Biochemistry international 1987-12-01

Racemic LTA4 methyl ester bioconversion into LTC4 methyl ester by various glutathione S-transferases.

G Maury, E Ginestar, D Sraïri, H Thaler-Dao, M J Dembélé-Duchesne, J Lorquin, A Crastes de Paulet

Index: Biochem. Int. 15(6) , 1127-35, (1987)

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Abstract

It has been shown that various glutathione transferases can synthesize leukotriene C4, or its methyl ester, from glutathione and leukotriene A4. We questioned whether the same enzymes could be used to resolve racemic leukotriene A4 methyl ester (more easily prepared than the optically active enantiomer) and to produce leukotriene C4 methyl ester selectively. We present in this paper a study of the enantioselectivity of some rat liver glutathione transferase isozymes and of the glutathione transferase of human placenta for the leukotriene A4 methyl ester isomers. The rat liver 3-4 glutathione transferase exhibited the highest conversion rate but preferentially converted the (5R, 6R) leukotriene A4 methyl ester. The placental enzyme was fairly selective for the natural (5S, 6S) enantiomer but the rate of conversion was low.