Relevant bibliographies by topics / Transferases

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Academic literature on the topic 'Transferases'

Author: Grafiati
Published: 4 June 2021
Last updated: 25 May 2024

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Journal articles on the topic "Transferases"

1

Alin, P., H. Jensson, E. Cederlund, H. Jörnvall, and B. Mannervik. "Cytosolic glutathione transferases from rat liver. Primary structure of class alpha glutathione transferase 8-8 and characterization of low-abundance class Mu glutathione transferases." Biochemical Journal 261, no. 2 (July 15, 1989): 531–39. http://dx.doi.org/10.1042/bj2610531.

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Six GSH transferases with neutral/acidic isoelectric points were purified from the cytosol fraction of rat liver. Four transferases are class Mu enzymes related to the previously characterized GSH transferases 3-3, 4-4 and 6-6, as judged by structural and enzymic properties. Two additional GSH transferases are distinguished by high specific activities with 4-hydroxyalk-2-enals, toxic products of lipid peroxidation. The most abundant of these two enzymes, GSH transferase 8-8, a class Alpha enzyme, has earlier been identified in rat lung and kidney. The amino acid sequence of subunit 8 was determined and showed a typical class Alpha GSH transferase structure including an N-acetylated N-terminal methionine residue.
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Stockman, P. K., G. J. Beckett, and J. D. Hayes. "Identification of a basic hybrid glutathione S-transferase from human liver. Glutathione S-transferase δ is composed of two distinct subunits (B1 and B2)." Biochemical Journal 227, no. 2 (April 15, 1985): 457–65. http://dx.doi.org/10.1042/bj2270457.

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The purification of a hybrid glutathione S-transferase (B1 B2) from human liver is described. This enzyme has an isoelectric point of 8.75 and the B1 and B2 subunits are distinguishable immunologically and are ionically distinct. Hybridization experiments demonstrated that B1 B1 and B2 B2 could be resolved by CM-cellulose chromatography and have pI values of 8.9 and 8.4 respectively. Transferase B1 B2, and the two homodimers from which it is formed, are electrophoretically and immunochemically distinct from the neutral enzyme (transferase mu) and two acidic enzymes (transferases rho and lambda). Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis demonstrated that B1 and B2 both have an Mr of 26 000, whereas, in contrast, transferase mu comprises subunits of Mr 27 000 and transferases rho and lambda both comprise subunits of Mr 24 500. Antisera raised against B1 or B2 monomers did not cross-react with the neutral or acidic glutathione S-transferases. The identity of transferase B1 B2 with glutathione S-transferase delta prepared by the method of Kamisaka, Habig, Ketley, Arias & Jakoby [(1975) Eur. J. Biochem. 60, 153-161] has been demonstrated, as well as its relationship to other previously described transferases.
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Meyer, D. J., E. Lalor, B. Coles, A. Kispert, P. Ålin, B. Mannervik, and B. Ketterer. "Single-step purification and h.p.l.c. analysis of glutathione transferase 8–8 in rat tissues." Biochemical Journal 260, no. 3 (June 15, 1989): 785–88. http://dx.doi.org/10.1042/bj2600785.

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GSSG selectively elutes two GSH transferases from a mixture of rat GSH transferases bound to a GSH-agarose affinity matrix. One is a form of GSH transferase 1-1 and the other is shown to be GSH transferase 8-8. By using tissues that lack this form of GSH transferase 1-1 (e.g. lung), GSH transferase 8-8 may thus be purified from cytosol in a single step. Quantitative analysis of the tissue distribution of GSH transferase 8-8 was obtained by h.p.l.c.
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Yamamoto, Miyako, Emili Cid, and Fumiichiro Yamamoto. "ABO blood group A transferases catalyze the biosynthesis of FORS blood group FORS1 antigen upon deletion of exon 3 or 4." Blood Advances 1, no. 27 (December 20, 2017): 2756–66. http://dx.doi.org/10.1182/bloodadvances.2017009795.

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Key PointsABO blood group A transferases possess intrinsic FS activity upon deletion of exon 3 or 4 of A transferase messenger RNAs. Cointroduction of exon 3 or 4 deletion and GlyGlyAla substitution synergistically confers human A transferases with strong FS activity.
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Tan, K. H., D. J. Meyer, N. Gillies, and B. Ketterer. "Detoxification of DNA hydroperoxide by glutathione transferases and the purification and characterization of glutathione transferases of the rat liver nucleus." Biochemical Journal 254, no. 3 (September 15, 1988): 841–45. http://dx.doi.org/10.1042/bj2540841.

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DNA peroxidized by exposure to ionizing radiation in the presence of oxygen is a substrate for the Se-independent GSH peroxidase activity of several GSH transferases, GSH transferases 5-5, 3-3 and 4-4 being the most active in the rat liver soluble supernatant fraction (500, 35 and 20 nmol/min per mg of protein respectively) and GSH transferases mu and pi the most active, so far found, in the human liver soluble supernatant fraction (80 and 10 nmol/min per mg respectively). Although the GSH transferase content of the rat nucleus was found to be much lower than that of the soluble supernatant, nuclear GSH transferases are likely to be more important in the detoxification of DNA hydroperoxide produced in vivo. Two nuclear fractions were studied, one extracted with 0.075 M-saline/0.025 M-EDTA, pH 8.0, and the other extracted from the residue with 8.5 M-urea. The saline/EDTA fraction contained subunits 1, 2, 3, 4 and a novel subunit, similar but not identical to 5, provisionally referred to as 5*, in the proportions 40:25:5:5:25 respectively. The 8.5 M-urea-extracted fraction contained principally subunit 5* together with a small amount of subunit 6 in the proportion 95:5 respectively. GSH transferase 5*-5* purified from the 8.5 M-urea extract has the highest activity towards DNA hydroperoxide of any GSH transferase so far studied (1.5 mumol/min per mg). A Se-dependent GSH peroxidase fraction from rat liver was also active towards DNA hydroperoxide; however, since this enzyme accounts for only 14% of the GSH peroxidase activity detectable in the nucleus, GSH transferases may be the more important source of this activity. The possible role of GSH transferases, in particular GSH transferase 5*-5*, in DNA repair is discussed.
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Peters, W. H. M., H. M. J. Roelofs, F. M. Nagengast, and J. H. M. van Tongeren. "Human intestinal glutathione S-transferases." Biochemical Journal 257, no. 2 (January 15, 1989): 471–76. http://dx.doi.org/10.1042/bj2570471.

