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Journal articles on the topic 'Methyl transferase'

Author: Grafiati

Published: 4 June 2021

Last updated: 31 January 2023

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1

Farid, Anila, Beenish Haider, Kehkashan Akbar, Ammar Mehfooz, Ziyad Ahmad, Fazal E. Raheem, Furqan Arshad, et al. "Homology Modeling of Predicted Methyl Transferases (STY 3264): A Protein of Salmonella TYPHI CT18." Pakistan Journal of Medical and Health Sciences 16, no. 3 (March 26, 2022): 720–22. http://dx.doi.org/10.53350/pjmhs22163720.

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Background: Salmonella typhi gives rise to typhoid fever which is life threatening illness.It puts end to approximately 600,000 people per annum around the world.Food and water are the leading components through which this disease is passed on and becomes origin of typhoid.It lays out widely where cleanliness is very substandard. Objective: To construct 3 dimensional structure of protein Methyl Transferase of Salmonella typhi CT18 by homology modeling. Materials and Methods: Bioinformatic tools and programs like Comprehensive Microbial Resource (CMR), Interproscan, Basic Local Alignment Search Tool (BLAST), Modellor 9.10, Procheck and Prosa were helpful for the complete homology modeling of methyl transferases (STY 3264).The models were visualized by DS Viever. Results: Homology modeling is an effective method to find structure of methyl transferase protein for future discovery of drugs. Conclusion: Homology modeling is an effective method to find structure of protein which provides good solution for drug discovery. Keywords: Methyl transferase ,Homology modeling, Typhoid fever,Salmonella typhi CT18.

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2

Ibrahim, Ragal K. "Plant O-methyl-transferase signatures." Trends in Plant Science 2, no. 7 (July 1997): 249–50. http://dx.doi.org/10.1016/s1360-1385(97)86345-5.

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3

Spencer, S. R., L. A. Xue, E. M. Klenz, and P. Talalay. "The potency of inducers of NAD(P)H:(quinone-acceptor) oxidoreductase parallels their efficiency as substrates for glutathione transferases. Structural and electronic correlations." Biochemical Journal 273, no. 3 (February 1, 1991): 711–17. http://dx.doi.org/10.1042/bj2730711.

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Induction of glutathione transferases (EC. 2.5.1.18), NAD(P)H:(quinone-acceptor) oxidoreductase (EC 1.6.99.2; quinone reductase) and other detoxification enzymes is a major mechanism for protecting cells against the toxicities of electrophiles, including many carcinogens. Although inducers of these two enzymes belong to many different chemical classes, they nevertheless contain (or acquire by metabolism) electrophilic centres that appear to be essential for inclusive activity, and many inducers are Michael reaction acceptors [Talalay, De Long & Prochaska (1988) Proc. Natl. Acad. Sci. U.S.A., 85, 8261-8265]. The inducers therefore share structural and electronic features with glutathione transferase substrates. To define these features more precisely, we examined the inductive potencies (by measuring quinone reductase in murine hepatoma cells) of two types of glutathione transferase substrates: a series of 1-chloro-2-nitrobenzenes bearing para-oriented electron-donating or -withdrawing substituents and a wide variety of other commonly used and structurally unrelated glutathione transferase substrates. We conclude that virtually all glutathione transferase substrates are inducers, and their potencies in the nitrobenzene series correlate linearly with the Hammett sigma or sigma- values of the aromatic substituents, precisely as previously reported for their efficiencies as glutathione transferase substrates. More detailed information on the electronic requirements for inductive activity was obtained with a series of methyl trans-cinnamates bearing electron-withdrawing or -donating substituents on the aromatic ring, and in which the electronic densities at the olefinic and adjacent carbon atoms were measured by 13C n.m.r. Electron-withdrawing meta-substituents markedly enhance inductive potency in parallel with their increased non-enzymic reactivity with GSH. Thus, methyl 3-bromo-, 3-nitro- and 3-chloro-cinnamates are 21, 14 and 8 times more potent inducers than the parent methyl cinnamate. This finding permits the design of more potent inducers, which are important for elucidation of the molecular mechanisms of induction.

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4

Nes, W. "Sterol methyl transferase: enzymology and inhibition." Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1529, no. 1-3 (December 15, 2000): 63–88. http://dx.doi.org/10.1016/s1388-1981(00)00138-4.

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5

Futó, J., J. E. Cannon, M. R. Fahey, C. F. Seals, J. P. Kupferberg, R. D. Miller, and J. Moss. "VECURONIUM INHIBITS HISTAMINE N-METHYL TRANSFERASE." Anesthesia & Analgesia 67, Supplement (February 1988): 67. http://dx.doi.org/10.1213/00000539-198802001-00067.

