Microsomal glutathione 5-transferase

Wallin H, Morgenstem R. 1990. Activation of microsomal glutathione transferase activity by reactive intermediates formed during the metabolism of phenol. Chem-Biol Interact 75 185-199. 

Jolivette, L.J., and Anders, M.W., Structure-activity relationship for the biotransformation of haloalkenes by rat liver microsomal glutathione transferase 1, Chem. Res. Toxicol., 15, 1036-1041, 2002. 

Morgenstern, R., Lundqvist, G., Andersson, G., Balk, L., and DePierre, J. W. (1984) The distribution of microsomal glutathione transferase among different organelles, different organs, and different organisms. Biochem. Pharmacol. 33, 3609-3614. 

A14. Andersson, C., Soderstrdm, M., and Mannervik, B., Activation and inhibition of microsomal glutathione transferase from mouse liver. Biochem. J. 249, 819-823 (1988). 

M20. Morgenstem, R., and DePierre, J. W., Microsomal glutathione transferase. Purification in unactivated form and further characterization of the activation process, substrate specificity and amino acid composition. Eur. J. Biochem. 134, 591-597 (1983). 

M22. Morgenstem, R., DePierre, J.W., and Jomvall, H., Microsomal glutathione transferase. Primary structure. J. Biol. Chem. 260, 13976-13983 (1985). 

Morgenstern R. Microsomal glutathione transferase 1. Methods Enzymol 2005 401 136-146. 

Ji,Y., Akerboom,T.P.M., Sies, H., Microsomal formation of S-nitrosoglutathione from organic nitrites possible role of membrane-bound glutathione transferase. Biochem. J. 313 (1996), p. 377-380... 

Y. Ji, T. P. M. Akerboom, H. Sies, Microsomal Formation of S-Ni IrosogIulathione from Organic Nitrites Possible Role of Membrane-Bound Glutathione Transferase , Biochem. J. 1996, 373,377-380. 

Shih TW, Hill DL. 1981. Metabolic activation of 1,2-dibromoethane by glutathione transferase and by microsomal mixed function oxidase Further evidence for formation of two reactive metabolites. Res Common Chem Pathol Pharmacol 33 449-461. 

Datta, J. and Samanta, T. B. Characterization of a novel microsomal glutathione S-transferase produced by Aspergillus ochraceus TS. Mol. Cell. Biochem. 1992, 118 31-38. 

Studies with ribosomes indicated that, in contrast to experiments with microsomes, the purified transferring enzyme described above failed to catalyze aminoacyl transfer (Tablem) however, the crude pH 5 Supernatant was active with both particle preparations. As described in Table IV, when the incubations with purified enzyme (transferase I) were supplemented with the dialyzed deoxycholate-soluble microsomal extract (transferase II) obtained during the isolation of ribosomes (Figure 1), transferring activity was restored (6, 7). Glutathione was also... 

The transfer of labeled amino acids from aminoacyl sRNA to purified rat-liver ribonucleoprotein particles has been shown to require GTP, and a soluble portion (pH 5 Supernatant) of the cell. An enzyme fraction, aminoacyl transferase (or polymerase) I, purified from the pH 5 Supernatant was found to catalyze the transfer of amino acid to protein with microsomes, but not with the more purified ribonucleoprotein particles (ribosomes). When transferase I was supplemented with glutathione and a microsomal extract, microsomal aminoacyl transferase (or polymerase) H, transferring activity was restored. Since the pH 5 Supernatant was active in catalyzing the transfer of amino acids from sRNA to ribosomal protein, it was concluded that both transferring activities were present in this crude fraction. Resolution of the two activities from the pH 5 Supernatant fraction was obtained by salt-fractionation procedures. Neither enzyme fraction was active when incubated individually or with glutathione, but together in the presence of... 

Flaenen GRMM, Bermeulen NPE, Taai Tin Tsoi JNL, et al. 1988. Activation of the microsomal glutathione-S-transferase and reduction of the gultathione dependent protection against lipid peroxidation by acrolein. Biochem Pharmacol 37 1933-1938. 

Snyder R, Chepiga T, Yang CS, et al. 1993a. Benzene metabolism by reconstituted cytochromes P450, 2B1, and 2E1 and its modulation by cytochrome b5, microsomal epoxide hydrolase, and glutathione transferases evidence for an important role of microsomal epoxide hydrolase in the formation of hydroquinone. Toxicol Appl Pharmacol 122(2) 172-181. 

Enzyme-catalyzed epoxide ring opening including discussion of convergent families of epoxide hydrolases, the catalytic mechanism of microsomal epoxide hydrolases, epoxide hydrolases in metabolism, and the synthesis, structure, and mechanism of leukotriene A4 hydrolase, and glutathione transferase has been reviewed by Armstrong <1999CONAP(5)51>. 

Wolf, C.R., Moll, E., Friedberg, T., Oesch, F., Buchmann, A., Knhl-mann, W.D. Kunz, H.W. Characterization, localization and regulation of a novel phenobarbital-inducible form of cytochrome P 450, compared with three further P450-isoenzymes, NADPH P450-reductase glutathione transferases and microsomal epoxide hydrolase. Carcinogenesis 1984 5 993-1001... 

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