title: Over-expression of pig lung carbonyl reductase in Escherichia coli.
abstract: Tetrameric carbonyl reductase of pig lung has been shown by cDNA cloning to be a member of the short-chain dehydrogenase family of enzymes. Construction of the carbonyl reductase cDNA in an expression vector yielded an abundant, enzymatically active enzyme in Escherichia coli. The recombinant enzyme was purified to homogeneity and shown to be structurally, immunologically and functionally similar to lung carbonyl reductase.
authors.affiliation: Laboratory of Biochemistry, Gifu Pharmaceutical University, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Nakanishi
authors.forename: Y
authors.initials: Y
authors.lastname: Tamada
authors.forename: Y
authors.initials: Y
authors.lastname: Deyashiki
authors.forename: A
authors.initials: A
authors.lastname: Hara
mesh_terms: D000429:Alcohol Oxidoreductases / Q000096:biosynthesis*; D000818:Animals; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics*; D008168:Lung / Q000201:enzymology*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011994:Recombinant Proteins / Q000096:biosynthesis*; D013552:Swine
chemical_list: D011994:Recombinant Proteins; D000429:Alcohol Oxidoreductases