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Cytosolic glutathione S-transferases were purified from the epithelial cells of human small and large intestine. These preparations were characterized with regard to specific activities, subunit and isoenzyme composition. Isoenzyme composition and specific activity showed little variation from proximal to distal small intestine. Specific activities of hepatic and intestinal enzymes from the same patient were comparable. Hepatic enzymes were mainly composed of 25 kDa subunits. Transferases from small intestine contained 24 and 25 kDa subunits, in variable amounts. Colon enzymes were composed of 24 kDa subunits. In most preparations, however, minor amounts of 27 and 27.5 kDa subunits were detectable. Separation into isoforms by isoelectric focusing revealed striking differences: glutathione S-transferases from liver were mainly basic or neutral, enzymes from small intestine were basic, neutral and acidic, whereas large intestine contained acidic isoforms only. The intestinal acidic transferase most probably was identical with glutathione S-transferase Pi, isolated from human placenta. In the hepatic preparation, this isoform was hardly detectable. The specific activity of glutathione S-transferase showed a sharp fall from small to large intestine. In proximal and distal colon, activity seemed to be about equal. In the ascending colon there might be a relationship between specific activity of glutathione S-transferases and age of the patient, activity decreasing with increasing age.
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Danielson, U. H., H. Esterbauer, and B. Mannervik. "Structure-activity relationships of 4-hydroxyalkenals in the conjugation catalysed by mammalian glutathione transferases." Biochemical Journal 247, no. 3 (November 1, 1987): 707–13. http://dx.doi.org/10.1042/bj2470707.

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The substrate specificities of 15 cytosolic glutathione transferases from rat, mouse and man have been explored by use of a homologous series of 4-hydroxyalkenals, extending from 4-hydroxypentenal to 4-hydroxypentadecenal. Rat glutathione transferase 8-8 is exceptionally active with the whole range of 4-hydroxyalkenals, from C5 to C15. Rat transferase 1-1, although more than 10-fold less efficient than transferase 8-8, is the second most active transferase with the longest chain length substrates. Other enzyme forms showing high activities with these substrates are rat transferase 4-4 and human transferase mu. The specificity constants, kcat./Km, for the various enzymes have been determined with the 4-hydroxyalkenals. From these constants the incremental Gibbs free energy of binding to the enzyme has been calculated for the homologous substrates. The enzymes responded differently to changes in the length of the hydrocarbon side chain and could be divided into three groups. All glutathione transferases displayed increased binding energy in response to increased hydrophobicity of the substrate. For some of the enzymes, steric limitations of the active site appear to counteract the increase in binding strength afforded by increased chain length of the substrate. Comparison of the activities with 4-hydroxyalkenals and other activated alkenes provides information about the active-site properties of certain glutathione transferases. The results show that the ensemble of glutathione transferases in a given species may serve an important physiological role in the conjugation of the whole range of 4-hydroxyalkenals. In view of its high catalytic efficiency with all the homologues, rat glutathione transferase 8-8 appears to have evolved specifically to serve in the detoxication of these reactive compounds of oxidative metabolism.
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Kurz, M. A., T. D. Boyer, R. Whalen, T. E. Peterson, and D. G. Harrison. "Nitroglycerin metabolism in vascular tissue: role of glutathione S-transferases and relationship between NO. and NO2– formation." Biochemical Journal 292, no. 2 (June 1, 1993): 545–50. http://dx.doi.org/10.1042/bj2920545.

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Nitroglycerin is a commonly employed pharmacological agent which produces vasodilatation by release of nitric oxide (NO.). The mechanism by which nitroglycerin releases NO. remains undefined. Recently, glutathione S-transferases have been implicated as important contributors to this process. They are known to release NO2- from nitroglycerin, but have not been shown to release NO.. The present studies were designed to examine the role of endogenous glutathione S-transferases in this metabolic process. Homogenates of dog carotid artery were incubated anaerobically with nitroglycerin, and NO. and NO2- production was determined by chemiluminescence. The role of glutathione S-transferases was studied by incubating homogenates with nitroglycerin in the presence of 1 mM GSH or 1 mM S-hexyl-glutathione, a potent inhibitor of glutathione S-transferases. Homogenates released 163 pmol of NO./h per mg of protein from nitroglycerin, and 2370 pmol of NO2-/h per mg. Adding GSH decreased NO. production by 82% and increased NO2- production by 98%. S-Hexylglutathione inhibited glutathione S-transferase activity by 96% and decreased NO2- production by 78%, but had no effect on NO. release. A linear relationship between glutathione S-transferase activity and NO2- production was observed, whereas glutathione S-transferase activity and NO. release were unrelated. Western-blot analysis demonstrated that dog carotid vascular smooth muscle contained Pi and Mu forms of glutathione S-transferases, with a predominance of the former. Purified preparations of human Pi and rat Mu isoforms metabolized nitroglycerin only to NO2- and not to NO.. On the basis of these findings, we conclude that (1) glutathione S-transferases do not contribute to the bioconversion of nitroglycerin to NO., but instead act as a degradative pathway for nitroglycerin, and (2) the release of NO. from nitroglycerin is not dependent on the formation of NO2-.
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Wang, Qiang-Qiang, Kai He, Muhammad-Tahir Aleem, and Shaojun Long. "Prenyl Transferases Regulate Secretory Protein Sorting and Parasite Morphology in Toxoplasma gondii." International Journal of Molecular Sciences 24, no. 8 (April 12, 2023): 7172. http://dx.doi.org/10.3390/ijms24087172.

