PMID: 8586617May 1, 1995Paper

Purification and characterization of the 3-ketosteroid-delta 1-dehydrogenase of Arthrobacter simplex produced in Streptomyces lividans

Journal of Biochemistry
K P ChoiY Murooka

Abstract

The 3-ketosteroid-delta 1-dehydrogenase (KS1DH) gene of Arthrobacter simplex IFO12069 cloned in Streptomyces lividans was overexpressed, resulting in production of the enzyme both extracellularly and intracellularly. The enzyme was purified by ammonium sulfate fractionation and chromatographies using DEAE-Toyopearl, Butyl-Toyopearl and Toyopearl HW55S from the supernatant of culture broth and cell-free extracts of S. lividans, and both preparations showed the same characteristics. The N-terminal amino acid sequence of both KS1DHs was M-D-W-A-E-E-Y-D, which coincided with the amino acid sequence deduced from the nucleotide sequence. Thus, the extracellular enzyme may derived from leakage of S. lividans cells during cultivation rather than secretion by processing of the signal sequence. The molecular weight of the enzyme was about 55,000, identical with the size deduced from the nucleotide sequence (M(r) 54,329). The optimum conditions for its activity were pH 10.0 and 40 degrees C. The enzyme catalyzed the conversion of several 3-keto-steroids, but those containing 11 alpha- or 11 beta-hydroxyl group were converted at low rates. The amino acid sequence of KS1DH from A. simplex is similar to those of KS1DH of Pseudomonas testoste...Continue Reading

Citations

Feb 4, 2009·Applied Biochemistry and Biotechnology·Liting ZhangJianmei Luo
Jun 22, 2017·Applied Microbiology and Biotechnology·Xiaojun WangYanhe Ma
Apr 28, 2019·Applied Microbiology and Biotechnology·T G LobastovaM V Donova
Nov 13, 2007·Applied and Environmental Microbiology·Yin-Ru ChiangGeorg Fuchs
Oct 31, 2014·Journal of Chemical Ecology·Nicholas S JohnsonWeiming Li
Apr 7, 2021·Biotechnology Advances·Ali Rohman, Bauke W Dijkstra

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