Characterization of rat spleen prostaglandin H D-isomerase as a sigma-class GSH transferase.
The prostaglandin H D-isomerase of rat immune accessory cells has been purified from spleen by a simple procedure, and its high specificity and activity [Urade, Fujimoto, Ujihara and Hayaishi (1987) J. Biol. Chem. 262, 3820-3825] have been confirmed in an assay coupled to prostaglandin H synthase. The enzyme also decreases the formation of 12[S]-hydroxy-5,8,10-heptadecatrienoic acid formed by the synthase in the presence of GSH and increases the overall rate of arachidonate oxidation. A partial amino acid sequence shows a strong relationship to GSH transferases of parasitic helminths and molluscs, indicating that it is the first example of a vertebrate sigma-class GSH transferase, and suggesting that certain helminth GSH transferases may be involved in prostaglandin synthesis.
D000595:Amino Acid Sequence; D000818:Animals; D005982:Glutathione Transferase / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D019746:Intramolecular Oxidoreductases; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D007535:Isomerases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D054834:Lipocalins; D008297:Male; D008969:Molecular Sequence Data; D011451:Prostaglandin-Endoperoxide Synthases / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley; D017386:Sequence Homology, Amino Acid; D013154:Spleen / Q000201:enzymology*
D007527:Isoenzymes; D054834:Lipocalins; D011451:Prostaglandin-Endoperoxide Synthases; D005982:Glutathione Transferase; D007535:Isomerases; D019746:Intramolecular Oxidoreductases; C022466:prostaglandin R2 D-isomerase