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6

SUGUMARAN, Geetha, Maya KATSMAN, and E. Jeremiah SILBERT. "Subcellular co-localization and potential interaction of glucuronosyltransferases with nascent proteochondroitin sulphate at Golgi sites of chondroitin synthesis." Biochemical Journal 329, no. 1 (January 1, 1998): 203–8. http://dx.doi.org/10.1042/bj3290203.

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Microsomal membranes from chick embryo epiphyseal cartilage were fractionated by equilibrium sucrose-density-gradient centrifugation and assayed for GlcA (glucuronic acid) transferase I (the enzyme that transfers GlcA from UDP-GlcA to Gal-Gal-Xyl of proteochondroitin linkage region), for comparison with GlcA transferase II (the GlcA transferase of chondroitin polymerization). Gal(β1-3)Galβ1-methyl (disaccharide) and GalNAc(β1-4)GlcA(β1-3)GalNAc(β1-4)GlcA(β1-3)GalNAc (pentasaccharide) were used respectively as acceptors of [14C]GlcA from UDP-[14C]GlcA. Distributions of the two GlcA transferase activities in the sucrose-density-gradient fractions were compared with each other and with the previously reported distribution of the activities of Gal transferases (UDP-Gal to ovalbumin, and to xylose of the proteochondroitin linkage region) and GalNAc (N-acetylgalactosamine) transferase II of chondroitin polymerization. The linkage-region GlcA transferase I had a dual Golgi distribution similar to that of chondroitin-polymerizing GlcA transferase II and distinctly different from the distribution of linkage-region Gal transferases I and II, which were found exclusively in the heavier fractions. Solubilized GlcA transferase I was partly purified by sequential use of Q-Sepharose, heparin-Sepharose and wheatgerm agglutinin-agarose and was accompanied at each step by some of the GlcA transferase II activity. Both GlcA transferase I and II bound to the Q-Sepharose as though they were highly anionic. However, treatment with chondroitin ABC lyase eliminated the binding while markedly decreasing enzyme stability. The enzyme activities could not be reconstituted by adding chondroitin or chondroitin pentasaccharide to the chondroitin ABC lyase-treated enzymes. Incubation of the partly purified enzymes with both UDP-GlcA and UDP-GalNAc resulted in a 40-fold greater incorporation than with just one sugar nucleotide, indicating the presence of bound, nascent proteochondroitin serving as the acceptor for chondroitin polymerization. These results, together with the membrane co-localization, indicate that GlcA transferase I and GlcA transferase II occur closely together with nascent proteochondroitin at the site of synthesis and that this complex with the nascent proteochondroitin stabilizes both enzymes during purification.

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7

Pacifici, GM, P. Donatelli, and L. Giuliani. "Histamine N-methyl transferase: inhibition by drugs." British Journal of Clinical Pharmacology 34, no. 4 (October 1992): 322–27. http://dx.doi.org/10.1111/j.1365-2125.1992.tb05637.x.

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8

Bruce, C., and W. H. Taylor. "Fluoride - An Activator of Histamine Methyl Transferase." Clinical Science 93, s37 (August 1, 1997): 17P. http://dx.doi.org/10.1042/cs093017p.

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9

Acuna-Johnson, Adriana P., Allan C. Oehlschlager, Aldona M. Pierce, Harold D. Pierce, and Eva K. Czyzewska. "Stereochemistry of yeast Δ24-sterol methyl transferase." Bioorganic & Medicinal Chemistry 5, no. 5 (May 1997): 821–32. http://dx.doi.org/10.1016/s0968-0896(97)00010-2.

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10

Pitt, James J., Nicholas Tzanakos, and Thanh Nguyen. "Newborn screening for guanidinoacetate methyl transferase deficiency." Molecular Genetics and Metabolism 111, no. 3 (March 2014): 303–4. http://dx.doi.org/10.1016/j.ymgme.2014.01.005.

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11

Casimiri, Viviane, Wayne R. Cohen, Simone Parvez, Calvin Hobel, and Hasan Parvez. "Phenylethanolamine-N-methyl transferase and catechol-O-methyl transferase activity in rat uterus: Cyclic and steroid-induced changes." Acta Obstetricia et Gynecologica Scandinavica 72, no. 8 (January 1993): 606–10. http://dx.doi.org/10.3109/00016349309021151.

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12

Leutwein, Christina, and Johann Heider. "Succinyl-CoA:(R)-Benzylsuccinate CoA-Transferase: an Enzyme of the Anaerobic Toluene Catabolic Pathway in Denitrifying Bacteria." Journal of Bacteriology 183, no. 14 (July 15, 2001): 4288–95. http://dx.doi.org/10.1128/jb.183.14.4288-4295.2001.

