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Adenine binding to glutamate dehydrogenase: Natural and magnetic circular dichroism studies
Author(s) -
Jallon J.M.,
Risler Y.,
Schneider C.,
Thiery J.M.
Publication year - 1973
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(73)80115-2
Subject(s) - crystallography , circular dichroism , stereochemistry , physics , chemistry , microbiology and biotechnology , biology
In the study of a nicotinamide adenine dinucleotide dependent dehydrogenase, one meets, among others, the following problems: are both aromatic rings of the nucleotide necessary for the binding to the enzyme and for the catalysis; which is their respective role; how are they interacting with the protein and with one another? In the case of lactate dehydrogenase, crystallographic data are available showing that both the adenine and nicotinamide parts are bound to the protein [ 11. For glutamate dehydrogenase, only indirect information is deduced from kinetic studies and from studies of spectral perturbations associated with ligand binding. Kinetic studies have shown that apart from NAD(H)* and NADP(H), a certain number of analogues are active as coenzymes, although with different efficiencies [2]. For example, NMNH binds, but with a