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Articoli di riviste sul tema "Transferases"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 25 luglio 2025

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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 (1989): 531–39. http://dx.doi.org/10.1042/bj2610531.

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Abstract (sommario):

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 deter

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2

Stockman, P. K., G. J. Beckett та 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, № 2 (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

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3

Meyer, D. J., E. Lalor, B. Coles, et al. "Single-step purification and h.p.l.c. analysis of glutathione transferase 8–8 in rat tissues." Biochemical Journal 260, no. 3 (1989): 785–88. http://dx.doi.org/10.1042/bj2600785.

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Abstract (sommario):

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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4

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 (2017): 2756–66. http://dx.doi.org/10.1182/bloodadvances.2017009795.

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Abstract (sommario):

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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5

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 (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, n

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6

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 (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

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7

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 (1987): 707–13. http://dx.doi.org/10.1042/bj2470707.

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Abstract (sommario):

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 huma

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8

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 (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

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9

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 (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,

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10

Charrier, Cédric, Gary J. Duncan, Martin D. Reid, et al. "A novel class of CoA-transferase involved in short-chain fatty acid metabolism in butyrate-producing human colonic bacteria." Microbiology 152, no. 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 val

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11

Guthenberg, C., H. Jensson, L. Nyström, E. Österlund, M. K. Tahir, and B. Mannervik. "Isoenzymes of glutathione transferase in rat kidney cytosol." Biochemical Journal 230, no. 3 (1985): 609–15. http://dx.doi.org/10.1042/bj2300609.

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Glutathione transferases from rat kidney cytosol were purified about 40-fold by chromatography on S-hexylglutathione linked to epoxy-activated Sepharose 6B. Further purification by fast protein liquid chromatography with chromatofocusing in the pH interval 10.6-7.6 resolved five major peaks of activity with 1-chloro-2,4-dinitrobenzene as the second substrate. Four of the peaks were identified with rat liver transferases 1-1, 1-2, 2-2 and 4-4 respectively. The criteria used for identification included physical properties, reactions with specific antibodies, substrate specificities and sensitivi

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12

Muhammad Mohiuddin Alamgir, Qamar Jamal, and Talat Mirza. "Gene-gene and gene-environment interaction: an important predictor of oral cancer among smokeless tobacco users in Karachi." Journal of the Pakistan Medical Association 72, no. 3 (2022): 477–82. http://dx.doi.org/10.47391/jpma.1806.

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Objective: To determine the risk for oral cancer caused by simultaneous occurrence of more than one of the tested cytochrome P450 1A1MspI, glutathione S-transferaseM1 null gnd Glutathione S-transferasesT1 null gene polymorphisms. Method: The cross-sectional case-control study was conducted from December 2011 to October 2016 at the Ziauddin University, Karachi, in collaboration with Dow University of Health Sciences, Karachi, and comprised oral squamous cell carcinoma cases in group A and healthy tobacco habit-matched controls in group B. All investigations were done using standardised laborato

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13

Pollock, Thomas J., Wilbert A. T. van Workum, Linda Thorne, et al. "Assignment of Biochemical Functions to Glycosyl Transferase Genes Which Are Essential for Biosynthesis of Exopolysaccharides in Sphingomonas Strain S88 andRhizobium leguminosarum." Journal of Bacteriology 180, no. 3 (1998): 586–93. http://dx.doi.org/10.1128/jb.180.3.586-593.1998.

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ABSTRACT Glycosyl transferases which recognize identical substrates (nucleotide-sugars and lipid-linked carbohydrates) can substitute for one another in bacterial polysaccharide biosynthesis, even if the enzymes originate in different genera of bacteria. This substitution can be used to identify the substrate specificities of uncharacterized transferase genes. The spsK gene ofSphingomonas strain S88 and the pssDE genes ofRhizobium leguminosarum were identified as encoding glucuronosyl-(β1→4)-glucosyl transferases based on reciprocal genetic complementation of mutations in the spsK gene and the

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14

Ali, Nahla Osman Mohamed. "Bioinformatical Analysis of HGPRT Transferase from Different Malaria Parasite Plasmodium spp. Using Computational Tools." Malaysian Journal of Medical and Biological Research 4, no. 2 (2017): 85–90. http://dx.doi.org/10.18034/mjmbr.v4i2.430.

