title: Three-dimensional structures of human alcohol dehydrogenase isoenzymes reveal the molecular basis for their functional diversity.
authors.affiliation: Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202, USA. hurley@biochem6.iupui.edu
authors.forename: T D
authors.initials: TD
authors.lastname: Hurley
authors.forename: C G
authors.initials: CG
authors.lastname: Steinmetz
authors.forename: P
authors.initials: P
authors.lastname: Xie
authors.forename: Z N
authors.initials: ZN
authors.lastname: Yang
mesh_terms: D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D001665:Binding Sites; D003001:Cloning, Molecular; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012984:Software
chemical_list: D007527:Isoenzymes; D011994:Recombinant Proteins; D000426:Alcohol Dehydrogenase