Alternate Substrates and Isotope Effects as a Probe of the Malic Enzyme Reaction
Description:
Dissociation constants for alternate dirmcleotide substrates and competitive inhibitors suggest that the dinucleotide binding site of the Ascaris suum NAD-malic enzyme is hydrophobic in the vicinity of the nicotinamide ring. Changes in the divalent metal ion activator from Mg^2+ to Mn^2+ or Cd^2+ results in a decrease in the dinucleotide affinity and an increase in the affinity for malate. Primary deuterium and 13-C isotope effects obtained with the different metal ions suggest either a change …
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Date:
August 1988
Creator:
Gavva, Sandhya Reddy
Partner:
UNT Libraries