| Autor: |
Sukhodolskaya GV; G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290, Pushchino, Moscow Region, Russia., Nikolayeva VM, Khomutov SM, Donova MV |
| Jazyk: |
angličtina |
| Zdroj: |
Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 2007 Mar; Vol. 74 (4), pp. 867-73. Date of Electronic Publication: 2006 Nov 30. |
| DOI: |
10.1007/s00253-006-0728-4 |
| Abstrakt: |
The strain of Mycobacterium sp. VKM Ac-1817D forms 9alpha-hydroxy-androst-4-ene-3,17-dione (9-OH-AD) as a major product from sitosterol. The formation of 9-OH-AD was accompanied with its partial destruction due to residual steroid-1-dehydrogenase (St1DH) activity. The activity was found to be induced by androst-4-ene-3,17-dione (AD), while other intermediates of sitosterol oxidation did not influence 1(2)-dehydrogenation. The enzyme is located mainly in the cytosolic fraction. The cytosolic St1DH (dimer, M (r) approximately 58 kDa) was partially purified by ammonium sulfate fractionation, ion-exchange chromatography on DEAE-Sepharose and Phenyl-Sepharose, and gel filtration on Bio-Gel A-0.5M. It expressed the St1DH activity toward both AD and 9-OH-AD. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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