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- W54960425 abstract "New targets are needed to develop antimicrobial therapies to combat M. tuberculosis (Mtb), especially the multi and extremely drug resistant organisms (MDR-TB and XDR-TB). Mycobacteria have been reported to oxidize 3β -hydroxysterols to 3-ketosteroids, but the enzyme(s) responsible for this activity have not been identified in mycobacterial species. Rv3409c, from Mycobacteria tuberculosis H37Rv genome is annotated as choD, a putative cholesterol oxidase. The choD gene was heterologously expressed behind an acetamidase promoter with a C-terminal hexa-histidine tag in Mycobacterium smegmatis mc2 155. Using established cholesterol oxidase assays that follow the formation of the by-product H2O2 or final product cholest-4-en-3-one, there was no cholesterol oxidizing activity detected. The choD gene is also conserved in M. smegmatis, M. leprae and Rhodococcus equi. The M. smegmatis orthologue has 83% amino acid identity with choD from M. tuberculosis. The M. smegmatis choD transposon mutant Myc11 can still catabolize cholesterol. Moreover, Myc11 has significantly different colony morphology than wild-type as observed by light microscopy. The total lipids from both M. smegmatis WT and Myc11 were extracted and analyzed by MALDI-TOF MS and TLC. There are distinct differences between the Myc11 lipid profile and the wild-type lipid profile. Based on our results, we propose that choD is not a cholesterol oxidase, but rather plays a role in lipid cell wall modification or synthesis." @default.
- W54960425 created "2016-06-24" @default.
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- W54960425 date "2008-03-01" @default.
- W54960425 modified "2023-09-26" @default.
- W54960425 title "ChoD Is Important for Lipid Modification in M. smegmatis" @default.
- W54960425 doi "https://doi.org/10.1096/fasebj.22.1_supplement.611.17" @default.
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