A random rapid equilibrium mechanism for leukotriene C4 synthase.
Kinetic studies performed on the conjugation reaction catalyzed by LTC4 synthase proved to conform to a random rapid equilibrium mechanism which was further substantiated by competition patterns ruling out other possible mechanisms. Most cytosolic Gst's investigated to date appear to follow a random kinetic mechanism although are mainly responsible for detoxification purposes. Conversely, LTC4 synthase possesses a very different biological role yet still follows a similar mechanism. Therefore, it can be concluded that most GSTs function in a consistent manner regardless of their biological function. Of interest are the mechanisms of the other members of the MAPEG family which in some respects are closer to conventional GSTs than to LTC4 synthase, yet they remain to be deciphered.
Gupta
N
N
Merck Frosst Centre for Therapeutic Research, Pointe Claire-Dorval, Quebec, Canada.
Greeser
M J
MJ
Ford-Hutchinson
A W
AW
D004791:Enzyme Inhibitors / Q000494:pharmacology; D005978:Glutathione / Q000378:metabolism; D005982:Glutathione Transferase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007211:Indoles / Q000494:pharmacology; D007700:Kinetics; D017572:Leukotriene A4 / Q000378:metabolism; D008954:Models, Biological; D011725:Pyridines / Q000494:pharmacology
D004791:Enzyme Inhibitors; D007211:Indoles; D017572:Leukotriene A4; D011725:Pyridines; C086903:L 699333; D005982:Glutathione Transferase; C041116:leukotriene-C4 synthase; D005978:Glutathione