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In this study, HGPRT transferases from different malaria parasite Plasmodium species was analyzed and presented in this communication. The composition of leucine, lysine and Isoleucine were the highest while lowest concentrations of tryptophan and glutamine residues were noticed when compared to other amino acids. pI value of P. reichenowi HGPRT was 7.59 while the lowest pI of 6.22 was shown by P. chabaudi HGPRT. The instability index of all the transferases is varied, but for all of them it was less than 40, which indicates that all of them are stable. The aliphatic index was found to span wi

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15

Hsiao, C. D., E. O. Martsen, J. Y. Lee, S. P. Tsai, and M. F. Tam. "Amino acid sequencing, molecular cloning and modelling of the chick liver class-theta glutathione S-transferase CL1." Biochemical Journal 312, no. 1 (1995): 91–98. http://dx.doi.org/10.1042/bj3120091.

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Glutathione S-transferase CL1-2 heterodimers purified from 1-day-old chick livers were digested with Achromobacter proteinase I. The resulting fragments were separated for amino acid sequence analysis. Oligonucleotide probes were constructed based on sequence similarity to class-Theta glutathione S-transferases for PCR using a chicken liver cDNA library as template. A full-length clone (1725 bp) encoding a polypeptide comprising 261 amino acids was isolated. Including conservative substitutions, this protein has 70-73% sequence similarity with other mammalian class-Theta glutathione S-transfer

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16

Benson, A. M., M. J. Hunkeler, and J. L. York. "Mouse hepatic glutathione transferase isoenzymes and their differential induction by anticarcinogens. Specificities of butylated hydroxyanisole and bisethylxanthogen as inducers of glutathione transferases in male and female CD-1 mice." Biochemical Journal 261, no. 3 (1989): 1023–29. http://dx.doi.org/10.1042/bj2611023.

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GSH transferase isoenzymes of class Mu (two forms), class Pi (one form) and class Alpha (two forms) were purified from liver cytosols of female CD-1 mice pretreated with an anticarcinogenic inducer, 2(3)-t-butyl-4-hydroxyanisole. GSH transferases GT-8.7, GT-8.8a and GT-8.8b, GT-9.0, GT-9.3, GT-10.3 and GT-10.6 contained a minimum of six types of subunits distinguishable by structural, catalytic and immunological characteristics. H.p.l.c. analysis of the subunit compositions of affinity-purified GSH transferases from liver cytosols of induced and non-induced male and female CD-1 mice showed tha

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17

Hayes, J. D., and T. J. Mantle. "Inhibition of hepatic and extrahepatic glutathione S-transferases by primary and secondary bile acids." Biochemical Journal 233, no. 2 (1986): 407–15. http://dx.doi.org/10.1042/bj2330407.

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Glutathione S-transferases are a complex family of dimeric proteins that play a dual role in cellular detoxification; they catalyse the first step in the synthesis of mercapturic acids, and they bind potentially harmful non-substrate ligands. Bile acids are quantitatively the major group of ligands encountered by the glutathione S-transferases. The enzymes from rat liver comprise Yk (Mr 25 000), Ya (Mr 25 500), Yn (Mr 26 500), Yb1, Yb2 (both Mr 27 000) and Yc (Mr 28 500) monomers. Although bile acids inhibited the catalytic activity of all transferases studied, the concentration of a particula

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18

Brophy, P. M., C. Southan, and J. Barrett. "Glutathione transferases in the tapeworm Moniezia expansa." Biochemical Journal 262, no. 3 (1989): 939–46. http://dx.doi.org/10.1042/bj2620939.

