title: Leukotriene C4 formation catalyzed by three distinct forms of human cytosolic glutathione transferase.
abstract: The ability of three distinct types of human cytosolic glutathione transferase to catalyze the formation of leukotriene C4 from glutathione and leukotriene A4 has been demonstrated. The near-neutral transferase (mu) was the most efficient enzyme with Vmax= 180 nmol X min-1 X mg-1 and Km= 160 microM. The Vmax and Km values for the basic (alpha-epsilon) and the acidic (pi) transferases were 66 and 24 nmol X min-1 X mg-1 and 130 and 190 microM, respectively. The synthetic methyl ester derivative of leukotriene A4 was somewhat more active as a substrate for all the three forms of the enzyme.
authors.forename: M
authors.initials: M
authors.lastname: Söderström
authors.forename: B
authors.initials: B
authors.lastname: Mannervik
authors.forename: L
authors.initials: L
authors.lastname: Orning
authors.forename: S
authors.initials: S
authors.lastname: Hammarström
mesh_terms: D001095:Arachidonic Acids / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D003600:Cytosol / Q000201:enzymology; D005978:Glutathione / Q000378:metabolism; D005982:Glutathione Transferase / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D017572:Leukotriene A4; D013189:SRS-A / Q000096:biosynthesis*
chemical_list: D001095:Arachidonic Acids; D007527:Isoenzymes; D017572:Leukotriene A4; D013189:SRS-A; D005982:Glutathione Transferase; D005978:Glutathione