Steroid-1-dehydrogenase of Rhodococcus erythropolis: purification and N-terminal amino acid sequence.

The Journal of steroid biochemistry and molecular biology

PubMedID: 1390281

Kaufmann G, Thole H, Kraft R, Atrat P. Steroid-1-dehydrogenase of Rhodococcus erythropolis: purification and N-terminal amino acid sequence. J Steroid Biochem Mol Biol. 1992;43(4):297-301.
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.