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Four forms of GSH transferase were resolved from Moniezia expansa cytosol by GSH-Sepharose affinity chromatography and chromatofocusing in the range pH 6-4, and the presence of isoenzymes was further suggested by analytical isoelectric focusing. The four GSH transferase forms in the cestode showed no clear biochemical relationship to any one mammalian GSH transferase family. The N-terminal of the major GSH transferase form showed sequence homology with the Mu and Alpha family GSH transferases. The major GSH transferase appeared to bind a number of commercially available anthelmintics but did n

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19

Danielson, U. H., and B. Mannervik. "Paradoxical inhibition of rat glutathione transferase 4-4 by indomethacin explained by substrate-inhibitor-enzyme complexes in a random-order sequential mechanism." Biochemical Journal 250, no. 3 (1988): 705–11. http://dx.doi.org/10.1042/bj2500705.

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Under standard assay conditions, with 1-chloro-2,4-dinitrobenzene (CDNB) as electrophilic substrate, rat glutathione transferase 4-4 is strongly inhibited (I50 = 1 microM) by indomethacin. No other glutathione transferase investigated is significantly inhibited by micromolar concentrations of indomethacin. Paradoxically, the strong inhibition of glutathione transferase 4-4 was dependent on high (millimolar) concentrations of CDNB; at low concentrations of this substrate or with other substrates the effect of indomethacin on the enzyme was similar to the moderate inhibition noted for other glut

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20

Williams, Ernest, Tsvetan Bachvaroff, and Allen Place. "A Comparison of Dinoflagellate Thiolation Domain Binding Proteins Using In Vitro and Molecular Methods." Marine Drugs 20, no. 9 (2022): 581. http://dx.doi.org/10.3390/md20090581.

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Dinoflagellates play important roles in ecosystems as primary producers and consumers making natural products that can benefit or harm environmental and human health but are also potential therapeutics with unique chemistries. Annotations of dinoflagellate genes have been hampered by large genomes with many gene copies that reduce the reliability of transcriptomics, quantitative PCR, and targeted knockouts. This study aimed to functionally characterize dinoflagellate proteins by testing their interactions through in vitro assays. Specifically, nine Amphidinium carterae thiolation domains that

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21

Beláňová, Martina, Petronela Dianišková, Patrick J. Brennan, et al. "Galactosyl Transferases in Mycobacterial Cell Wall Synthesis." Journal of Bacteriology 190, no. 3 (2007): 1141–45. http://dx.doi.org/10.1128/jb.01326-07.

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ABSTRACT Two galactosyl transferases can apparently account for the full biosynthesis of the cell wall galactan of mycobacteria. Evidence is presented based on enzymatic incubations with purified natural and synthetic galactofuranose (Galf) acceptors that the recombinant galactofuranosyl transferase, GlfT1, from Mycobacterium smegmatis, the Mycobacterium tuberculosis Rv3782 ortholog known to be involved in the initial steps of galactan formation, harbors dual β-(1→4) and β-(1→5) Galf transferase activities and that the product of the enzyme, decaprenyl-P-P-GlcNAc-Rha-Galf-Galf, serves as a dir

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22

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 (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: succ

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23

Garcerá, Ana, Lina Barreto, Lidia Piedrafita, Jordi Tamarit, and Enrique Herrero. "Saccharomyces cerevisiae cells have three Omega class glutathione S-transferases acting as 1-Cys thiol transferases." Biochemical Journal 398, no. 2 (2006): 187–96. http://dx.doi.org/10.1042/bj20060034.

