Alternate Substrates and Isotope Effects as a Probe of the Malic Enzyme Reaction
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+ re...
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| Format: | Others |
| Language: | English |
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University of North Texas
1988
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| Online Access: | https://digital.library.unt.edu/ark:/67531/metadc330840/ |