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ABSTRACT Anaerobic microbial toluene catabolism is initiated by addition of fumarate to the methyl group of toluene, yielding (R)-benzylsuccinate as first intermediate, which is further metabolized via β-oxidation to benzoyl-coenzyme A (CoA) and succinyl-CoA. A specific succinyl-CoA:(R)-benzylsuccinate CoA-transferase activating (R)-benzylsuccinate to the CoA-thioester was purified and characterized from Thauera aromatica. The enzyme is fully reversible and forms exclusively the 2-(R)-benzylsuccinyl-CoA isomer. Only some close chemical analogs of the substrates are accepted by the enzyme: succinate was partially replaced by maleate or methylsuccinate, and (R)-benzylsuccinate was replaced by methylsuccinate, benzylmalonate, or phenylsuccinate. In contrast to all other known CoA-transferases, the enzyme consists of two subunits of similar amino acid sequences and similar sizes (44 and 45 kDa) in an α2β2 conformation. Identity of the subunits with the products of the previously identified toluene-inducedbbsEF genes was confirmed by determination of the exact masses via electrospray-mass spectrometry. The deduced amino acid sequences resemble those of only two other characterized CoA-transferases, oxalyl-CoA:formate CoA-transferase and (E)-cinnamoyl-CoA:(R)-phenyllactate CoA-transferase, which represent a new family of CoA-transferases. As suggested by kinetic analysis, the reaction mechanism of enzymes of this family apparently involves formation of a ternary complex between the enzyme and the two substrates.

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13

Vandel, Laurence, and Didier Trouche. "Physical association between the histone acetyl transferase CBP and a histone methyl transferase." EMBO reports 2, no. 1 (January 2001): 21–26. http://dx.doi.org/10.1093/embo-reports/kve002.

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14

Dey, Joydeb. "Structure based functional annotation of a MYND-less lysine methyl transferase in Candida albicans." Bioinformation 18, no. 12 (December 31, 2022): 1146–53. http://dx.doi.org/10.6026/973206300181146.

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Candida albicans is opportunistic pathogenic yeast that is widely distributed throughout the world and is classified as the most critical fungal pathogen group. Candida albicans is a common microbiota of healthy individuals but can cause superficial and invasive infections in immune compromised individuals. Protein Post-translational modifications involving methylation of lysine amino acids stand for a major regulator of eukaryotic transcription, and pathways controlling several cellular processes. SMYD makes up a SET (Su (Var) 3–9, Enhancer-of-zeste and Trithorax) and MYND (Myeloid, Nervy, and DEAF-1) domain containing lysine methyl transferase subfamily that transfers methyl groups from methyl donors onto lysine residues in histones (H3 and H4) and non-histone proteins. The SET domain is the methyl transferase catalytic domain, while MYND participates in both protein and DNA interactions. Well-studied examples of SMYD proteins are five human and two Saccharomyces cerevisiae, constituting examples of histone and non-histone protein lysine methyl transferase members. However, there is limited understanding of SET lysine methyltransferases, including the SMYD subfamily, in the pathogenic fungi Candida albicans. Using bioinformatics tools, we characterized the SMYD domain containing proteins in the important pathogen. We report the presence of an atypical SMYD member (CaO19.3863) as a new lysine methyltransferase that can be a target for antifungal therapy.

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15

Piechulla, Birgit, Nancy Magnus, Marie Chantal Lemfack, and Stephan von Reuss. "Terpenoid Cyclization by SAM-Dependent C-Methyl Transferase." Trends in Chemistry 2, no. 6 (June 2020): 585–86. http://dx.doi.org/10.1016/j.trechm.2020.01.006.

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16

Ferenz, Hans-Jörg, Martin G. Peter, and Dieter Berg. "Inhibition of Farnesoic Acid Methyl transferase by Sinefungin." Agricultural and Biological Chemistry 50, no. 4 (April 1986): 1003–8. http://dx.doi.org/10.1080/00021369.1986.10867495.

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17

Jiménez, Elvia Mera, Teresa Żołek, Paola Gabriela Hernández Perez, Rene Miranda Ruvalcaba, María Inés Nicolás-Vázquez, and Maricarmen Hernández-Rodríguez. "Drug Repurposing to Inhibit Histamine N-Methyl Transferase." Molecules 28, no. 2 (January 6, 2023): 576. http://dx.doi.org/10.3390/molecules28020576.