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The Saccharomyces cerevisiae genome encodes three proteins that display similarities with human GSTOs (Omega class glutathione S-transferases) hGSTO1-1 and hGSTO2-2. The three yeast proteins have been named Gto1, Gto2 and Gto3, and their purified recombinant forms are active as thiol transferases (glutaredoxins) against HED (β-hydroxyethyl disulphide), as dehydroascorbate reductases and as dimethylarsinic acid reductases, while they are not active against the standard GST substrate CDNB (1-chloro-2,4-dinitrobenzene). Their glutaredoxin activity is also detectable in yeast cell extracts. The en

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24

Danielson, U. H., and B. Mannervik. "Kinetic independence of the subunits of cytosolic glutathione transferase from the rat." Biochemical Journal 231, no. 2 (1985): 263–67. http://dx.doi.org/10.1042/bj2310263.

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The steady-state kinetics of the dimeric glutathione transferases deviate from Michaelis-Menten kinetics, but have hyperbolic binding isotherms for substrates and products of the enzymic reaction. The possibility of subunit interactions during catalysis as an explanation for the rate behaviour was investigated by use of rat isoenzymes composed of subunits 1, 2, 3 and 4, which have distinct substrate specificities. The kinetic parameter kcat./Km was determined with 1-chloro-2,4-dinitrobenzene, 4-hydroxyalk-2-enals, ethacrynic acid and trans-4-phenylbut-3-en-2-one as electrophilic substrates for

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25

Anderson, K., R. Andrews, L. Yin, et al. "Cytotoxicity of xenobiotics and expression of glutathione-S-transferases in immortalised rat hepatocyte cell lines." Human & Experimental Toxicology 17, no. 3 (1998): 131–37. http://dx.doi.org/10.1177/096032719801700301.

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1 Immortalised rat hepatocyte cell lines are more sensitive to the cytotoxicity of 1-chloro-2,4-dinitroben-zene and ethacrynic acid than primary cultures of hepatocytes. 2 Class alpha glutathione S-transferases are not expressed in immortalised hepatocyte cell lines. Class pi glutathione S-transferase expression is elevated in the immortalised cell lines compared with freshly isolated hepatocytes, but it is not as high as in the HTC rat hepatoma cell line. 3 Immortalised hepatocyte cell lines may provide a sensitive model system for detecting cytotoxicity associated with xenobiotics which are

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26

Gerken, Thomas A., Jiexin Zhang, Jessica Levine, and Åke Elhammer. "Mucin CoreO-Glycosylation Is Modulated by Neighboring Residue Glycosylation Status." Journal of Biological Chemistry 277, no. 51 (2002): 49850–62. http://dx.doi.org/10.1074/jbc.m205851200.

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The influence of peptide sequence and environment on the initiation and elongation of mucinO-glycosylation is not well understood. Thein vivoglycosylation pattern of the porcine submaxillary gland mucin (PSM) tandem repeat containing 31O-glycosylation sites (Gerken, T. A., Gilmore, M., and Zhang, J. (2002)J. Biol. Chem.277, 7736–7751) reveals a weak inverse correlation with hydroxyamino acid density (and by inference the density of glycosylation) with the extent of GalNAc glycosylation and core-1 substitution. We now report the time course of thein vitroglycosylation of the apoPSM tandem repea

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27

Theodore, C., S. V. Singh, T. D. Hong, and Y. C. Awasthi. "Glutathione S-transferases of human brain. Evidence for two immunologically distinct types of 26500-Mr subunits." Biochemical Journal 225, no. 2 (1985): 375–82. http://dx.doi.org/10.1042/bj2250375.

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Human brain contains one cationic (pI8.3) and two anionic (pI5.5 and 4.6) forms of glutathione S-transferase. The cationic form (pI8.3) and the less-anionic form (pI5.5) do not correspond to any of the glutathione S-transferases previously characterized in human tissues. Both of these forms are dimers of 26500-Mr subunits; however, immunological and catalytic properties indicate that these two enzyme forms are different from each other. The cationic form (pI8.3) cross-reacts with antibodies raised against cationic glutathione S-transferases of human liver, whereas the anionic form (pI5.5) does

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28

Tahir, M. K., N. Ozer, and B. Mannervik. "Isoenzymes of glutathione transferase in rat small intestine." Biochemical Journal 253, no. 3 (1988): 759–64. http://dx.doi.org/10.1042/bj2530759.

