; de 8 adénocarcinomes du sein (3 cas), du poumon (2 cas), d'origine indéterminée (2 cas) et du colon (1 cas); d'1 sarcome d'Ewing; d'1 cancer bronchique peu différencié), 1 médulloblastome, 1 tératome malin, 3 épendymomes. L'analyse en southern blot de l'ADN de 33 tumeurs cérébrales humaines, hybride avec la sonde de la résistance pléiotropique (MDR1) ne montre jamais d'amplification de ce gène. Cette résistance pléiotropique et les 3 autres mécanismes principaux de chimiorésistance ont été étudiés par la technique du northern blot avec les sondes de la résistance pléiotropique (MDR1), de la glutathion-s-transférase (GSTPIL), de la dihydrofolate réductase (DHFR) et de la topoisomérase 2 (topo 2). Le principal résultat de ce travail est la non-expression du gène de la topoisomérase 2 dans le tissu cérébral humain normal (100%) et dans 75% (44/59) des échantillons tumoraux. Le deuxième gène, GSTPI, est surexprimé dans 23% (12/53) des tumeurs cérébrales (6/32 des tumeurs cérébrales primitives, 3/10 métastases, 3/11 des méningiomes). Les deux autres gènes lies a la chimiorésistance sont trouvés exceptionnellement surexprimés 2% pour MDR1 (1 gliome grade 4 sur 61 tumeurs), 8% pour DHFR (4/49: 2 gliomes grade 2,3; 1 métastase; 1 méningiome). Nos résultats suggèrent qu'il existe une chimiorésistance intrinsèque dans les tumeurs cérébrales humaines; elle est associée à 2 mécanismes majeurs de résistance (topo 2, GSTPI) en cause avec les drogues utilisées dans le traitement de ces tumeurs.
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Shan, Yujie. "Sequence requirements of early firing origin activity in the dihydrofolate reductase locus of Chinese hamster ovary cells /." 2000. http://wwwlib.umi.com/dissertations/fullcit/9987171.

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Kaisaki, Pamela Jane. "Characterization of the expression of 10-formyl tetrahydrofolate dehydrogenase in altered physiological states." 1993. http://catalog.hathitrust.org/api/volumes/oclc/30117417.html.

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Book chapters on the topic "Tetrahydrofolate dehydrogenase"

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"Stereochemistry of Hydride Transfer to NADP+ by Methylene Tetrahydrofolate Dehydrogenase from Pig Liver." In Montreal, Canada, June 15–20, 1986, 901–4. De Gruyter, 1986. http://dx.doi.org/10.1515/9783110856262-169.

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