Appl Microbiol Biotechnol
Donova MV, Egorova OV (2012) Microbial steroid transformations: cur-
rent state and prospects. Appl Microbiol Biotechnol 94(6):1423–
1447
El-Hadi AA (2003) Production of prednisolone by Bacillus pumilus E601
cells incorporated in radiation induced poly(vinyl alcohol g-2
hydroxyethylmethacrylate) cryogels. Process Biochem 38(12):
1653–1657
Fernandes P, Cruz A, Angelova B, Pinheiro HM, Cabral JMS (2003)
Microbial conversion of steroid compounds: recent developments.
Enzyme Microb Tech 32(6):688–705
known to catalyze the introduction of double bonds into ste-
roids. Further studies are desired to understand the reaction
mechanisms of double-bond formation by these enzymes,
which may facilitate their utilization in biosynthesis of medi-
cally important steroidal compounds. It is anticipated that fur-
ther research in this aspect and additional biocatalyst improve-
ment by mutagenesis may facilitate the full potential of KstD
in steroid production.
Fokina VV, Donova MV (2003) 21-Acetoxy-pregna-4(5),9(11),16(17)-
triene-21-ol-3,20-dione conversion by Nocardioides simplex VKM
ac-2033D. J Steroid Biochem Mol Biol 87(4–5):319–325
Fokina VV, Sukhodolskaya GV, Baskunov BP, Turchin KF, Grinenko
GS, Donova MV (2003) Microbial conversion of pregna-4,9(11)-
diene-17α,21- diol-3,20-dione acetates by Nocardioides simplex
VKM Ac-2033D. Steroids 68(5):415–421
van der Geize R, Hessels GI, van Gerwen R, Vrijbloed JW, van der
Meijden P, Dijkhuizen L (2000) Targeted disruption of the KstD
gene encoding a 3-ketosteroid Δ1-dehydrogenase isoenzyme of
Rhodococcus erythropolis strain SQ1. Appl Environ Microbiol
66(5):2029–2036
Acknowledgements This work was financially supported by the STS
Program of Chinese Academy of Sciences (KFJ-SW-STS-164) and the
National High Technology Research and Development Program
(B863^Program) of China (Nos. 02011AA02A211). The authors thank
the sponsorship from Zhejiang Xianju Junye Pharmaceutical Co., Ltd.
(Zhejiang, China), and greatly appreciate Professor Peter Lau at the same
institute for his help and constructive suggestions on this manuscript.
Compliance with ethical standards This article does not contain any
studies with human participants or animals performed by the authors.
van der Geize R, Hessels GI, Dijkhuizen L (2002) Molecular and func-
tional characterization of the kstD2 gene of Rhodococcus
erythropolis SQ1 encoding a second 3-ketosteroid Δ1-dehydroge-
nase isoenzyme. Microbiology 148(10):3285–3292
Conflict of interest The authors declare that they have no conflict of
interest.
Grote A, Hiller K, Scheer M, Munch R, Nortemann B, Hempel DC, Jahn
D (2005) JCat: a novel tool to adapt codon usage of a target gene to
its potential expression host. Nucleic Acids Res 33:526–531
de las Heras LF, van der Geize R, Drzyzga O, Perera J, Navarro Llorens
JM (2012) Molecular characterization of three 3-ketosteroid-Δ1-de-
hydrogenase isoenzymes of Rhodococcus ruber strain Chol-4. J
Steroid Biochem Mol Biol 132(3–5):271–281
Itagaki E, Hatta T, Wakabayashi T, Suzuki K (1990a) Spectral properties
of 3-ketosteroid-Δ1-dehydrogenase from Nocardia corallina.
Biochim Biophys Acta 1040:281–286
Itagaki E, Wakabayashi T, Hatta T (1990b) Purification and characteriza-
tion of 3-ketosteroid-Δ1-dehydrogenase from Nocardia corallina.