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Protein prenylation is an important protein modification that is responsible for diverse physiological activities in eukaryotic cells. This modification is generally catalyzed by three types of prenyl transferases, which include farnesyl transferase (FT), geranylgeranyl transferase (GGT-1) and Rab geranylgeranyl transferase (GGT-2). Studies in malaria parasites showed that these parasites contain prenylated proteins, which are proposed to play multiple functions in parasites. However, the prenyl transferases have not been functionally characterized in parasites of subphylum Apicomplexa. Here, we functionally dissected functions of three of the prenyl transferases in the Apicomplexa model organism Toxoplasma gondii (T. gondii) using a plant auxin-inducible degron system. The homologous genes of the beta subunit of FT, GGT-1 and GGT-2 were endogenously tagged with AID at the C-terminus in the TIR1 parental line using a CRISPR-Cas9 approach. Upon depletion of these prenyl transferases, GGT-1 and GGT-2 had a strong defect on parasite replication. Fluorescent assay using diverse protein markers showed that the protein markers ROP5 and GRA7 were diffused in the parasites depleted with GGT-1 and GGT-2, while the mitochondrion was strongly affected in parasites depleted with GGT-1. Importantly, depletion of GGT-2 caused the stronger defect to the sorting of rhoptry protein and the parasite morphology. Furthermore, parasite motility was observed to be affected in parasites depleted with GGT-2. Taken together, this study functionally characterized the prenyl transferases, which contributed to an overall understanding of protein prenylation in T. gondii and potentially in other related parasites.
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Charrier, Cédric, Gary J. Duncan, Martin D. Reid, Garry J. Rucklidge, Donna Henderson, Pauline Young, Valerie J. Russell, Rustam I. Aminov, Harry J. Flint, and Petra Louis. "A novel class of CoA-transferase involved in short-chain fatty acid metabolism in butyrate-producing human colonic bacteria." Microbiology 152, no. 1 (January 1, 2006): 179–85. http://dx.doi.org/10.1099/mic.0.28412-0.

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Bacterial butyryl-CoA CoA-transferase activity plays a key role in butyrate formation in the human colon, but the enzyme and corresponding gene responsible for this activity have not previously been identified. A novel CoA-transferase gene is described from the colonic bacterium Roseburia sp. A2-183, with similarity to acetyl-CoA hydrolase as well as 4-hydroxybutyrate CoA-transferase sequences. The gene product, overexpressed in an Escherichia coli lysate, showed activity with butyryl-CoA and to a lesser degree propionyl-CoA in the presence of acetate. Butyrate, propionate, isobutyrate and valerate competed with acetate as the co-substrate. Despite the sequence similarity to 4-hydroxybutyrate CoA-transferases, 4-hydroxybutyrate did not compete with acetate as the co-substrate. Thus the CoA-transferase preferentially uses butyryl-CoA as substrate. Similar genes were identified in other butyrate-producing human gut bacteria from clostridial clusters IV and XIVa, while other candidate CoA-transferases for butyrate formation could not be detected in Roseburia sp. A2-183. This suggests strongly that the newly identified group of CoA-transferases described here plays a key role in butyrate formation in the human colon.
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Dissertations / Theses on the topic "Transferases"

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Corrigall, Anne Vint. "Human glutathione S-transferases : characterization, tissue distribution and kinetic studies." Doctoral thesis, University of Cape Town, 1988. http://hdl.handle.net/11427/27205.

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In this study the purification of human basic and near-neutral liver, and human basic and acidic lung glutathione S-transferases (GSH S-T) was undertaken. Purification of the basic and near-neutral GSH S-T was achieved using a combination of affinity chromatography, chromatofocusing and immunoaffinity chromatography. Affinity and ion exchange chromatography were employed in the purification of the basic and acidic lung forms. The purified proteins had similar physicochemical characteristics to the GSH S-T purified by others. The binding of 1-chloro-2,4-dinitrobenzene (CDNB) to the 3 classes of human GSH S-T, viz. basic, near-neutral and acidic and the effects of such binding, if any, were examined. Human acidic lung GSH S-T is irreversibly inactivated by CDNB in the absence of the co-substrate glutathione (GSH). The time-dependent inactivation is pseudo-first order and demonstrates saturation kinetics, suggesting that inactivation occurs from an EI complex. GSH protects the enzyme against CDNB inactivation. In contrast, the basic and near-neutral GSH S-T are not significantly inactivated by CDNB. Incubation with [¹⁴C]-CDNB indicated covalent binding to all 3 classes of GSH S-T. When the basic and acidic GSH S-T were incubated with [¹⁴C]-CDNB and GSH, cleaved with cyanogen bromide, and chromatographed by HPLC, a single peptide fraction was found to be labelled in both classes. Incubation in the absence of GSH yielded 1 and 2 additional labelled peptide fractions for the basic and acidic transferases, respectively. These results suggest that while CDNB arylates all 3 classes of human GSH S-T, only the acidic GSH S-T possesses a specific GSH-sensitive CDNB binding site, which when occupied leads to time-dependent inactivation of the enzyme. The tissue distribution and localization of the 3 classes of human GSH S-T in normal and tumour tissue was examined. Antibodies to representatives of the 3 classes were raised in rabbits, and radial immunodiffusion employed to quantitate their concentrations in the cytosol of 18 organs from 9 individuals. The data provide the first direct, quantitative evidence for the inter-individual and inter-organ variation suggested by earlier workers. The absence of the near-neutral GSH S-T in 5 of the 9 individuals studied confirms an earlier suggestion of a "null" allele for this transferase. Basic and acidic GSH S-T (apart from in a single liver), were always present. Near-neutral GSH S-T, when present, were found in all tissues examined. The marked inter-organ and inter-individual variation observed in this study may explain individual and organ susceptibility to drugs, toxins and carcinogens. The immunohistochemical localization of the 3 classes of GSH S-T reveals important differences in their localization, and may provide insight into their functions in various organs and tissues.
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Goold, Richard David. "The glutathione S-transferases : kinetics, binding and inhibition." Doctoral thesis, University of Cape Town, 1989. http://hdl.handle.net/11427/27175.