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The major glutathione transferases in the rat small-intestine cytosol were isolated and characterized. The enzymes active with 1-chloro-2,4-dinitrobenzene as second substrate were almost quantitatively recovered after affinity chromatography on immobilized S-hexylglutathione. The different basic forms of glutathione transferase, which account for 90% of the activity, were resolved by chromatofocusing. Fractions containing enzymes with lower isoelectric points were not further resolved. The isolated fractions were characterized by their elution position in chromatofocusing, apparent subunit Mr,

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29

Schecter, Robyn L., Moulay A. Alaoui-Jamali, and Gerald Batist. "Glutathione S-transferase in chemotherapy resistance and in carcinogenesis." Biochemistry and Cell Biology 70, no. 5 (1992): 349–53. http://dx.doi.org/10.1139/o92-054.

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Abstract (sommario):

Cytosolic glutathione S-transferases are composed of two monomeric subunits. These monomers are the products of different gene families designated alpha, mu, and pi. Dimerization yields either homodimeric or heterodimeric holoenzymes within the same family. The members of this complex group of proteins have been linked to the detoxification of environmental chemicals and carcinogens, and have been shown to be overexpressed in normal and tumor cells following exposure to cytotoxic drugs. They also are overexpressed in carcinogen-induced rat liver preneoplastic nodules in rat liver. In all of th

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30

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 (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

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MEYER, David J., Richmond MUIMO, Michael THOMAS, David COATES, and R. Elwyn ISAAC. "Purification and characterization of prostaglandin-H E-isomerase, a sigma-class glutathione S-transferase, from Ascaridia galli." Biochemical Journal 313, no. 1 (1996): 223–27. http://dx.doi.org/10.1042/bj3130223.

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Comparison of partial primary sequences of sigma-class glutathione S-transferases (GSH) of parasitic helminths and a GSH-dependent prostaglandin (PG)-H D-isomerase of rat immune accessory cells suggested that some of the helminth enzymes may also be involved in PG biosynthesis [Meyer and Thomas (1995) Biochem. J. 311, 739-742]. A soluble GSH transferase of the parasitic nematode Ascaridia galli has now been purified which shows high activity and specificity in the GSH-dependent isomerization of PGH to PGE, comparable to that of the rat spleen enzyme in its isomerization of PGH to PGD, and simi

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32

Hayes, J. D. "Purification and physical characterization of glutathione S-transferase K. Differential use of S-hexylglutathione and glutathione affinity matrices to isolate a novel glutathione S-transferase from rat liver." Biochemical Journal 233, no. 3 (1986): 789–98. http://dx.doi.org/10.1042/bj2330789.

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Abstract (sommario):

A novel hepatic enzyme, glutathione S-transferase K, is described that, unlike previously characterized transferases, possesses little affinity for S-hexylglutathione-Sepharose 6B but can be isolated because it binds to a glutathione affinity matrix. A purification scheme for this new enzyme was devised, with the use of DEAE-cellulose, S-hexylglutathione-Sepharose 6B, glutathione-Sepharose 6B and hydroxyapatite chromatography. The final hydroxyapatite step results in the elution of three chromatographically interconvertible forms, K1, K2 and K3. The purified protein has an isoelectric point of

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33

Tang, Fang, Xiu-Bo Zhang, Yu-Sheng Liu, and Xi-Wu Gao. "Tissue Distribution and Properties of Glutathione S-transferases in Micromelalopha troglodyta (Lepidoptera: Notodontidae)." Journal of Entomological Science 43, no. 3 (2008): 268–78. http://dx.doi.org/10.18474/0749-8004-43.3.268.

