title: Genesis of Drosophila ADH: the shaping of the enzymatic activity from a SDR ancestor.
abstract: Drosophila alcohol dehydrogenase (ADH) is an NAD(H)-dependent oxidoreductase that catalyzes the oxidation of alcohols and aldehydes. Structurally and biochemically distinct from all the reported ADHs (typically, the mammalian medium-chain dehydrogenase/reductase-ethanol-metabolizing enzyme), it stands as the only small-alcohol transforming system that has originated from a short-chain dehydrogenase/reductase (SDR) ancestor. The crystal structures of the apo, binary (E.NAD(+)) and three ternary (E.NAD(+).acetone, E.NAD(+).3-pentanone and E.NAD(+).cyclohexanone) forms of Drosophila lebanonensis ADH have allowed us to infer the structural and kinetic features accounting for the generation of the ADH activity within the SDR lineage.
authors: Center for Structural Biochemistry, Karolinska Institutet, Hälsovägen 7, 141 57, Huddinge, Sweden.
authors: J
authors: J
authors: Benach
authors: S
authors: S
authors: Atrian
authors: R
authors: R
authors: Ladenstein
authors: R
authors: R
authors: Gonzàlez-Duarte
mesh_terms: D000426:Alcohol Dehydrogenase; D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D000438:Alcohols / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D020134:Catalytic Domain; D019281:Dimerization; D004330:Drosophila / Q000201:enzymology* / Q000235:genetics*; D029721:Drosophila Proteins; D019143:Evolution, Molecular; D008958:Models, Molecular; D009243:NAD / Q000378:metabolism; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D000438:Alcohols; D029721:Drosophila Proteins; D009243:NAD; D000429:Alcohol Oxidoreductases; C073796:ADH protein, Drosophila; D000426:Alcohol Dehydrogenase