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The glutathione S-transferases are a group of enzymes which catalyse the conjugation of reduced glutathione with a variety of electrophilic molecules, and they are therefore thought to play a major role in drug biotransformation and the detoxification of xenobiotics. The cytosolic GSH S-transferase isoenzymes of rat, man and mouse have been assigned to three groups, Alpha, Mu and Pi, based on N-terrninal amino acid sequences, substrate specificities, immunological cross-reactivity and sensitivities to inhibitors. The kinetic mechanism of the GSH S-transferases is controversial, due to the observation of non-Michaelian (non-hyperbolic) substrate-rate saturation curves. The most detailed investigations of the steady-state kinetics of glutathione S-transferase have been performed with isoenzyme 3-3 (class Mu) and the substrate 1,2-dichloro-4-nitrobenzene (DCNB). Explanations for the apparently anomalous non-hyperbolic kinetics have included subunit cooperativity, steady-state mechanisms of differing degrees of complexity and the superimposition of either product inhibition or enzyme memory on these mechanisms. This study has confirmed the biphasic kinetics for isoenzyme 3-3 with DCNB and shown non-hyperbolic kinetics for this isoenzyme with 1-chloro-2,4-dinitrobenzene (CDNB) and for isoenzyme 3-4 with DCNB and CDNB. It is proposed that the basic steady-state random sequential Bi Bi mechanism is the simplest mechanism sufficient to explain the non-hyperbolic kinetics of GSH S-transferases 3-3 and 3-4 under initial rate conditions. Neither more complex steady-state mechanisms nor the superimposition of product inhibition or enzyme memory on the simplest steady-state mechanism are necessary.
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Mosi, Renée M. "Mechanistic studies on Ã-glycosyl transferases." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp02/NQ34594.pdf.

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Dixon, David Peter. "Glutathione transferases in maize (Zea mays)." Thesis, Durham University, 1998. http://etheses.dur.ac.uk/4788/.

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The glutathione transferases (GSTs) of maize have been the most studied GSTs in plants, however much is still not known about these enzymes. In the course of the current study six GST subunits (Zm GSTs I, II and III, which have been reported previously, and Zm GSTs V, VI and VII, which have not been previously reported) have been identified in the dimers Zm GST I-I, I-II, I-III, V-V, V-VI and V-VII. Maize GSTs are known to be important in herbicide detoxification and the purified maize enzymes were each found to have differing activities toward a number of herbicides, and also a range of other potential GST substrates. Additionally, Zm GST I II and Zm GST V-V possessed glutathione peroxidase activity. The developmental regulation and chemical inducibility of maize GSTs were studied in maize seedlings using western blotting, with different subunits showing markedly different responses. Zm GST I was constitutively present in all plant parts and unaffected by chemical treatment, Zm GST II was only detected in young roots but was induced in roots and shoots by many different chemical treatments, and Zm GST V was present at low levels throughout maize plants, with levels enhanced greatly by treatment with the safener dichlormid but not by other chemicals tested. cDNA clones corresponding to Zm GST subunits I, III, V, VI and VII were isolated by library screening using antibody or DNA probes. The cDNA sequences for Zm GST subunits V, VI and VH were different from those of previously cloned type I (theta class) maize GSTs and were most similar to the auxin-regulated GST family (type III or tau class GSTs) previously only identified in dicotyledonous species. The cloned GSTs were expressed as recombinant proteins in E. coli, allowing further characterisation, including detailed kinetic analysis for recombinant Zm GST I-I and Zm GST V-V.
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Barrozo, Alexandre. "Promiscuity and Selectivity in Phosphoryl Transferases." Doctoral thesis, Uppsala universitet, Struktur- och molekylärbiologi, 2016. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-279693.

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Phosphoryl transfers are essential chemical reactions in key life processes, including energy production, signal transduction and protein synthesis. They are known for having extremely low reaction rates in aqueous solution, reaching the scale of millions of years. In order to make life possible, enzymes that catalyse phosphoryl transfer, phosphoryl transferases, have evolved to be tremendously proficient catalysts, increasing reaction rates to the millisecond timescale. Due to the nature of the electronic structure of phosphorus atoms, understanding how hydrolysis of phosphate esters occurs is a complex task. Experimental studies on the hydrolysis of phosphate monoesters with acidic leaving groups suggest a concerted mechanism with a loose, metaphosphate-like transition state. Theoretical studies have suggested two possible concerted pathways, either with loose or tight transition state geometries, plus the possibility of a stepwise mechanism with the formation of a phosphorane intermediate. Different pathways were shown to be energetically preferable depending on the acidity of the leaving group. Here we performed computational studies to revisit how this mechanistic shift occurs along a series of aryl phosphate monoesters, suggesting possible factors leading to such change. The fact that distinct pathways can occur in solution could mean that the same is possible for an enzyme active site. We performed simulations on the catalytic activity of β-phosphoglucomutase, suggesting that it is possible for two mechanisms to occur at the same time for the phosphoryl transfer. Curiously, several phosphoryl transferases were shown to be able to catalyse not only phosphate ester hydrolysis, but also the cleavage of other compounds. We modeled the catalytic mechanism of two highly promiscuous members of the alkaline phosphatase superfamily. Our model reproduces key experimental observables and shows that these enzymes are electrostatically flexible, employing the same set of residues to enhance the rates of different reactions, with different electrostatic contributions per residue.
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Hayes, Peter C. "Glutathione S-transferases in the pancreas." Thesis, University of Edinburgh, 1993. http://hdl.handle.net/1842/19832.

