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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Dihydroxyacetone Phosphate / analogs & derivatives*
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Dihydroxyacetone Phosphate / metabolism*
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Fructose-Bisphosphate Aldolase / metabolism*
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Glyceraldehyde 3-Phosphate / analogs & derivatives*
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Glyceraldehyde 3-Phosphate / metabolism
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Imines
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Models, Chemical
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Muscles / enzymology
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Organophosphorus Compounds / metabolism*
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Rabbits
Substances
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Imines
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Organophosphorus Compounds
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Glyceraldehyde 3-Phosphate
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4-hydroxy-3-oxobutyl-1-phosphonic acid
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Dihydroxyacetone Phosphate
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Fructose-Bisphosphate Aldolase