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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.
Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation.
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Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation.
Stepwise versus concerted oxidative decarboxylation catalyzed by malic enzyme: a reinvestigation. Biochemistry. 1994 Mar 01; 33(8):2096-103.
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PubMed
subject areas
Animals
Ascaris
Carboxylic Acids
Catalysis
Chickens
Horses
Isotopes
Malate Dehydrogenase
NAD
NADP
Oxaloacetates
Oxidation-Reduction
authors with profiles
Paul F Cook