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Lower activity of the histaminergic system is associated with neurological disorders, including Alzheimer’s disease (AD). Thus, the enhancement of histaminergic neurotransmission by inhibition of histamine N-methyl transferase (HNMT), which degrades histamine, appears as an important approach. For this purpose, rigid and flexible molecular docking studies of 185 FDA-approved drugs with the HNMT enzyme were carried out to select two compounds to perform molecular dynamics (MD) simulations to evaluate the binding free energies and stability of the enzyme–drug complexes. Finally, an HNMT inhibition assay was performed to corroborate their effect towards HNMT. Molecular docking studies with HNMT allowed the selection of dihydroergotamine and vilazodone since these molecules showed the lowest Gibbs free energy values. Analysis of the binding mode of vilazodone showed interactions with the binding pocket of HNMT with Glu28, Gln143, and Asn283. In contrast, dihydroergotamine binds to the HNMT active site in a different location, apparently because it is overall the more rigid ligand compared to flexible vilazodone. HNMT inhibitory activity for dihydroergotamine and vilazodone was corroborated (IC50 = 72.89 μM and 45.01 μM, respectively) by in vitro assays. Drug repurposing of HNMT was achieved by employing computational studies.

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18

Bakker, Walbert J., Montserrat Blázquez-Domingo, Andrea Kolbus, Janey Besooyen, Peter Steinlein, Hartmut Beug, Paul J. Coffer, Bob Löwenberg, Marieke von Lindern, and Thamar B. van Dijk. "FoxO3a regulates erythroid differentiation and induces BTG1, an activator of protein arginine methyl transferase 1." Journal of Cell Biology 164, no. 2 (January 19, 2004): 175–84. http://dx.doi.org/10.1083/jcb.200307056.

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Erythropoiesis requires tight control of expansion, maturation, and survival of erythroid progenitors. Because activation of phosphatidylinositol-3-kinase (PI3K) is required for erythropoietin/stem cell factor–induced expansion of erythroid progenitors, we examined the role of the PI3K-controlled Forkhead box, class O (FoxO) subfamily of Forkhead transcription factors. FoxO3a expression and nuclear accumulation increased during erythroid differentiation, whereas untimely induction of FoxO3a activity accelerated differentiation of erythroid progenitors to erythrocytes. We identified B cell translocation gene 1 (BTG1)/antiproliferative protein 2 as a FoxO3a target gene in erythroid progenitors. Promoter studies indicated BTG1 as a direct target of FoxO3a. Expression of BTG1 in primary mouse bone marrow cells blocked the outgrowth of erythroid colonies, which required a domain of BTG1 that binds protein arginine methyl transferase 1. During erythroid differentiation, increased arginine methylation coincided with BTG1 expression. Concordantly, inhibition of methyl transferase activity blocked erythroid maturation without affecting expansion of progenitor cells. We propose FoxO3a-controlled expression of BTG1 and subsequent regulation of protein arginine methyl transferase activity as a novel mechanism controlling erythroid expansion and differentiation.

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19

Kaschabek, Stefan R., Bernd Kuhn, Dagmar Müller, Eberhard Schmidt, and Walter Reineke. "Degradation of Aromatics and Chloroaromatics by Pseudomonas sp. Strain B13: Purification and Characterization of 3-Oxoadipate:Succinyl-Coenzyme A (CoA) Transferase and 3-Oxoadipyl-CoA Thiolase." Journal of Bacteriology 184, no. 1 (January 1, 2002): 207–15. http://dx.doi.org/10.1128/jb.184.1.207-215.2002.

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ABSTRACT The degradation of 3-oxoadipate in Pseudomonas sp. strain B13 was investigated and was shown to proceed through 3-oxoadipyl-coenzyme A (CoA) to give acetyl-CoA and succinyl-CoA. 3-Oxoadipate:succinyl-CoA transferase of strain B13 was purified by heat treatment and chromatography on phenyl-Sepharose, Mono-Q, and Superose 6 gels. Estimation of the native molecular mass gave a value of 115,000 ± 5,000 Da with a Superose 12 column. Polyacrylamide gel electrophoresis under denaturing conditions resulted in two distinct bands of equal intensities. The subunit A and B values were 32,900 and 27,000 Da. Therefore it can be assumed that the enzyme is a heterotetramer of the type A2B2 with a molecular mass of 120,000 Da. The N-terminal amino acid sequences of both subunits are as follows: subunit A, AELLTLREAVERFVNDGTVALEGFTHLIPT; subunit B, SAYSTNEMMTVAAARRLKNGAVVFV. The pH optimum was 8.4. K m values were 0.4 and 0.2 mM for 3-oxoadipate and succinyl-CoA, respectively. Reversibility of the reaction with succinate was shown. The transferase of strain B13 failed to convert 2-chloro- and 2-methyl-3-oxoadipate. Some activity was observed with 4-methyl-3-oxoadipate. Even 2-oxoadipate and 3-oxoglutarate were shown to function as poor substrates of the transferase. 3-Oxoadipyl-CoA thiolase was purified by chromatography on DEAE-Sepharose, blue 3GA, and reactive brown-agarose. Estimation of the native molecular mass gave 162,000 ± 5,000 Da with a Superose 6 column. The molecular mass of the subunit of the denatured protein, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, was 42 kDa. On the basis of these results, 3-oxoadipyl-CoA thiolase should be a tetramer of the type A4. The N-terminal amino acid sequence of 3-oxoadipyl-CoA thiolase was determined to be SREVYI-DAVRTPIGRFG. The pH optimum was 7.8. K m values were 0.15 and 0.01 mM for 3-oxoadipyl-CoA and CoA, respectively. Sequence analysis of the thiolase terminus revealed high percentages of identity (70 to 85%) with thiolases of different functions. The N termini of the transferase subunits showed about 30 to 35% identical amino acids with the glutaconate-CoA transferase of an anaerobic bacterium but only an identity of 25% with the respective transferases of aromatic compound-degrading organisms was found.