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Glutathione S-transferase (GST) is an important xenobiotic metabolising enzyme which has been extensively studied in the liver. In the first part of this study immunohistochemistry was used to identify the presence and histological localisation of different GST isoenzymes in various gastrointestinal tract tissues in the human in health and disease. GSTP was found throughout the gastrointestinal and biliary tract whilst the position and quantity of other isoenzymes varied locally. Increased expression of GSTP was observed in cholangiocarcinoma and colonic adenocarcinoma, but not hepatocellular carcinoma. In the pancreas GSTP was present in ductal and centroacinar cells, whilst GSTA was present in acinar cells. GSTM was universally present in the cells of islets of Langerhan, not demonstrating genetic polymorphism. In both chronic pancreatitis and pancreatic carcinoma increased expression of GSTP was demonstrated. Using affinity chromatography and high performance liquid chromatography GSTA, P and M were purified from human pancreatic tissue. A novel GST isoenzyme, which ran on SDS/PAGE, similar to GSTP, was identified, purified and confirmed by Western blot analysis to be a GSTA. Feeding rats exclusively on raw soya flour resulted in pancreatic hypertrophy and eventually carcinoma. Serial measurements of GST activity showed only a minor reduction with short term feeding which returned to normal with chronic administration contrary to what has been proposed (Ross & Barrowman, 1987). No selective change in GST isoenzymes was identified. A dominant cytoplasmic protein, shown both enzymatically and by Western blot analysis to be α-amylase fell dramatically with short term administration recovering only marginally with chronic administration.
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DAWOOD, KUTAYBA F. "New physiological roles of glautathione transferases." Doctoral thesis, Università degli Studi di Roma "Tor Vergata", 2009. http://hdl.handle.net/2108/923.

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Glutathione transferases (GSTs) are enzymes able to conjugate GSH to a lot of toxic compounds thereby favoring their excretion. Recently, other protective roles of these enzymes have been discovered. In particular, it has been observed that a peculiar and strong interaction exists between some mammalian GSTs and an endogenous carrier of nitric oxide, the dinitrosyl-diglutathionyl iron complex (DNDGIC). This iron complex is a paramagnetic molecule with a characteristic EPR spectrum centered at g = 2.03, that is spontaneously formed when NO enters the cell. This complex is a strong irreversible inhibitor of glutathione reductase. The present work explores the possible role of GSTs like a protection system against DNDGIC. Actually, mammalian GSTs bind DNDGIC with extraordinary affinity (KD = 10-9-10-10 M). When rat hepatocytes are incubated in the presence of GSNO, a natural source of NO, a rapid formation of 0.1 - 0.2 mM intracellular DNDGIC has been observed. This concentration would be lethal for glutathione reductase. However the complex does not appear like a free species but completely bound to GSTs, that are present at the cytosolic level of 0.8 mM. In this form the complex is completely harmless for glutathione reductase. Surprisingly, electron paramagnetic data, reveal that DNGIC-GST is partially associated to subcellular fractions and in particular to nuclei. Our data indicate that about 10% of the cytosolic pool GST is electrostatically associated with the outer nuclear membrane, and a similar quantity is compartmentalized inside the nucleus. Mainly Alpha class GSTs, in particular GSTA1-1, GSTA2-2 and GSTA3-3, are involved in this double modality of interaction. Confocal microscopy and immunofluorescence experiments have been used to detail the electrostatic association in hepatocytes. A quantitative analysis of the membrane-bound Alpha GSTs suggests the existence of a multilayer assembly of these enzymes at the outer nuclear envelope that could represent a potent protection shell for the nucleus and an amazing novelty in cell physiology. A second target of this study is represented by the particular GST isoenzyme expressed by the Plasmodium falciparum (PfGST), the parasite causative of malaria. This enzyme is characterized by a peculiar dimer/tetramer transition that occurs in the absence of GSH and that causes a total loss of its enzymatic activity. Moreover PfGST binds hemin with high affinity and this interaction is finalized to the protection of the parasite against this toxic compound. Binding of hemin is regulated by a cooperative mechanism and does not occur in the tetrameric enzyme. Side directed mutagenesis, steady-state kinetic experiments, fluorescence anisotropy and X-ray crystallography were used to verify the involvement of some protein segment in the tetramerization process and in the cooperative phenomenon. Actually the loop 113-118 represents one the most prominent structural difference between PfGST and other GSTs. Our results demonstrate that truncation, increased rigidity or even a simple point mutation of this loop cause a dramatic change of the tetramerization kinetics that becomes hundred times slower than that observed in the native enzyme. Furthermore all mutants loose the positive cooperativity for hemin binding found in the native structure suggesting that the integrity of this peculiar loop is essential for intersubunit communication. Interestingly, the tetramerization process, that is very fast in the absence of GSH in the native enzyme, is prevented not only by GSH but even by GSSG. This result indicate that the protection of the parasite against free hemin is independent of the redox status of the cell.
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Dolan, Catherine. "Regulation of mouse hepatic glutathione S-transferases." Thesis, University of Edinburgh, 1991. http://hdl.handle.net/1842/23855.