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Abstract (sommario):

The small prominent, Micromelalopha troglodyta (Graeser) (Lepidoptera: Notodontidae), is an important pest of poplar in China. Glutathione S-transferases are known to be responsible for adaptation mechanisms of M. troglodyta. Thus, the tissue distribution and kinetic constants of glutathione S-transferase activity in the small prominent were studied. Significant differences in glutathione S-transferase (GST) activity and distribution percentages of GST activity and kinetic characteristics were observed among 4 tissues (head, midgut, fat body and integument). Furthermore, the inhibition of glut

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34

Boyer, T. D., and W. C. Kenney. "Acidic glutathione S-transferases of rat testis." Biochemical Journal 230, no. 1 (1985): 125–32. http://dx.doi.org/10.1042/bj2300125.

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Abstract (sommario):

In most organs of the rat the predominant forms of glutathione S-transferase have alkaline (greater than 7.0) pI values. In contrast, in the cytosol from rat testes almost 50% of the transferase activity is due to isoenzymes with acidic (less than 7.0) pI values. We have purified three acidic forms of glutathione S-transferase from rat testis cytosol. One form accounted for more than 90% of the enzymic activity in the acidic fraction. This major form was a homodimer of a new subunit, termed Yt. This subunit had an electrophoretic mobility that was different from the subunits that form the alka

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35

Dixon, David P., and Robert Edwards. "Glutathione Transferases." Arabidopsis Book 8 (January 2010): e0131. http://dx.doi.org/10.1199/tab.0131.

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36

Hayes, John D., Jack U. Flanagan, and Ian R. Jowsey. "GLUTATHIONE TRANSFERASES." Annual Review of Pharmacology and Toxicology 45, no. 1 (2005): 51–88. http://dx.doi.org/10.1146/annurev.pharmtox.45.120403.095857.

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Abstract (sommario):

This review describes the three mammalian glutathione transferase (GST) families, namely cytosolic, mitochondrial, and microsomal GST, the latter now designated MAPEG. Besides detoxifying electrophilic xenobiotics, such as chemical carcinogens, environmental pollutants, and antitumor agents, these transferases inactivate endogenous α,β-unsaturated aldehydes, quinones, epoxides, and hydroperoxides formed as secondary metabolites during oxidative stress. These enzymes are also intimately involved in the biosynthesis of leukotrienes, prostaglandins, testosterone, and progesterone, as well as the

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37

Meyer, D. J., and M. Thomas. "Characterization of rat spleen prostaglandin H d-isomerase as a sigma-class GSH transferase." Biochemical Journal 311, no. 3 (1995): 739–42. http://dx.doi.org/10.1042/bj3110739.

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Abstract (sommario):

The prostaglandin H D-isomerase of rat immune accessory cells has been purified from spleen by a simple procedure, and its high specificity and activity [Urade, Fujimoto, Ujihara and Hayaishi (1987) J. Biol. Chem. 262, 3820-3825] have been confirmed in an assay coupled to prostaglandin H synthase. The enzyme also decreases the formation of 12[S]-hydroxy-5,8,10-heptadecatrienoic acid formed by the synthase in the presence of GSH and increases the overall rate of arachidonate oxidation. A partial amino acid sequence shows a strong relationship to GSH transferases of parasitic helminths and mollu

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38

Cao, Min, Bryan A. Bernat, Zhepeng Wang, Richard N. Armstrong та John D. Helmann. "FosB, a Cysteine-Dependent Fosfomycin Resistance Protein under the Control of ςW, an Extracytoplasmic-Function ς Factor in Bacillus subtilis". Journal of Bacteriology 183, № 7 (2001): 2380–83. http://dx.doi.org/10.1128/jb.183.7.2380-2383.2001.

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Abstract (sommario):

ABSTRACT We demonstrate that the Bacillus subtilis fosB(yndN)gene encodes a fosfomycin resistance protein. Expression offosB requires ςW, and both fosBand sigW mutants are fosfomycin sensitive. FosB is a metallothiol transferase related to the FosA class of Mn2+-dependent glutathione transferases but with a preference for Mg2+ and l-cysteine as cofactors.

