title: Tetrameric NAD-dependent alcohol dehydrogenase.
abstract: Three-dimensional structures of the ethanol-induced, tetrameric alcohol dehydrogenase from Escherichia coli have recently been determined in the absence and presence of NAD. The structure of the E. coli enzyme is similar to those of the dimeric mammalian alcohol dehydrogenases, but it has a deletion of 21 residues located at the surface of the catalytic domain. The catalytic zinc ions have two different types of coordination, which are also observed in the class III dimeric mammalian alcohol dehydrogenase. Comparison of the structures provide new insights into the relationship between tetrameric and dimeric alcohol dehydrogenases and provide a link to the structure of the tetrameric yeast alcohol dehydrogenase.
authors.affiliation: Department of Molecular Biology, Swedish University of Agricultural Sciences, S-751 24, Uppsala, Sweden.
authors.forename: Andreas
authors.initials: A
authors.lastname: Karlsson
authors.forename: Mustapha
authors.initials: M
authors.lastname: El-Ahmad
authors.forename: Kenth
authors.initials: K
authors.lastname: Johansson
authors.forename: Jawed
authors.initials: J
authors.lastname: Shafqat
authors.forename: Hans
authors.initials: H
authors.lastname: Jörnvall
authors.forename: Hans
authors.initials: H
authors.lastname: Eklund
authors.forename: S
authors.initials: S
authors.lastname: Ramaswamy
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry / Q000378:metabolism*; D000595:Amino Acid Sequence; D001704:Biopolymers / Q000737:chemistry / Q000378:metabolism; D002384:Catalysis; D004926:Escherichia coli / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009243:NAD / Q000378:metabolism*; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D015032:Zinc / Q000378:metabolism
chemical_list: D001704:Biopolymers; D009243:NAD; D000426:Alcohol Dehydrogenase; D015032:Zinc