Human glutathione transferase catalysis of the formation of S‐nitrosoglutathione from organic nitrites plus glutathione

FEBS Letters

Ketterer, Brian¹  Meyer, David J.¹  Kramer, Harry¹ 

[1] Molecular Toxicolgy Research Group, Department of Biochemistry and Molecular Biology, University College London, Windeyer Building, Cleveland Street, London W1P 6DB, UK

关键词: S-Nitrosoglutathione;    Amyl nitrite;    Butyl nitrite;    Glutathione;    Glutathione transferase;    Human;    AIDS;    GSH;    reduced gluthathione;    GSNO;    S-nitrosoglutathione;   

DOI  :  10.1016/0014-5793(94)00904-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown