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Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate.
Evidence from nitrogen-15 and solvent deuterium isotope effects on the chemical mechanism of adenosine deaminase.
Formation of the alpha-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase.
Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites.
Expression and stereochemical and isotope effect studies of active 4-oxalocrotonate decarboxylase.
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Expression and stereochemical and isotope effect studies of active 4-oxalocrotonate decarboxylase.
Expression and stereochemical and isotope effect studies of active 4-oxalocrotonate decarboxylase. Biochemistry. 2000 Feb 01; 39(4):718-26.
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PubMed
subject areas
Carbon Isotopes
Carboxy-Lyases
Deuterium
Enzyme Activation
Escherichia coli
Genetic Vectors
Glutamic Acid
Glutamine
Hydro-Lyases
Kinetics
Mutagenesis, Site-Directed
Nuclear Magnetic Resonance, Biomolecular
Protons
Pseudomonas putida
Recombinant Proteins
Stereoisomerism
authors with profiles
Paul F Cook