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. 1998 Jul 28;1386(1):59-64.
doi: 10.1016/s0167-4838(98)00061-2.

Interaction of phosphonomethyl analog of dihydroxyacetone phosphate with rabbit muscle aldolase

P Page  1 , C Blonski, J Périé
Affiliations

Interaction of phosphonomethyl analog of dihydroxyacetone phosphate with rabbit muscle aldolase

P Page et al. Biochim Biophys Acta. .

Abstract

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.

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