Leukotriene C4 formation catalyzed by three distinct forms of human cytosolic glutathione transferase.
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.
Söderström
M
M
Mannervik
B
B
Orning
L
L
Hammarström
S
S
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*
D001095:Arachidonic Acids; D007527:Isoenzymes; D017572:Leukotriene A4; D013189:SRS-A; D005982:Glutathione Transferase; D005978:Glutathione