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
Related Documents :
15588018 - Gestational age and birth weight in relation to n-3 fatty acids among inuit (canada).
8457508 - Ophthalmic findings in classical galactosaemia--prospective study.
9755178 - Modifications of u2 snrna are required for snrnp assembly and pre-mrna splicing.
16192348 - Parent-of-origin transmission of thrombophilic alleles to intrauterine growth-restricte...
10819788 - Evidence for spontaneous postlactational estrus in gray short-tailed opossums (monodelp...
23470068 - Safety of procedural sedation in pregnancy.
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.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Functional and structural similarity between the X protein of hepatitis B virus and nucleoside dipho...
Next Document:  Thiol dependent isomerization of all-trans-retinoic acid to 9-cis-retinoic acid.