Reference on EC 1.14.15.30 - 3-ketosteroid 9alpha-monooxygenase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wei, W.; Fan, S.; Wang, F.; Wei, D.
A new steroid-transforming strain of Mycobacterium neoaurum and cloning of 3-ketosteroid 9alpha-hydroxylase in NwIB-01
Appl. Biochem. Biotechnol.
162
1446-1456
2010
Mycolicibacterium neoaurum (C9E9N6), Mycolicibacterium neoaurum NwIB-01 (C9E9N6)
Hu, Y.; Van Der Geize, R.; Besra, G.; Gurcha, S.; Liu, A.; Rohde, M.; Singh, M.; Coates, A.
3-Ketosteroid 9alpha-hydroxylase is an essential factor in the pathogenesis of Mycobacterium tuberculosis
Mol. Microbiol.
75
107-121
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Andor, A.; Jekkel, A.; Hopwood, D.; Jeanplong, F.; Ilkoy, .; Kónya, A.; Kurucz, I.; Ambrus, G.
Generation of useful insertionally blocked sterol degradation pathway mutants of fast-growing mycobacteria and cloning, characterization, and expression of the terminal oxygenase of the 3-ketosteroid 9alpha-hydroxylase in Mycobacterium smegmatis mc2155
Appl. Environ. Microbiol.
72
6554-6559
2006
Mycolicibacterium smegmatis (Q27W16), Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (Q27W16)
Van Der Geize, R.; Hessels, G.; Nienhuis-Kuiper, M.; Dijkhuizen, L.
Characterization of a second Rhodococcus erythropolis SQ1 3-ketosteroid 9alpha-hydroxylase activity comprising a terminal oxygenase homologue, KshA2, active with oxygenase-reductase component KshB
Appl. Environ. Microbiol.
74
7197-7203
2008
Rhodococcus erythropolis (B2ZFP6), Rhodococcus erythropolis (B5TYS8), Rhodococcus erythropolis, Rhodococcus erythropolis SQ1 (B2ZFP6), Rhodococcus erythropolis SQ1 (B5TYS8), Rhodococcus erythropolis SQ1
Fan, S.; Wei, W.; Wang, F.; Wei, D.
Cloning, heterologous expression and purification of a 3-ketosteroid-9alpha-hydroxylase (KSH) from Mycobacterium sp. NwIB-01
Chin. J. Biotechnol.
25
2014-2021
2009
Mycobacterium sp., Mycobacterium sp. NwIB-01
Petrusma, M.; Hessels, G.; Dijkhuizen, L.; van der Geize, R.
Multiplicity of 3-ketosteroid-9alpha-hydroxylase enzymes in Rhodococcus rhodochrous DSM43269 for specific degradation of different classes of steroids
J. Bacteriol.
193
3931-3940
2011
Rhodococcus rhodochrous (B6V6V5), Rhodococcus rhodochrous (F1CMX0), Rhodococcus rhodochrous (F1CMX3), Rhodococcus rhodochrous (F1CMX6), Rhodococcus rhodochrous (F1CMX8), Rhodococcus rhodochrous (F1CMY8), Rhodococcus rhodochrous, Rhodococcus rhodochrous DSM 43269 (B6V6V5), Rhodococcus rhodochrous DSM 43269 (F1CMX0), Rhodococcus rhodochrous DSM 43269 (F1CMX3), Rhodococcus rhodochrous DSM 43269 (F1CMX6), Rhodococcus rhodochrous DSM 43269 (F1CMX8), Rhodococcus rhodochrous DSM 43269 (F1CMY8), Rhodococcus rhodochrous DSM 43269
Petrusma, M.; Dijkhuizen, L.; van Der Geize, R.
Structural features in the KshA terminal oxygenase protein that determine substrate preference of 3-ketosteroid 9alpha-hydroxylase enzymes
J. Bacteriol.
194
115-121
2012
Rhodococcus rhodochrous (F1CMX0), Rhodococcus rhodochrous (F1CMX3), Rhodococcus rhodochrous (F1CMY8), Rhodococcus rhodochrous DSM 43269 (F1CMX0), Rhodococcus rhodochrous DSM 43269 (F1CMX3), Rhodococcus rhodochrous DSM 43269 (F1CMY8), Rhodococcus rhodochrous DSM 43269
Capyk, J.; DAngelo, I.; Strynadka, N.; Eltis, L.
Characterization of 3-ketosteroid 9alpha-hydroxylase, a Rieske oxygenase in the cholesterol degradation pathway of Mycobacterium tuberculosis
J. Biol. Chem.
284
9937-9946
2009
Mycobacterium tuberculosis (P71875), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P71875)
Capyk, J.; Casabon, I.; Gruninger, R.; Strynadka, N.; Eltis, L.