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39

Næssan, Cecilia L., Wolfgang Egge-Jacobsen, Ryan W. Heiniger, et al. "Genetic and Functional Analyses of PptA, a Phospho-Form Transferase Targeting Type IV Pili in Neisseria gonorrhoeae." Journal of Bacteriology 190, no. 1 (2007): 387–400. http://dx.doi.org/10.1128/jb.00765-07.

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Abstract (sommario):

ABSTRACT The PilE pilin subunit protein of Neisseria gonorrhoeae undergoes unique covalent modifications with phosphoethanolamine (PE) and phosphocholine (PC). The pilin phospho-form transferase A (PptA) protein, required for these modifications, shows sequence relatedness with and architectural similarities to lipopolysaccharide PE transferases. Here, we used regulated expression and mutagenesis as means to better define the relationships between PptA structure and function, as well as to probe the mechanisms by which other factors impact the system. We show here that pptA expression is coupl

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40

Tahir, M. K., C. Guthenberg, and B. Mannervik. "Glutathione transferases in rat hepatoma cells. Effects of ascites cells on the isoenzyme pattern in liver and induction of glutathione transferases in the tumour cells." Biochemical Journal 257, no. 1 (1989): 215–20. http://dx.doi.org/10.1042/bj2570215.

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Abstract (sommario):

Rat hepatoma cells grown intraperitoneally as an ascites tumour were analysed with respect to their contents of cytosolic glutathione transferases. In contrast with normal liver tissue, the hepatoma cells were dominated by the class Pi glutathione transferase 7-7. All the major hepatic enzyme forms were down-regulated to almost undetectable concentrations. Livers of rats bearing ascites-hepatoma cells expressed low, but significant, amounts of protein which, by electrophoretic and immunochemical properties, appeared identical with transferase 7-7. This enzyme is not detectable in normal hepato

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41

El-Sayed, S., J. Hemingway, and R. P. Lane. "Susceptibility baselines for DDT metabolism and related enzyme systems in the sandfly Phlebotomus papatasi (Scopoli) (Diptera: Psychodidae)." Bulletin of Entomological Research 79, no. 4 (1989): 679–84. http://dx.doi.org/10.1017/s0007485300018836.

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Abstract (sommario):

AbstractDDT metabolism in Phlebotomus papatasi (Scopoli) was investigated and compared to that in DDT-resistant and susceptible strains of Culex quinquefasciatus Say and Anopheles gambiae Giles with the objective of establishing baselines for sandfly studies. P. papatasi produced eight metabolites of DDT, with DDE predominating, as in the two mosquito species. Both oxidases and glutathione transferases were found to be involved in DDT metabolism in insecticide-susceptible adults of P. papatasi. The activity level of glutathione transferases and the reduced and oxidized difference spectra of cy

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42

Nigam, Rita, Tracy Whiting, and Brian M. Bennett. "Effect of inhibitors of glutathione S-transferase on glyceryl trinitrate activity in isolated rat aorta." Canadian Journal of Physiology and Pharmacology 71, no. 2 (1993): 179–84. http://dx.doi.org/10.1139/y93-025.

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Abstract (sommario):

We investigated the role of glutathione S-transferases (enzymes known to biotransform organic nitrates) in the vascular action of glyceryl trinitrate (GTN). Relaxation of phenylephrine-contracted rat aortic strips was assessed in the presence or absence of the glutathione S-transferase inhibitors Basilen Blue, bromosulfophthalein, Rose Bengal, hematin, chlorotriphenyltin, and (octyloxy)benzoylvinylglutathione. Whereas none of the inhibitors increased the EC50 for GTN relaxation, glutathione S-transferase activity in the 100 000 × g supernatant fraction of rat aorta was inhibited markedly by mo

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43

van Grinsven, Koen W. A., Silke Rosnowsky, Susanne W. H. van Weelden, et al. "Acetate:Succinate CoA-transferase in the Hydrogenosomes of Trichomonas vaginalis." Journal of Biological Chemistry 283, no. 3 (2007): 1411–18. http://dx.doi.org/10.1074/jbc.m702528200.