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The glutathione S-transferases (GST) are a multi-gene family of dimeric proteins which catalyse the conjugation of glutathione to a wide range of electrophilic compounds. Three classes of mouse cytosolic GST have been isolated, alpha, mu and pi, comprising Ya-, Yb- and Yf-type subunits respectively. A marked sexual dimorphism in mouse hepatic GST has been observed. The YfYf GST is the most abundant form in the male, constituting approximately 70% of total hepatic GST content. By contrast, the Yf subunit represents only a minor form in the livers of female mice. The hormonal controls which regulate the expression of the YfYf GST in mouse liver have been investigated. Testosterone, the major male sex hormone, is found to regulate the levels of Yf in mouse liver. Castration of the male leads to a decline in the levels of Yf to that observed in females. Replacement therapy with testosterone partially restores the levels of Yf. Testosterone treatment induces expression of this subunit in the female. Growth hormone secretion from the pituitary gland differs markedly between the sexes. Androgens act to produce the male pattern of growth hormone secretion which regulates the sex-specific expression of numerous hepatic proteins. Male 'little mice', specifically defective in the production of growth hormone, exhibit a feminine pattern of GST expression, despite having normal levels of testosterone. Testosterone treatment has no effect on the expression of YfYf in little mice. In contrast, growth hormone replacement therapy, administered to simulate the male-specific pattern causes an increase in the expression of the Yf subunit. These findings strongly suggest that testosterone regulates the hepatic expression of the Yf subunit indirectly through the male-specific pattern of growth hormone secretion. The effects of the xenobiotics, phenobarbital, dexamethasone and 1,4-Bis[2-(3,5-dichloropyridyloxy)]-benzene (TCBOP) on mouse hepatic GST content have been investigated in two strains of mice, C57BL/6 and DBA/2. All three compounds were found to induce hepatic GST in both strains and sexes, predominately affecting expression of members of the mu class. TCBOP was the most potent inducer. Hypophysectomy did not significantly affect induction of GST by these compounds.
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Meikle, Ian. "Glutathione S-transferases in the adrenal cortex." Thesis, University of Edinburgh, 1992. http://hdl.handle.net/1842/19139.

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Data available prior to this thesis had shown that, of all bovine organs examined, the adrenal cortex exhibited the second highest level of glutathione S-transferase (GST) expression behind the liver. This finding, along with increasing evidence implicating the importance of GST in endogenous detoxification processes, formed the basis for a further extensive investigation of the GST isoenzymes expressed by the adrenal cortex. Investigation of the GST isoenzymes expressed by a number of different bovine organs using affinity chromatography on S-hexylglutathione-Sepharose 6B (S-hexG-Ag) revealed a marked organ-specific distribution of these enzymes. Bovine adrenal cortex, in particular, expressed isoenzymes from each GST class, as determined by immunoblotting experiments. GST activity determinations of these enzyme pools using a number of model substrates revealed the bovine enzymes to possess a specificity distinct to that of rat and human GST. Isoelectric focusing of the bovine adrenal cortex isoenzymes showed them to possess pl values similar to those found in other species. The affinity-purified mu- and pi-glass isoenzymes were resolved using anion-exchange chromatography, followed by reverse-phase hplc. Using this approach, at least 3 mu-class GST subunits and 1 pi-class GST subunit were identified. Ion-exchange chromatography failed to resolve the affinity-purified alpha-class GSTs, and reverse-phase hplc analysis resolved 2 polypeptides, designated Ya1 and Ya3 respectively. Analysis of the protein that failed to bind to the S-hexG-Ag column revealed that about 35% of GST activity remained in this fraction. Application of this material to glutathione-Sepharose 6B (GSH-Ag) resulted in the purification of an abundant alpha-class GST (1.3% total cytosolic protein). This GST was found to exhibit marked peroxidase and Δ5-ketosteroid isomerase activities, in addition to high activity with 4-hydroxynonenal. SDS/PAGE analysis revealed 2 distinct polypeptides of Mr 25900 and 26500, the former being equivalent to the Ya3 subunit purified on S-hexG-Ag, and the latter named Ya2. Ion-exchange chromatography of the GSH-Ag purified alpha-class GST isoenzyme pool resulted in a complex picture, suggesting there to be at least 3 distinct subunits in this pool.
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Hill, Alison Elspeth. "Regulation of glutathione S-transferases during stress." Thesis, University of Edinburgh, 1994. http://hdl.handle.net/1842/19846.

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Elevation of glutathione S-transferases (GST) in tumour cells can be responsible for resistance to a variety of chemotherapeutic agents. It has been hypothesised that GSTs may be induced as part of a stress response, similar to that of the prokaryotic adaptive response. To further this investigation I studied the induction of GSTs in a variety of permanent and transient stress models. A chlorambucil resistant CHO cell line which was known to express increased levels of Alpha-class GST was studied to determine the nature of the increase in protein. Northern and Southern blot analysis revealed a 4-8 fold amplification in the DNA encoding the Alpha-class GSTs with an accompanying increase in mRNA levels. Elevated levels of an Alpha-class GST were noted in oxygen resistant CHO cells. Transient exposure to 98% oxygen also induced the same Alpha-class GST. A heat shocked lung tumour cell line as well as heat selected sublines showed some changes in the levels of Pi- and Mu-class GSTs. A novel putative Mu-class GST subunit has been identified in the nucleus of heat shocked cells. The nature of the GST level variations at the RNA and DNA levels were studied. These studies do not suggest co-ordinate regulation of the GSTs as part of a general stress response. It does not exclude the possibility of GST π and perhaps the nuclear Mu-class GST are induced as part of a more limited response either to heat or in certain tissues. Inconsistencies in the data from the preliminary induction experiments led to the investigation of the effect of growth conditions on GST levels. Unexpectedly isoenzymes from three classes of GST were found to be elevated by increased confluence and a low frequency of feeding. This response was found to be mediated through the culture media.
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Books on the topic "Transferases"

1

D, Hayes J., Pickett C. B, Mantle T. J, University of Edinburgh. Dept. of Clinical Chemistry., and International GST Conference (3rd : 1989 : Royal College of Physicians of Edinburgh), eds. Glutathione S-transferases and drug resistance. London: Taylor & Francis, 1990.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 Transferases. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-85697-9.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 Transferases. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-85699-3.

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D, Tew Kenneth, ed. Structure and function of glutathione transferases. Boca Raton: CRC Press, 1993.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 · Transferases I. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-37715-8.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 · Transferases IV. Berlin, Heidelberg: Springer Berlin Heidelberg, 2006. http://dx.doi.org/10.1007/3-540-37718-2.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 · Transferases VI. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-49753-0.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 · Transferases VI. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-49755-4.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 Transferases VIII. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-49756-1.

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Schomburg, Dietmar, Ida Schomburg, and Antje Chang, eds. Class 2 • Transferases IX. Berlin, Heidelberg: Springer Berlin Heidelberg, 2007. http://dx.doi.org/10.1007/978-3-540-47815-7.

