Document Detail

Human glutathione transferase catalysis of the formation of S-nitrosoglutathione from organic nitrites plus glutathione.
MedLine Citation:
PMID:  8082808     Owner:  NLM     Status:  MEDLINE    
The kinetics of spontaneous and human glutathione transferase catalysed formation of S-nitrosoglutathione (GSNO) from glutathione (GSH) and n-butyl- or amyl nitrite have been studied. At physiological pH and temperature, k2 values of 22.3 and 21.0 M-1.min-1 were obtained for n-butyl- and amyl nitrites, respectively. Rate enhancements, (kcat/Km x k2) x 10(-4), due to purified human GSH transferases A1-1, A2-2 and M1a-1a were, respectively, 7.00, 2.94 and 10.6 for n-butyl nitrite and 121, 3.92 and 34.5 for amyl nitrite. GSH transferase P1-1 showed no detectable catalysis of the formation of GSNO. The data suggest that the presence of GSTs A1-1, A2-2 or M1-1 contribute substantially to intracellular metabolism of alkyl nitrites to GSNO. The results may be significant with regard to the immunotoxicity of alkyl nitrites.
D J Meyer; H Kramer; B Ketterer
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  FEBS letters     Volume:  351     ISSN:  0014-5793     ISO Abbreviation:  FEBS Lett.     Publication Date:  1994 Sep 
Date Detail:
Created Date:  1994-10-13     Completed Date:  1994-10-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0155157     Medline TA:  FEBS Lett     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  427-8     Citation Subset:  IM    
Department of Biochemistry and Molecular Biology, University College London, UK.
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MeSH Terms
Glutathione / analogs & derivatives*,  metabolism*
Glutathione Transferase / metabolism*
Kidney / enzymology
Liver / enzymology
Nitrites / metabolism*
Nitroso Compounds / metabolism*
Reg. No./Substance:
0/Nitrites; 0/Nitroso Compounds; 57564-91-7/S-Nitrosoglutathione; 70-18-8/Glutathione; EC Transferase

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