Quinoprotein alcohol dehydrogenase from ethanol-grown Pseudomonas aeruginosa.
Cell-free extracts of Pseudomonas aeruginosa strains, grown on ethanol, showed dye-linked alcohol dehydrogenase activities. The enzyme responsible for this activity was purified to homogeneity. It appeared to contain two molecules of pyrroloquinoline quinone per enzyme molecule. In many respects, it resembled other quinoprotein alcohol dehydrogenases (EC 1.1.99.8), having a substrate specificity intermediate between that of methanol dehydrogenases and ethanol dehydrogenases in this group. On the other hand, it also showed dissimilarities: the enzyme was found to be a monomer (Mr 101 000), to need only one molecule of the suicide substrate cyclopropanol to become fully inactivated, and to have a different aromatic amino acid composition.
D000429:Alcohol Oxidoreductases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D003067:Coenzymes / Q000378:metabolism; D000431:Ethanol; D004988:Ethers, Cyclic / Q000494:pharmacology; D007700:Kinetics; D045542:PQQ Cofactor; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D011804:Quinolines / Q000378:metabolism
D000596:Amino Acids; D003067:Coenzymes; D004988:Ethers, Cyclic; D011804:Quinolines; C043657:cyclopropanol; D000431:Ethanol; D045542:PQQ Cofactor; D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor)