Kinetics and thermodynamics of ethanol oxidation catalyzed by genetic variants of the alcohol dehydrogenase from Drosophila melanogaster and D. simulans

• Published in: Biochimica et biophysica acta Vol. 967; no. 2; pp. 224 - 233
• Main Authors: Heinstra, P.W.H, Thorig, G.E.W, Scharloo, W, Drenth, W, Nolte, R.J.M
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier 17.11.1988; North-Holland
• Subjects: alcohol dehydrogenase; Alcohol Dehydrogenase - genetics; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Drosophila; Drosophila - enzymology; Drosophila - genetics; Drosophila melanogaster; Drosophila melanogaster - enzymology; Drosophila melanogaster - genetics; Enzymes and enzyme inhibitors; Ethanol - metabolism; evolution; Fundamental and applied biological sciences. Psychology; genetic variation; Isoenzymes - genetics; Isoenzymes - metabolism; Kinetics; Oxidation-Reduction; Oxidoreductases; Thermodynamics; Purification; Ethanol; Enzyme; Insecta; Enthalpy; Primary structure; Entropy; Alcohol dehydrogenase; Drosophilidae; Thermodynamics; Arthropoda; Oxidation; Kinetics; Invertebrata; Drosophila melanogaster; Diptera

Four naturally occurring variants of the alcohol dehydrogenase enzyme (ADH; EC 1.1.1.1) from Drosophila melanogaster and D. simulans, with different primary structures, have been subjected to kinetic studies of ethanol oxidation at five temperatures. Two amino acid replacements in the N-terminal reg...