Literature DB >> 2254303

Isozyme specificity in the conversion of hepoxilin A3 (HxA3) into a glutathionyl hepoxilin (HxA3-C) by the Yb2 subunit of rat liver glutathione S-transferase.

O Laneuville1, M Chang, C C Reddy, E J Corey, C R Pace-Asciak.   

Abstract

1-14C-Labeled hepoxillin A3 is transformed by a purified preparation of glutathione S-transferase in the presence of glutathione into a glutathionyl conjugate in which the glutathione is covalently coupled to the carbon 11 position of hepoxilin A3. We have termed the glutathione conjugate hepoxilin A3-C in keeping with the established nomenclature for glutathione conjugates in the leukotriene series. Using [3H]glutathione as cosubstrate, the kinetics of the reaction were followed. Among various rat liver glutathione S-transferase isozymes, a homodimer of the Yb2 subunit showed the best activity, while isozymes containing the Ya and Yc subunits showed marginal activity with hepoxilin A3 as substrate.

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Year:  1990        PMID: 2254303

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

Review 1.  Novel eicosanoid pathways: the discovery of prostacyclin/6-keto prostaglandin F1alpha and the hepoxilins.

Authors:  Cecil R Pace-Asciak
Journal:  Mol Neurobiol       Date:  2005-08       Impact factor: 5.590

Review 2.  The hepoxilins and some analogues: a review of their biology.

Authors:  Cecil R Pace-Asciak
Journal:  Br J Pharmacol       Date:  2009-04-30       Impact factor: 8.739

Review 3.  Hepoxilins: a review on their enzymatic formation, metabolism and chemical synthesis.

Authors:  C R Pace-Asciak; D Reynaud; P M Demin
Journal:  Lipids       Date:  1995-02       Impact factor: 1.880

4.  Hepoxilin A3-specific binding in human neutrophils.

Authors:  D Reynaud; P Demin; C R Pace-Asciak
Journal:  Biochem J       Date:  1996-01-15       Impact factor: 3.857

  4 in total

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