| Literature DB >> 4051502 |
M E Spearman, R A Prough, R W Estabrook, J R Falck, S Manna, K C Leibman, R C Murphy, J Capdevila.
Abstract
The catalysis of glutathione (GSH) conjugation to epoxyeicosatrienoic acids (EETs) by various purified isozymes of glutathione S-transferase was studied. A GSH conjugate of 14,15-EET was isolated by HPLC and TLC; this metabolite contained one molecule of EET and one molecule of GSH. Fast atom bombardment mass spectrometry of the isolated metabolite confirmed the structure as a GSH conjugate of 14,15-EET. Studies designed to determine the isozyme specificity of this reaction demonstrated that two isozymes, 3-3, and 5-5, efficiently catalyzed this conjugation reaction. The Km values for 14,15-EET were approximately 10 microM and the Vmax values ranged from 25 to 60 nmol conjugate formed min-1 mg-1 purified transferase 3-3 and 5-5. The 5,6-, 8,9-, and 11,12-EETs were also substrates for the reaction, albeit at lower rates. These results demonstrate that the EETs can serve as substrates for the cytosolic glutathione S-transferases.Entities:
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Year: 1985 PMID： 4051502 DOI： 10.1016/0003-9861(85)90496-5
Source DB: PubMed Journal: Arch Biochem Biophys ISSN： 0003-9861 Impact factor: 4.013