The coenzyme-binding characteristics of highly purified preparations of sheep liver cytoplasmic aldehyde dehydrogenase.
The binding of NADH and NAD+ by cytoplasmic aldehyde dehydrogenase was studied by various direct and indirect methods. At pH 7.0 at 25 degrees C there appears to be approx. 1 binding site for both nucleotides per 200 000 daltons of protein, although the NAD+-binding results are rather uncertain. Estimates of the dissociation constants of the E . NADH and E . NAD+ complexes under the stated conditions are also presented. Preparations of enzyme are sometimes found to contain significant amounts of very tightly bound NAD+ and NADH. The implications of these findings are discussed.
D000444:Aldehyde Dehydrogenase; D000445:Aldehyde Oxidoreductases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D003593:Cytoplasm / Q000201:enzymology; D005779:Immunodiffusion; D008099:Liver / Q000201:enzymology*; D046911:Macromolecular Substances; D009243:NAD / Q000378:metabolism*; D012756:Sheep; D013050:Spectrometry, Fluorescence
D046911:Macromolecular Substances; D009243:NAD; D000445:Aldehyde Oxidoreductases; D000444:Aldehyde Dehydrogenase