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Book chapters on the topic "Transferases"

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Ferreira, Patricia, Marta Martínez-Júlvez, and Milagros Medina. "Electron Transferases." In Methods in Molecular Biology, 79–94. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0452-5_5.

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Althaus, Felix R., and Christoph Richter. "Cellular Transferases." In Molecular Biology Biochemistry and Biophysics, 195–208. Berlin, Heidelberg: Springer Berlin Heidelberg, 1987. http://dx.doi.org/10.1007/978-3-642-83077-8_14.

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Mannervik, Bengt, and Birgitta Sjödin. "Glutathione Transferases." In Glutathione, 175–99. Boca Raton: Taylor & Francis, 2018. | Series: Oxidative stress and: CRC Press, 2018. http://dx.doi.org/10.1201/9781351261760-11.

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Dostalek, Miroslav, and Anna-Katarina Stark. "Glutathione S-Transferases." In Metabolism of Drugs and Other Xenobiotics, 147–64. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527630905.ch5.

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Kedam, Thyaga Raju, Pallavi Chittoor, and Divya Kurumala. "Glutathione-S-Transferases." In Encyclopedia of Signaling Molecules, 2146–61. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_28.

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Sherratt, Philip J., and John D. Hayes. "Glutathione S-transferases." In Enzyme Systems that Metabolise Drugs and Other Xenobiotics, 319–52. Chichester, UK: John Wiley & Sons, Ltd, 2002. http://dx.doi.org/10.1002/0470846305.ch9.

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Ward, Tony Milford. "Glutathione-S-Transferases." In Proteins and Tumour Markers May 1995, 1209–10. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-011-0681-8_38.

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Kedam, Thyaga Raju, Pallavi Chittoor, and Divya Kurumala. "Glutathione-S-Transferases." In Encyclopedia of Signaling Molecules, 1–16. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4614-6438-9_28-1.

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Soffer, Richard L. "Aminoacyl-tRNA Transferases." In Advances in Enzymology - and Related Areas of Molecular Biology, 91–139. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470122853.ch4.

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Raha, Abhijit, and Kenneth D. Tew. "Glutathione S-Transferases." In Drug Resistance, 83–122. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-1267-3_4.

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Conference papers on the topic "Transferases"

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Gogić, Anđela D., Marina Ž. Vesović, Miloš V. Nikolić, Andriana M. Bukonjić, Dušan Lj Tomović, and Nikola V. Nedeljković. "Molecular docking study of designed N-myristoyl transferase inhibitors." In 2nd International Conference on Chemo and Bioinformatics. Institute for Information Technologies, University of Kragujevac, 2023. http://dx.doi.org/10.46793/iccbi23.479g.

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N-myristoyl transferase has a key role in the myristoylation of vital proteins and is necessary for the growth and synthesis of material for the survival of various fungi. Due to the difference in the structure of fungal and mammalian N-myristoyl transferase, the crystal structure of the N-myristoyl transferase originating from Candida albicans was used as the target molecule. The present in silico study aims to design compounds, benzofuran derivatives, and simulate the interactions of the compounds and the amino acid sequences of the active center N-myristoyl transferases from Candida albicans using the molecular docking method. The highest number of significant binding interactions is realized by the derivative 4. Affinity toward the N-myristoyl transferase active site was very similar to the co-crystallized ligand, and important hydrogen interactions were retained. Based on the obtained results of molecular docking, it can be concluded that derivative 4 has the potential to inhibit N-myristoyl transferase, on which future research of its antifungal activity can be based.
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Blanchard, Sophie, Vincent Ferrieres, and Daniel Plusquellec. "STUDY OF GLYCOFURANOSYL TRANSFERASES. A GENERAL SYNTHESIS OF SUITABLE HEXOFURANOSYL DONORS." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.759.

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Hwa, Kuo-Yuan, Te-Ling Pang, and Mei-Yu Chen. "Classification of LARGE-liked GlcNAc-Transferases of Dictyostelium discoideum by Phylogenetic Analysis." In 2007 Frontiers in the Convergence of Bioscience and Information Technologies. IEEE, 2007. http://dx.doi.org/10.1109/fbit.2007.106.

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Valeeva, L. R., and M. R. Sharipova. "The role of prenyl transferases in the development of multicellular thallus Marchantia polymorpha." In IX Congress of society physiologists of plants of Russia "Plant physiology is the basis for creating plants of the future". Kazan University Press, 2019. http://dx.doi.org/10.26907/978-5-00130-204-9-2019-92.

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Bautista Jimenez, Robin Charlotte. "Diapause regulation in the flesh fly (Sarcophagabullata) by histone acetylase transferases and histone deacetylases." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.114622.

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Withers, Stephen G. "ENZYMATIC CLEAVAGE AND FORMATION OF GLYCOSIDIC BONDS: FROM GLYCOSIDASES AND LYASES TO TRANSFERASES AND GLYCOSYNTHASES." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.355.

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Mailula, Dineo, Magriet Van Der Nest, Almuth Hammerbacher, Nokuthula Mchunu, and Brenda Wingfield. "Catabolism of branched chain and aromatic amino transferases, route to fusel alcohols and acetates by the Ceratocystidaceae." In 1st International Electronic Conference on Microbiology. Basel, Switzerland: MDPI, 2020. http://dx.doi.org/10.3390/ecm2020-07097.

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Kakuda, Shinako, Yuki Sato, Kazuaki Ohtsubo, Seiichi Imajo, Masamichi Ishiguro, Shogo Oka, and Toshisuke Kawasaki. "SUBSTRATE SPECIFICITY AND STRUCTURE-FUNCTION RELATIONSHIP OF THE HNK-1 ASSOCIATED GLUCURONYL TRANSFERASES, GlcAT-P and GlcAT-S." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.428.

