Kinetic studies of bovine liver fructose-1,6-bisphosphatase.

摘要: Initial rate kinetic studies with bovine liver fructose-1,6-bisphosphatase were carried out in both directions of the reaction to determine sequence product release from enzyme. Product inhibition by fructose-6-P was found be S-linear, I-linear noncompetitive relative fructose-1,6-bisphosphate, whereas inorganic orthophosphate determined linear competitive respect substrate. The kinetics reverse studied coupling phosphatase aldolase, triosephosphate isomerase, and glycerolphosphate dehydrogenase reactions. results harmony Uni Bi ordered random sequential mechanisms as well a ping-pong mechanism. nomenclature is that Cleland (Cleland, W.W. (1963) Biochim. Biophys. Acta 67, 104-137). However, nonkinetic considerations, when taken together results, suggest steady state mechanism most likely possibility. There evidence isomerization binary complex enzyme phosphate occurs Although magnesium required for reaction, there no discriminates between magnesium-associated or divalent cation-free forms substrates.