Evidence for the nonhydrophobic interaction of aromatic, nitrogen-containing compounds with the coenzyme binding site of a NAD-linked D-lactate dehydrogenase.
Quantitative structure activity relationships suggest that the binding of quinoline and phenanthroline analogs to D-lactate dehydrogenase from the barnacle, Balanus nubilus Darwin, does not involve primarily hydrophobic effects. This phenomenon appears to exist also for other lactate dehydrogenases.
D001665:Binding Sites; D001667:Binding, Competitive; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D009243:NAD; D010618:Phenanthrolines / Q000378:metabolism; D011804:Quinolines / Q000378:metabolism; D013329:Structure-Activity Relationship
D010618:Phenanthrolines; D011804:Quinolines; D009243:NAD; D007770:L-Lactate Dehydrogenase