Fructose-1,6-bisphosphate aldolase from rabbit muscle. Kinetic resolution of the enamine phosphate from the enamine-aldehyde intermediate at low temperature.
At or below -12 degrees C and in the presence of 40% ethylene glycol, only two out of the four dihydroxyacetone phosphate binding sites of aldolase are catalytically active. At these same temperatures and at pH* 8.3, the equilibrium between the pre-enamine and the enamine plus the post-enamine intermediates is largely shifted in favor of the latter. The enamine phosphate and the enamine-aldehyde phosphate intermediates have been resolved by studying the rate of their formation at -13 degrees C and pH* 5.28 and the trapping by DL-glyceraldehyde 3-phosphate at -24 degrees C and pH* 5.24.
D000447:Aldehydes; D000818:Animals; D001665:Binding Sites; D005615:Freezing; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D011485:Protein Binding; D011817:Rabbits; D012545:Schiff Bases
D000447:Aldehydes; D012545:Schiff Bases; D005634:Fructose-Bisphosphate Aldolase