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20

Saygili, E. Ilker, Tulay Akcay, Yildiz Dinçer, Can Öbek, Ali Riza Kural, and Cansel Çakalir. "Methylguanine DNA Methyl Transferase Activities, Glutathione S Transferase and Nitric Oxide in Bladder Cancer Patients." Cancer Investigation 24, no. 3 (January 2006): 256–60. http://dx.doi.org/10.1080/07357900600634120.

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21

Söderström, M., S. Hammarström, and B. Mannervik. "Leukotriene C synthase in mouse mastocytoma cells. An enzyme distinct from cytosolic and microsomal glutathione transferases." Biochemical Journal 250, no. 3 (March 15, 1988): 713–18. http://dx.doi.org/10.1042/bj2500713.

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Leukotriene C4 synthesis was studied in preparations from mouse mastocytoma cells. Enzymic conjugation of leukotriene A4 with glutathione was catalysed by both the cytosol and the microsomal fraction. The specific activity of the microsomal fraction (7.8 nmol/min per mg of protein) was 17 times that of the cytosol fraction. The cytosol fraction of the mastocytoma cells contained two glutathione transferases, which were purified to homogeneity and characterized. A microsomal glutathione transferase was purified from mouse liver; this enzyme was shown by immunoblot analysis to be present in the mastocytoma microsomal fraction at a concentration one-tenth or less of that in the liver microsomal fraction. Both the cytosolic and the microsomal glutathione transferases in the mastocytoma cells were identified with enzymes previously characterized, by determining specific activities with various substrates, sensitivities to inhibitors, reactions with antibodies, and physical properties. The purified microsomal glutathione transferase from liver was inactive with leukotriene A4 or its methyl ester as substrate. The cytosolic enzymes displayed activity with leukotriene A4, but their specific activities and intracellular concentrations were too low to account for the leukotriene C4 formation in the mastocytoma cells. The microsomal fraction of the cells contained an enzyme distinguishable by various criteria from the previously studied glutathione transferases. This membrane-bound enzyme, leukotriene C synthase (leukotriene A4:glutathione S-leukotrienyltransferase), appears to carry the main responsibility for the biosynthesis of leukotriene C4.

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22

Zai, Clement C., Arun K. Tiwari, Daniel J. Müller, Vincenzo de Luca, Takahiro Shinkai, Sajid Shaikh, Xingqun Ni, et al. "The catechol-O-methyl-transferase gene in tardive dyskinesia." World Journal of Biological Psychiatry 11, no. 6 (June 29, 2010): 803–12. http://dx.doi.org/10.3109/15622975.2010.486043.

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23

García-Martín, Elena, Carmen Martínez, Mercedes Serrador, Hortensia Alonso-Navarro, Francisco Navacerrada, José A. G. Agúndez, and Félix Javier Jiménez-Jiménez. "Histamine-N-Methyl Transferase Polymorphism and Risk for Migraine." Headache: The Journal of Head and Face Pain 48, no. 9 (October 2008): 1343–48. http://dx.doi.org/10.1111/j.1526-4610.2007.01056.x.

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24

Bertocci, B., G. Garotta, G. Zürcher, V. Miggiano, and M. Da Prada. "Immunoaffinity purification of pig liver catechol-O-methyl transferase." Pharmacological Research Communications 20 (September 1988): 39. http://dx.doi.org/10.1016/s0031-6989(88)80169-3.

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25

Matsumoto, Naomichi. "Cerebral gigantism with histone methyl transferase abnormality: Sotos syndrome." Neuroscience Research 58 (January 2007): S7. http://dx.doi.org/10.1016/j.neures.2007.06.036.

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26

Gao, Canhong, Juncheng Lin, Liangxia Zhao, Fule Xu, and Shuiming Zhang. "Homocysteine S-methyl transferase regulates sulforaphane concentration inBrassica oleraceavar.italica." Indian Journal of Genetics and Plant Breeding (The) 75, no. 3 (2015): 357. http://dx.doi.org/10.5958/0975-6906.2015.00056.5.

