Specifically deuterated l-malate as an NMR probe of the aspartate transcarbamylase catalytic site

摘要: Abstract Replacement of protons by deuterium at specific positions l -malate results in simplified proton magnetic resonance spectra and a large reduction the effect intramolecular dipole-dipole relaxation resonances. Under conditions concomitant decoupling, these are further simplified. These advantages used to study two specifically deuterated -malates presence catalytic subunit aspartate transcarbamylase. The bound rates L-malates much smaller than those undeuterated implying that major mechanism for enzyme bound, is interaction.