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Human glutathione transferase catalysis of the formation of S ‐nitrosoglutathione from organic nitrites plus glutathione
Author(s) -
Meyer David J.,
Kramer Harry,
Ketterer Brian
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00904-x
Subject(s) - glutathione , s nitrosoglutathione , chemistry , glutathione transferase , catalysis , glutathione s transferase , biochemistry , enzyme
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, k 2 values of 22.3 and 21.0 M −1 · min −1 were obtained for n ‐butyl‐ and amyl nitrites, respectively. Rate enhancements, ( k cat / K m × k 2 ) × 10 −4 , due to purified human GSH transferases A1−1, A2−2 and Mla−la 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.