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27

Benkhalifa, M., P. C. Bacrie, M. Dumont, A. M. Junca, S. Belloc, and Y. Menezo. "Imprinting in the human oocyte: homocysteine recycling to methionine through methyltetrahydrofolate homocysteine methyl transferase (MTR) and betaine homocysteine methyl transferase (BHMT 2)." Fertility and Sterility 90 (September 2008): S328. http://dx.doi.org/10.1016/j.fertnstert.2008.07.1658.

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28

Mcintyre, CL, AL Rae, MD Curtis, and JM Manners. "Sequence and Expression of a Caffeic Acid O-Methyl Transferase Cdna Homologue in the Tropical Forage Legume Stylosanthes Humilis." Functional Plant Biology 22, no. 3 (1995): 471. http://dx.doi.org/10.1071/pp9950471.

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The isolation and characterisation of a cDNA encoding a caffeic acid 0-methyl transferase cDNA homologue (COMT) from Stylosanthes humilis are described. The clone is 1391 nucleotides in length, with an open reading frame encoding a predicted protein of 366 amino acids. Cluster analysis of the deduced amino acid sequence revealed extensive homology to other published O-methyl transferase sequences. Maximum levels of homology were seen with COMTs from alfalfa (87%) and aspen (84%). Southern analysis suggested that this enzyme is encoded by two genes in S. humilis. The mRNA is most strongly expressed in stem tissue, with intermediate levels of expression in young leaves and roots, and does not appear to be induced upon fungal infection or wounding.

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29

Dinçer, Yıldız, Tülay Akçay, Nilgün Çelebi, İlhami Uslu, Özlem Özmen, and Hüsrev Hatemi. "Glutathione S-Transferase and O6-Methylguanine DNA Methyl Transferase Activities in Patients with Thyroid Papillary Carcinoma." Cancer Investigation 20, no. 7-8 (January 2002): 965–71. http://dx.doi.org/10.1081/cnv-120005912.

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30

Shaffi, SheikhMohd, and MohdAmin Shah. "Promoter hypermethylation of methyl guanine methyl transferase in lung cancer patients of Kashmir valley." International Journal of Medicine and Public Health 3, no. 2 (2013): 89. http://dx.doi.org/10.4103/2230-8598.115161.

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31

Rosic, Gvozden, Zorica Lazic, Suzana Pantovic, and Mirko Rosic. "Phenylethylamine effects on histamine-induced contraction of isolated guinea-pig trachea rings." Jugoslovenska medicinska biohemija 24, no. 2 (2005): 95–97. http://dx.doi.org/10.2298/jmh0502095r.

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Histamine produces constriction of tracheal smooth muscle via H1 receptors, but it also decreases tracheal smooth muscle tone via H2 and H3 receptors. In addition, it has already been reported that phenylethylamine is competitive antagonist of histamine N-methyl-transferase (HMT), enzyme responsible for rapid inactivation of histamine. Our results suggest possibility that phenylethylamine as competitive antagonist of histamine N-methyl-transferase leads to potentiation of histamine induced constriction of isolated guinea-pig trachea, which could be consequence of decreased histamine methylation and subsequent histamine inactivation. At the same time, phenylethylamine had no direct effect on basal tone of intact isolated trachea rings, as well as on other mechanisms leading to increased responsiveness of guinea-pig tracheal smooth muscle (acetylcholine, KCl, electro stimulation).

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32

Lee, E., P. G. Tardi, R. Y. K. Man, and P. C. Choy. "The modulation of phosphatidylinositol biosynthesis in hamster hearts by methyl lidocaine." Biochemical Journal 309, no. 3 (August 1, 1995): 871–76. http://dx.doi.org/10.1042/bj3090871.

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Methyl lidocaine is an experimental anti-arrhythmic drug which has been shown to enhance the biosynthesis of phosphatidyl-inositol (PI) in the hamster heart. In this study, the effect of methyl lidocaine on enzymes involved in the biosynthesis of PI in the heart was examined. When the hamster heart was perfused with labelled methyl lidocaine, the majority of the compound was not metabolized after perfusion. The direct action of methyl lidocaine on an enzyme was studied by the presence of the drug in enzyme assays, whereas its indirect action was studied by assaying the enzyme activity in the heart after methyl lidocaine perfusion. CTP:phosphatidic acid cytidylyl-transferase, a rate-limiting enzyme in PI biosynthesis, was stimulated by methyl lidocaine in a direct manner. Kinetic studies revealed that methyl lidocaine caused a change in the affinity between the enzyme and phosphatidic acid and resulted in the enhancement of the reaction. Alternatively, acyl-CoA:lysophosphatidic acid acyltransferase, another key enzyme for PI biosynthesis, was not activated by the presence of methyl lidocaine. However, the enzyme activity was stimulated in hearts perfused with methyl lidocaine. The enhancement of the acyl-transferase by methyl lidocaine perfusion was found to be mediated via the adenylate cyclase cascade with the elevation of the cyclic AMP level. The stimulation of protein kinase A activity by cyclic AMP resulted in the phosphorylation and activation of the acyltransferase. Interestingly, the activity of protein kinase C was not stimulated by methyl lidocaine perfusion. We conclude that the enhancement of PI biosynthesis by methyl lidocaine in the hamster heart resulted from the direct activation of the cytidylyltransferase, as well as the phosphorylation and subsequent activation of the acyltransferase.

