Simian liver alcohol dehydrogenase: isolation and characterization of isoenzymes from Macaca mulatta.
Like human liver alcohol dehydrogenase, that of Macaca mulatta can be purified and separated into anodic and cathodic pyrazole-insensitive and cathodic pyrazole-sensitive enzyme forms. Their inhibition by 4-methylpyrazole and their substrate specificities are analogous to those observed for the corresponding isoenzymes of human liver. However, on the basis of data available so far, the physiochemical and compositional characteristics, i.e., molecular weight, zinc content, and dimeric structure, of all simian alcohol dehydrogenase forms are virtually identical with those of other mammalian alcohol dehydrogenases studied up to now. Zinc is essential for their enzymatic function, as demonstrated by inhibition with chelating agents.
D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000302:isolation & purification* / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002614:Chelating Agents / Q000494:pharmacology; D002942:Circular Dichroism; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000302:isolation & purification* / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D008253:Macaca mulatta; D008970:Molecular Weight; D011487:Protein Conformation; D015032:Zinc / Q000032:analysis
D000596:Amino Acids; D002614:Chelating Agents; D007527:Isoenzymes; D000429:Alcohol Oxidoreductases; D000426:Alcohol Dehydrogenase; D015032:Zinc