Equilibrium substrate binding studies of the malic enzyme of pigeon liver. Equivalence of nucleotide sites and anticooperativity associated with the binding of L-malate to the enzyme-manganese(II)-reduced nicotinamide adenine dinucleotide phosphate ternary complex
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00546a020
Reference52 articles.
1. Coenzyme Binding by X-Irradiated Glutamate and Lactate Dehydrogenase*
2. Mechanism of pigeon liver malic enzyme. Kinetics, specificity, and half-site stoichiometry of the alkylation of a cysteinyl residue by the substrate-inhibitor bromopyruvate
3. Mechanism of pigeon liver malic enzyme modification of histidyl residues by ethoxyformic anhydride
4. Cornish-Bowden, A. (1976) Principles of Enzyme Kinetics, pp120-122, Butterworths, Boston, MA.
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