Activity of 3-ketosteroid 9alpha-hydroxylase (KshAB) indicates cholesterol side chain and ring degradation occur simultaneously in Mycobacterium tuberculosis
J. Biol. Chem.
286
40717-40724
2011
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P71875), Mycobacterium tuberculosis (P9WJ93), Mycobacterium tuberculosis H37Rv (P71875), Mycobacterium tuberculosis H37Rv (P9WJ93)
Van Der Geize, R.; Hessels, G.; Van Gerwen, R.; Van Der Meijden, P.; Dijkhuizen, L.
Molecular and functional characterization of kshA and kshB, encoding two components of 3-ketosteroid 9alpha-hydroxylase, a class IA monooxygenase, in Rhodococcus erythropolis strain SQ1
Mol. Microbiol.
45
1007-1018
2002
Rhodococcus erythropolis (Q8KQH9), Rhodococcus erythropolis (Q8KQI0), Rhodococcus erythropolis SQ1 (Q8KQH9), Rhodococcus erythropolis SQ1 (Q8KQI0)
Yao, K.; Xu, L.Q.; Wang, F.Q.; Wei, D.Z.
Characterization and engineering of 3-ketosteroid-Delta1-dehydrogenase and 3-ketosteroid-9alpha-hydroxylase in Mycobacterium neoaurum ATCC 25795 to produce 9alpha-hydroxy-4-androstene-3,17-dione through the catabolism of sterols
Metab. Eng.
24
181-191
2014
Mycolicibacterium neoaurum (C9E9N6), Mycolicibacterium neoaurum NwIB-01 (C9E9N6), Mycolicibacterium neoaurum ATCC 25795 (C9E9N6)
Petrusma, M.; van der Geize, R.; Dijkhuizen, L.
3-Ketosteroid 9alpha-hydroxylase enzymes Rieske non-heme monooxygenases essential for bacterial steroid degradation
Antonie van Leeuwenhoek
106
157-172
2014
Mycolicibacterium smegmatis, Rhodococcus erythropolis, Rhodococcus rhodochrous, Rhodococcus jostii, Rhodococcus jostii (Q0RXD9), Rhodococcus jostii (Q0S812), Mycobacterium tuberculosis (P71875), Mycolicibacterium smegmatis mc2 155, Rhodococcus erythropolis SQ1, Mycobacterium tuberculosis H37Rv (P71875), Rhodococcus rhodochrous DSM 43269
Penfield, J.S.; Worrall, L.J.; Strynadka, N.C.; Eltis, L.D.
Substrate specificities and conformational flexibility of 3-ketosteroid 9alpha-hydroxylases
J. Biol. Chem.
289
25523-25536
2014
Rhodococcus rhodochrous (F1CMX0), Rhodococcus rhodochrous (F1CMY8), Mycobacterium tuberculosis (P71875), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P71875), Rhodococcus rhodochrous DSM 43269 (F1CMX0), Rhodococcus rhodochrous DSM 43269 (F1CMY8), Rhodococcus rhodochrous DSM 43269
Guevara, G.; Heras, L.F.L.; Perera, J.; Llorens, J.M.N.
Functional characterization of 3-ketosteroid 9alpha-hydroxylases in Rhodococcus ruber strain chol-4
J. Steroid Biochem. Mol. Biol.
172
176-187
2017
Rhodococcus ruber, Rhodococcus ruber (I0B6I9), Rhodococcus ruber Chol-4, Rhodococcus ruber Chol-4 (I0B6I9)
Yeh, C.H.; Kuo, Y.S.; Chang, C.M.; Liu, W.H.; Sheu, M.L.; Meng, M.
Deletion of the gene encoding the reductase component of 3-ketosteroid 9alpha-hydroxylase in Rhodococcus equi USA-18 disrupts sterol catabolism, leading to the accumulation of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid and 1,4-androstadiene-3,17-dione
Microb. Cell Fact.
13
130
2014
Rhodococcus equi (A0A060CNE1), Rhodococcus equi 103S (A0A060CNE1)
Zhang, X.; Rao, Z.; Zhang, L.; Xu, M.; Yang, T.
Efficient 9alpha-hydroxy-4-androstene-3,17-dione production by engineered Bacillus subtilis co-expressing Mycobacterium neoaurum 3-ketosteroid 9alpha-hydroxylase and B. subtilis glucose 1-dehydrogenase with NADH regeneration
SpringerPlus
5
1207
2016
Mycolicibacterium neoaurum (A0A0F7JI94 AND D2Y640), Mycolicibacterium neoaurum JC-12 (A0A0F7JI94 AND D2Y640)
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