Biochim Biophys Acta 1038:60–67
Jing Y, Xu CG, Ding K, Lin JR, Jin RH, Tian WS (2010) Protecting group
effect on the 1,2-dehydrogenation of 19-hydroxysteroids: a highly
efficient protocol for the synthesis of estrogens. Tetrahedron Lett
51(24):3242–3245
Kaul R, Mattiasson B (1986) Extractive bioconversion in aqueous two-
phase systems. Appl Microbiol Biotechnol 24(4):259–265
Knol J, Bodewits K, Hessels GI, Dijkhuizen L, van der Geize R (2008) 3-
Keto-5α-steroid Δ1-dehydrogenase from Rhodococcus erythropolis
SQ1 and its orthologue in Mycobacterium tuberculosis H37Rv are
highly specific enzymes that function in cholesterol catabolism.
Biochem J 410(2):339–346
Marcos-Escribano A, Bermejo FA, Bonde-Larsen AL, Retuerto JI, Sierra
IH (2009) 1,2-Dehydrogenation of steroidal 6-methylene deriva-
tives. Synthesis of exemestane. Tetrahedron 65(36):7587–7590
Morii S, Fujii C, Miyoshi T, Iwami M, Itagaki E (1998) 3-Ketosteroid-
Δ1-dehydrogenase of Rhodococcus rhodochrous: sequencing of the
genomic DNA and hyperexpression, purification, and characteriza-
tion of the recombinant enzyme. J Biochem 124(5):1026–1032
Plesiat P, Grandguillot M, Harayama S, Vragar S, Michel-Briand Y
(1991) Cloning, sequencing, and expression of the Pseudomonas
testosteroni gene encoding 3-oxosteroid Δ1-dehydrogenase. J
Bacteriol 173(22):7219
References
Adham NZ, El-Hady AA, Naim N (2003) Biochemical studies on the
microbial Δ1-dehydrogenation of cortisol by Pseudomonas
fluorescens. Process Biochem 38(6):897–902
Arinbasarova AGM, Akimenko VK, Koshcheyenko KA, Skryabin GK
(1985) Redox reactions in hydrocortisone transformation by
Arthrobacter globiformis cells. J Steroid Biochem 23:307–312
Bhatti HN, Khera RA (2012) Biological transformations of steroidal
compounds: a review. Steroids 77(12):1267–1290
Bredehoft M, Baginski R, Parr MK, Thevis M, Schanzer W (2012)
Investigations of the microbial transformation of cortisol to prednis-
olone in urine samples. J Steroid Biochem Mol Biol 129(1–2):54–
60
Carballeira JD, Quezada MA, Hoyos P, Simeó Y, Hernaiz MJ, Alcantara
AR, Sinisterra JV (2009) Microbial cells as catalysts for
stereoselective red-ox reactions. Biotechnol Adv 27(6):686–714
Chen K, Liu C, Deng L, Xu G (2010) A practical Δ1-dehydrogenation of
Δ4-3-keto-steroids with DDQ in the presence of TBDMSCl at room
temperature. Steroids 75(7):513–516
Chen MM, Wang FQ, Lin LC, Yao K, Wei DZ (2012) Characterization
and application of fusidane antibiotic biosynethsis enzyme 3-keto-
steroid-Δ1-dehydrogenase in steroid transformation. Appl
Microbiol Biotechnol 96(1):133–142
Chiang YR, Ismail W, Gallien S, Heintz D, Van Dorsselaer A, Fuchs G
(2008) Cholest-4-en-3-one-Δ1-dehydrogenase, a flavoprotein cata-
lyzing the second step in anoxic cholesterol metabolism. Appl
Environ Microbiol 74(1):107–113
Choi KP, Molnár I, Yamashita M, Murooka Y (1995a) Purification and
characterization of the 3-ketosteroid-Δ1-dehydrogenase of
Arthrobacter simplex produced in Streptomyces liuidans. J
Biochem 117:1043–1049
Choi KP, Murooka Y, Molnár I (1995b) Secretory overproduction of
Arthrobacter simplex 3-ketosteroid Δ1-dehydrogenase by
Streptomyces lividans with a multi-copy shuttle vector. Appl
Microbiol Biotechnol 43:1044–1049
Rohman A, van Oosterwijk N, Thunnissen AM, Dijkstra BW (2013)
Crystal structure and site-directed mutagenesis of 3-ketosteroid
Δ1-dehydrogenase from Rhodococcus erythropolis SQ1 explain its
catalytic mechanism. J Biol Chem 288(49):35559–35568
Donova MV (2007) Transformation of steroids by actinobacteria: a re-
view. Appl Biochem Microbiol 43(1):1–14