title: Properties and evolution of an alcohol dehydrogenase from the Crenarchaeota Pyrobaculum aerophilum.
abstract: The gene encoding a novel alcohol dehydrogenase (ADH) that belongs to the medium chain dehydrogenase/reductase (MDR) superfamily was identified in the hyperthermophilic archaeon, Pyrobaculum aerophilum. The P. aerophilum ADH gene (Pae2687) was over-expressed in Escherichia coli, and the protein (PyAeADHII) was purified to homogeneity and characterized. The PyAeADHII belongs to a medium chain class because its monomer size is 330 residues and even if it is structurally similar to other enzymes belonging to MDR superfamily, it lacks key residues involved in the coordination of the catalytic Zn ion and in the binding of alcoholic substrates typical of other ADHs. Consistently, PyAeADHII does not show activity on a large number of alcohols, aldheydes or ketones. It is active only when alpha-tetralone is used as a substrate. The enzyme has a strict requirement for NADP(H) as the coenzyme and has remarkable thermophilicity, displaying activity at temperatures up to 95 degrees C. The study of the metabolic pathways of P. aerophilum can provide information on the evolution of genes and enzymes and may be crucial for understanding the evolution of eukaryotic cells.
authors.affiliation: Laboratory for Molecular Sensing, IBP-CNR, Naples, Italy.
authors.forename: Annalisa
authors.initials: A
authors.lastname: Vitale
authors.forename: Francesco
authors.initials: F
authors.lastname: Rosso
authors.forename: Alfonso
authors.initials: A
authors.lastname: Barbarisi
authors.forename: Tullio
authors.initials: T
authors.lastname: Labella
authors.forename: Sabato
authors.initials: S
authors.lastname: D'Auria
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D000595:Amino Acid Sequence; D019143:Evolution, Molecular; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D041543:Pyrobaculum / Q000201:enzymology*; D011994:Recombinant Proteins / Q000378:metabolism; D016415:Sequence Alignment; D013696:Temperature
chemical_list: D011994:Recombinant Proteins; D000426:Alcohol Dehydrogenase