title: Steroid-1-dehydrogenase of Rhodococcus erythropolis: purification and N-terminal amino acid sequence.
abstract: The inducible steroid-1-dehydrogenase from the bacterium Rhodococcus erythropolis IMET 7030 was purified to homogeneity using affinity chromatographic, electrophoretic, and ion exchange techniques. The spectrum of the pure enzyme is characterized by the associated FAD. The M(r) of the enzyme is 56,000. The amino acid composition and the sequence of the 13 N-terminal amino acids are given.
authors.affiliation: Institute of Microbiology and Experimental Therapy, Jena, Germany.
authors.forename: G
authors.initials: G
authors.lastname: Kaufmann
authors.forename: H
authors.initials: H
authors.lastname: Thole
authors.forename: R
authors.initials: R
authors.lastname: Kraft
authors.forename: P
authors.initials: P
authors.lastname: Atrat
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D012240:Rhodococcus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D010088:Oxidoreductases; C022656:3-oxosteroid delta(1) dehydrogenase