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Yu, AL, K.-H. Liao, C.-H. Chang, Y.-C. Lin, T.-C. Fan, J.-T. Hung, H.-L. Yeo, R.-J. Lin, and J.-C. Yu. "Abstract P1-08-05: Expression levels of sialyl transfereases and fucosyl transferases in breast cancer and their prognostic significance." In Abstracts: Thirty-Eighth Annual CTRC-AACR San Antonio Breast Cancer Symposium; December 8-12, 2015; San Antonio, TX. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.sabcs15-p1-08-05.

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Abbate, María M., Daiana B. Leonardi, Javier N. Brandani, María C. Riccheri, Geraldine Gueron, Graciela Alfonso, Elba S. Vazquez, and Javier Cotignola. "Abstract 5021: Glutathione-S-transferases polymorphisms are associated with increased risk of relapse in pediatric patients with acute lymphoblastic leukemia." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-5021.

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Reports on the topic "Transferases"

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Haynes, Robin L., and Alan J. Townsend. Glutathione Transferases and the Multidrug Resistance - Associated Protein in Prevention of Potentially Carcinogenic Oxidant Stress in Breast Cancer. Fort Belvoir, VA: Defense Technical Information Center, June 2001. http://dx.doi.org/10.21236/ada398035.

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Kun, Ernest. Molecular Cloning of Adenosinediphosphoribosyl Transferase. Fort Belvoir, VA: Defense Technical Information Center, September 1987. http://dx.doi.org/10.21236/ada185458.

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Kapoor, T. M. Purification and characterization of the Oligosaccharyl transferase. Office of Scientific and Technical Information (OSTI), November 1990. http://dx.doi.org/10.2172/6278276.

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Cushing, Donish, and Bomi Joseph. Synthetic cannabinoids severely elevate amino transferase levels. Natural cannabidiol does not. Peak Health Center, July 2018. http://dx.doi.org/10.31013/2001e.

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Woldegiorgis, S., R. C. Ahmed, Y. Zhen, C. A. Erdmann, M. L. Russell, and R. Goth-Goldstein. Genetic polymorphism in three glutathione s-transferase genes and breast cancer risk. Office of Scientific and Technical Information (OSTI), April 2002. http://dx.doi.org/10.2172/799602.

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Mauzy, Camilla A., Nathan H. Johnson, Jason J. Jacobsen, Adam G. Quade, Jeremiah N. Betz, Jeanette S. Frey, Amanda Hanes, and David Kaziska. Correlation Between Iron and alpha and pi Glutathione-S-Transferase Levels in Humans. Fort Belvoir, VA: Defense Technical Information Center, September 2012. http://dx.doi.org/10.21236/ada580919.

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Ross, Jeffrey S. Development of an Assay for Prostate Cancer Based on Methylation Status of Glutathione S-Transferase (p). Fort Belvoir, VA: Defense Technical Information Center, March 2001. http://dx.doi.org/10.21236/ada395450.

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Ross, Jeffrey S. Development of an Assay for Prostate Cancer Based on Methylation Status of Glutathione S-Transferase-pi. Fort Belvoir, VA: Defense Technical Information Center, March 2000. http://dx.doi.org/10.21236/ada392285.

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Alanyalı, Filiz Susuz. Effects of Sodium Sulphate on Catalase and Glutathione-S-Transferase Enzyme Activities in Tubifex tubifex (Müller, 1774) (Oligochaeta:Tubificidae). "Prof. Marin Drinov" Publishing House of Bulgarian Academy of Sciences, December 2021. http://dx.doi.org/10.7546/crabs.2021.11.05.

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Gershoni, Jonathan M., David E. Swayne, Tal Pupko, Shimon Perk, Alexander Panshin, Avishai Lublin, and Natalia Golander. Discovery and reconstitution of cross-reactive vaccine targets for H5 and H9 avian influenza. United States Department of Agriculture, January 2015. http://dx.doi.org/10.32747/2015.7699854.bard.

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Research objectives: Identification of highly conserved B-cell epitopes common to either H5 or H9 subtypes of AI Reconstruction of conserved epitopes from (1) as recombinantimmunogens, and testing their suitability to be used as universal vaccine components by measuring their binding to Influenza vaccinated sera of birds Vaccination of chickens with reconstituted epitopes and evaluation of successful vaccination, clinical protection and viral replication Development of a platform to investigate the dynamics of immune response towards infection or an epitope based vaccine Estimate our ability to focus the immune response towards an epitope-based vaccine using the tool we have developed in (D) Summary: This study is a multi-disciplinary study of four-way collaboration; The SERPL, USDA, Kimron-Israel, and two groups at TAU with the purpose of evaluating the production and implementation of epitope based vaccines against avian influenza (AI). Systematic analysis of the influenza viral spike led to the production of a highly conserved epitope situated at the hinge of the HA antigen designated “cluster 300” (c300). This epitope consists of a total of 31 residues and was initially expressed as a fusion protein of the Protein 8 major protein of the bacteriophagefd. Two versions of the c300 were produced to correspond to the H5 and H9 antigens respectively as well as scrambled versions that were identical with regard to amino acid composition yet with varied linear sequence (these served as negative controls). The recombinantimmunogens were produced first as phage fusions and then subsequently as fusions with maltose binding protein (MBP) or glutathioneS-transferase (GST). The latter were used to immunize and boost chickens at SERPL and Kimron. Furthermore, vaccinated and control chickens were challenged with concordant influenza strains at Kimron and SEPRL. Polyclonal sera were obtained for further analyses at TAU and computational bioinformatics analyses in collaboration with Prof. Pupko. Moreover, the degree of protection afforded by the vaccination was determined. Unfortunately, no protection could be demonstrated. In parallel to the main theme of the study, the TAU team (Gershoni and Pupko) designed and developed a novel methodology for the systematic analysis of the antibody composition of polyclonal sera (Deep Panning) which is essential for the analyses of the humoral response towards vaccination and challenge. Deep Panning is currently being used to monitor the polyclonal sera derived from the vaccination studies conducted at the SEPRL and Kimron.
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