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33

Barra, Lise, Catherine Fontenelle, Gwennola Ermel, Annie Trautwetter, Graham C. Walker, and Carlos Blanco. "Interrelations between Glycine Betaine Catabolism and Methionine Biosynthesis in Sinorhizobium meliloti Strain 102F34." Journal of Bacteriology 188, no. 20 (October 1, 2006): 7195–204. http://dx.doi.org/10.1128/jb.00208-06.

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ABSTRACT Methionine is produced by methylation of homocysteine. Sinorhizobium meliloti 102F34 possesses only one methionine synthase, which catalyzes the transfer of a methyl group from methyl tetrahydrofolate to homocysteine. This vitamin B12-dependent enzyme is encoded by the metH gene. Glycine betaine can also serve as an alternative methyl donor for homocysteine. This reaction is catalyzed by betaine-homocysteine methyl transferase (BHMT), an enzyme that has been characterized in humans and rats. An S. meliloti gene whose product is related to the human BHMT enzyme has been identified and named bmt. This enzyme is closely related to mammalian BHMTs but has no homology with previously described bacterial betaine methyl transferases. Glycine betaine inhibits the growth of an S. meliloti bmt mutant in low- and high-osmotic strength media, an effect that correlates with a decrease in the catabolism of glycine betaine. This inhibition was not observed with other betaines, like homobetaine, dimethylsulfoniopropionate, and trigonelline. The addition of methionine to the growth medium allowed a bmt mutant to recover growth despite the presence of glycine betaine. Methionine also stimulated glycine betaine catabolism in a bmt strain, suggesting the existence of another catabolic pathway. Inactivation of metH or bmt did not affect the nodulation efficiency of the mutants in the 102F34 strain background. Nevertheless, a metH strain was severely defective in competing with the wild-type strain in a coinoculation experiment.

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34

M.P. O’Tuathaigh, Colm, Lieve Desbonnet, Peter Lee, and John L. Waddington. "Catechol-O-Methyl Transferase as a Drug Target for Schizophrenia." CNS & Neurological Disorders - Drug Targets 11, no. 3 (May 1, 2012): 282–91. http://dx.doi.org/10.2174/187152712800672418.

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35

Kalkeri, Raj, Govinda Bhisetti, and Nagraj Mani. "Human respiratory syncytial virus methyl transferase: a potential antiviral target?" F1000Research 8 (May 29, 2019): 750. http://dx.doi.org/10.12688/f1000research.18800.1.

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Human respiratory syncytial virus (HRSV) causes bronchiolitis and pneumonia. The role of methyltransferase (MTase) activity of HRSV polymerase in viral replication is unknown. Literature reviews of similar viral MTases and homology- modeling of RSV MTase bound to GTP and S-adenosylmethionine (SAM) have shown sequence similarity and the conserved catalytic residues (K-D-K-E) and the SAM-binding (GXGXG) domain. Combined with the recent reports of the importance of 2’O methylation of viral RNAs in the host innate immune response evasion, and its proposed role in viral replication, HRSV MTase holds promise as a potential antiviral target. Further biological validation of HRSV MTase could facilitate the discovery of novel HRSV antivirals targeting MTase enzyme activity.

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36

Kalkeri, Raj, Govinda Bhisetti, and Nagraj Mani. "Human respiratory syncytial virus methyl transferase: a potential antiviral target?" F1000Research 8 (September 23, 2019): 750. http://dx.doi.org/10.12688/f1000research.18800.2.

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Abstract:

Human respiratory syncytial virus (HRSV) causes bronchiolitis and pneumonia. The role of methyltransferase (MTase) activity of HRSV polymerase in viral replication is unknown. Literature reviews of similar viral MTases and homology- modeling of RSV MTase bound to GTP and S-adenosylmethionine (SAM) have shown sequence similarity and the conserved catalytic residues (K-D-K-E) and the SAM-binding (GXGXG) domain. Combined with the recent reports of the importance of 2’O methylation of viral RNAs in the host innate immune response evasion, and its proposed role in viral replication, HRSV MTase holds promise as a potential antiviral target. Further biological validation of HRSV MTase could facilitate the discovery of novel HRSV antivirals targeting MTase enzyme activity.

