Interaction of phosphonomethyl analog of dihydroxyacetone phosphate with rabbit muscle aldolase.
Aldolase presents the same binding affinity for dihydroxyacetone phosphate and its phosphonomethyl analog, but the partition coefficient between the intermediates from the Michaelis complex to the eneamine is different. The effects of the structural modification of the triose phosphate substrate on the interaction with rabbit muscle aldolase are discussed in connection with the mechanistic pathway and the three-dimensional structure of the enzyme.
Groupe de Chimie Organique Biologique, UMR CNRS 5623, Université Paul Sabatier, Bât. II R1, 118 route de Narbonne, 31062 Toulouse Cedex 4, France.
P
P
Page
C
C
Blonski
J
J
Périé
D000818:Animals; D004099:Dihydroxyacetone Phosphate / Q000031:analogs & derivatives* / Q000378:metabolism*; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D005986:Glyceraldehyde 3-Phosphate / Q000031:analogs & derivatives* / Q000378:metabolism; D007097:Imines; D008956:Models, Chemical; D009132:Muscles / Q000201:enzymology; D009943:Organophosphorus Compounds / Q000378:metabolism*; D011817:Rabbits
D007097:Imines; D009943:Organophosphorus Compounds; D005986:Glyceraldehyde 3-Phosphate; C008066:4-hydroxy-3-oxobutyl-1-phosphonic acid; D004099:Dihydroxyacetone Phosphate; D005634:Fructose-Bisphosphate Aldolase