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Abstract (sommario):

Acetate:succinate CoA-transferases (ASCT) are acetate-producing enzymes in hydrogenosomes, anaerobically functioning mitochondria and in the aerobically functioning mitochondria of trypanosomatids. Although acetate is produced in the hydrogenosomes of a number of anaerobic microbial eukaryotes such as Trichomonas vaginalis, no acetate producing enzyme has ever been identified in these organelles. Acetate production is the last unidentified enzymatic reaction of hydrogenosomal carbohydrate metabolism. We identified a gene encoding an enzyme for acetate production in the genome of the hydrogenos

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44

Shimoji, Miyuki, and Yoko Aniya. "Glutathione S-Transferases in Rat Testis Microsomes: Comparison with Liver Transferase." Journal of Biochemistry 115, no. 6 (1994): 1128–34. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a124468.

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45

Hayes, J. D., and T. J. Mantle. "Use of immuno-blot techniques to discriminate between the glutathione S-transferase Yf, Yk, Ya, Yn/Yb and Yc subunits and to study their distribution in extrahepatic tissues. Evidence for three immunochemically distinct groups of transferase in the rat." Biochemical Journal 233, no. 3 (1986): 779–88. http://dx.doi.org/10.1042/bj2330779.

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Abstract (sommario):

The glutathione S-transferases are dimeric enzymes whose subunits can be defined by their mobility during sodium dodecyl sulphate/polyacrylamide-gel electrophoresis as Yf (Mr 24,500), Yk (Mr 25,000), Ya (Mr 25,500), Yn (Mr 26,500), Yb1 (Mr 27,000), Yb2 (Mr 27,000) and Yc (Mr 28,500) [Hayes (1986) Biochem. J. 233, 789-798]. Antisera were raised against each of these subunits and their specificities assessed by immuno-blotting. The transferases in extrahepatic tissues were purified by using, sequentially, S-hexylglutathione and glutathione affinity chromatography. Immune-blotting was employed to

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46

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 (1998): 203–8. http://dx.doi.org/10.1042/bj3290203.

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Abstract (sommario):

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

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47

Cashman, Timothy J., and Chinmay M. Trivedi. "N-Acetyl Transferases." Circulation Research 128, no. 8 (2021): 1170–72. http://dx.doi.org/10.1161/circresaha.121.319049.

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48

Ketterman, Albert J., Chonticha Saisawang, and Jantana Wongsantichon. "Insect glutathione transferases." Drug Metabolism Reviews 43, no. 2 (2011): 253–65. http://dx.doi.org/10.3109/03602532.2011.552911.

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49

MANTLE, TIMOTHY J., FIONA M. McCUSKER, MICHAEL PHILLIPS, and SINEAD BOYCE. "Glutathione S-transferases." Biochemical Society Transactions 18, no. 2 (1990): 175–77. http://dx.doi.org/10.1042/bst0180175.

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50

Smith, A., I. Nuiry, and Y. C. Awasthi. "Interactions with glutathione S-transferases of porphyrins used in photodynamic therapy and naturally occurring porphyrins." Biochemical Journal 229, no. 3 (1985): 823–31. http://dx.doi.org/10.1042/bj2290823.

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Abstract (sommario):

Several naturally occurring porphyrins and porphyrins used in photodynamic therapy inhibit glutathione S-transferase isoenzymes either purified from rat liver or lung or in cytosol from normal and from cancerous (Morris 7288C hepatoma) liver. Although differences occur in the type and amount of transferases in normal and cancerous liver and in the liver of rats bearing an extrahepatic tumour, these enzymes are potential binding sites for porphyrins. Porphyrin structure is an important factor in determining the affinity of binding, as shown by the relative inhibitory effectiveness. Of the dicar

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