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37

Vaquero, Alejandro, Michael Scher, Hediye Erdjument-Bromage, Paul Tempst, Lourdes Serrano, and Danny Reinberg. "SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation." Nature 450, no. 7168 (November 2007): 440–44. http://dx.doi.org/10.1038/nature06268.

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38

Barnea, E., N. MacLusky, A. DeCherney, and F. Naftolin. "Catechol-O-Methyl Transferase Activity in the Human Term Placenta." American Journal of Perinatology 5, no. 02 (April 1988): 121–27. http://dx.doi.org/10.1055/s-2007-999669.

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39

García-Martín, E., C. Martínez, J. Benito-León, P. Calleja, M. Díaz-Sánchez, D. Pisa, H. Alonso-Navarro, et al. "Histamine-N-methyl transferase polymorphism and risk for multiple sclerosis." European Journal of Neurology 17, no. 2 (June 15, 2009): 335–38. http://dx.doi.org/10.1111/j.1468-1331.2009.02720.x.

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40

Ross, S. B., and Ö. Haljasmaa. "Catechol-O-Methyl Transferase Inhibitors. In Vivo Inhibition in Mice." Acta Pharmacologica et Toxicologica 21, no. 3 (March 13, 2009): 215–25. http://dx.doi.org/10.1111/j.1600-0773.1964.tb01786.x.

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41

Moskovitz, Jackob, Consuelo Walss-Bass, Dianne A. Cruz, Peter M. Thompson, and Marco Bortolato. "Methionine sulfoxide reductase regulates brain catechol-O-methyl transferase activity." International Journal of Neuropsychopharmacology 17, no. 10 (April 15, 2014): 1707–13. http://dx.doi.org/10.1017/s1461145714000467.

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42

Tomkova, Jana, David Friedecky, Adriana Polynkova, and Tomas Adam. "Capillary electrophoresis determination of thiopurine methyl transferase activity in erythrocytes." Journal of Chromatography B 877, no. 20-21 (July 2009): 1943–45. http://dx.doi.org/10.1016/j.jchromb.2009.05.005.

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43

Connaughton, John F., Philip G. Vanek, Shih-Queen Lee-Lin, and Jack G. Chirikjian. "Cloning of the BamHI methyl transferase gene from Bacillus amyloliquefaciens." Gene Analysis Techniques 5, no. 6 (November 1988): 116–24. http://dx.doi.org/10.1016/0735-0651(88)90011-8.

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44

Vetter, Roland, Jian Dai, Nasrin Masaeli, Vincenzo Panagia, and Naranjan S. Dhalla. "Role of sulfhydryl groups in heart sarcolemma phospholipid methyl-transferase." Journal of Molecular and Cellular Cardiology 22 (May 1990): S116. http://dx.doi.org/10.1016/0022-2828(90)91871-4.

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45

Zhou, Wenxu, Thi Thuy Minh Nguyen, Margaret S. Collins, Melanie T. Cushion, and W. David Nes. "Evidence for multiple sterol methyl transferase pathways in Pneumocystis carinii." Lipids 37, no. 12 (December 2002): 1177–86. http://dx.doi.org/10.1007/s11745-002-1018-8.

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Radulovic, Louis L., John J. LaFerla, and Arun P. Kulkarni. "Human placental glutathione S-transferase-mediated metabolism of methyl parathion." Biochemical Pharmacology 35, no. 20 (October 1986): 3473–80. http://dx.doi.org/10.1016/0006-2952(86)90614-3.

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47

Ni, X., and L. P. Hager. "Expression of Batis maritima methyl chloride transferase in Escherichia coli." Proceedings of the National Academy of Sciences 96, no. 7 (March 30, 1999): 3611–15. http://dx.doi.org/10.1073/pnas.96.7.3611.

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48

Wuosmaa, A., and L. Hager. "Methyl chloride transferase: a carbocation route for biosynthesis of halometabolites." Science 249, no. 4965 (July 13, 1990): 160–62. http://dx.doi.org/10.1126/science.2371563.

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Ari, Ferda, and Egemen Dere. "Glutathione S-transferase activity in rats exposed to methyl parathion." Chemistry and Ecology 24, no. 3 (June 2008): 213–19. http://dx.doi.org/10.1080/02757540802119889.

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50

Warthan, Michelle D., Jessica G. Freeman, Kathryn E. Loesser, Carolene W. Lewis, Min Hong, Carolyn M. Conway, and Jennifer K. Stewart. "Phenylethanolamine N-Methyl Transferase Expression in Mouse Thymus and Spleen." Brain, Behavior, and Immunity 16, no. 4 (August 2002): 493–99. http://dx.doi.org/10.1006/brbi.2001.0637.

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