| Autor: |
Ravindran, Madhu Sudhan, Rao, Srinivasa P.S., Cheng, Xiamin, Shukla, Ankit, Cazenave-Gassiot, Amaury, Yao, Shao Q., Wenk, Markus R. |
| Zdroj: |
Molecular and Cellular Proteomics (MCP Online); February 2014, Vol. 13 Issue: 2 p435-448, 14p |
| Abstrakt: |
Tetrahydrolipstatin (THL) is bactericidal but its precise target spectrum is poorly characterized. Here, we used a THL analog and activity-based protein profiling to identify target proteins after enrichment from whole cell lysates of Mycobacterium bovisBacillus Calmette-Guérin cultured under replicating and non-replicating conditions. THL targets α/β-hydrolases, including many lipid esterases (LipD, G, H, I, M, N, O, V, W, and TesA). Target protein concentrations and total esterase activity correlated inversely with cellular triacylglycerol upon entry into and exit from non-replicating conditions. Cellular overexpression of lipHand tesAled to decreased THL susceptibility thus providing functional validation. Our results define the target spectrum of THL in a biological species with particularly diverse lipid metabolic pathways. We furthermore derive a conceptual approach that demonstrates the use of such THL probes for the characterization of substrate recognition by lipases and related enzymes. |
| Databáze: |
Supplemental Index |
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