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Multiple isotope effects with alternative dinucleotide substrates as a probe of the malic enzyme reaction.
Product dependence of deuterium isotope effects in enzyme-catalyzed reactions.
Isotope partitioning for NAD-malic enzyme from Ascaris suum confirms a steady-state random kinetic mechanism.
Crystal structure of the malic enzyme from Ascaris suum complexed with nicotinamide adenine dinucleotide at 2.3 A resolution.
Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction.
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Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction.
Mechanism of the addition half of the O-acetylserine sulfhydrylase-A reaction. Biochemistry. 2005 Apr 12; 44(14):5541-50.
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PubMed
subject areas
Cysteine Synthase
Hydrogen-Ion Concentration
Kinetics
Nuclear Magnetic Resonance, Biomolecular
authors with profiles
Paul F Cook