Localization of 17beta-hydroxysteroid dehydrogenase in Mycobacterium sp. VKM Ac-1815D mutant strain.
The localization of mycobacterial 17beta-hydroxysteroid dehydrogenase (17beta-OH SDH) was studied using cell fractionation and cytochemical investigation. Mycobacterium sp. Et1 mutant strain derived from Mycobacterium sp. VKM Ac-1815D and characterized by increased 17beta-OH SDH activity was used as a model organism. Subcellular distribution study showed both soluble and membrane-bound forms of mycobacterial 17beta-hydroxysteroid dehydrogenase. The cytochemical method based on a copper ferrocyanide procedure followed by electron microscopic visualization was applied in order to investigate the intracellular localization of bacterial 17beta-OH SDH in more detail. The enzyme was found to be located in the peripheral cytoplasmic zone adjoining the cytoplasmic membrane (CM). 17beta-OH SDH was loosely membrane bound and easily released into the environment under the cell integrity failure.
Egorova
O V
OV
G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia. vycherova@ibpm.pushchino.ru
Nikolayeva
V M
VM
Suzina
N E
NE
Donova
M V
MV
D015067:17-Hydroxysteroid Dehydrogenases / Q000032:analysis*; D002458:Cell Fractionation; D042541:Intracellular Space / Q000201:enzymology / Q000648:ultrastructure; D009154:Mutation; D009161:Mycobacterium / Q000201:enzymology* / Q000235:genetics / Q000648:ultrastructure; D013256:Steroids / Q000378:metabolism
D013256:Steroids; D015067:17-Hydroxysteroid Dehydrogenases; C044256:3 (or 17)-beta-hydroxysteroid dehydrogenase