Elucidation of activities and structure-function relationships for lipid biosynthetic enzymes from Mycobacterium tuberculosis
EMSL Project ID
47783
Abstract
The goal of this Rapid Access proposal is to test our hypotheses about the function and structure-activity relationships of lipid biosynthetic enzymes in M. tuberculosis . Mycobacteria adapt the structure and composition of their cellular membranes depending on nutrient availability. Our ability to understand how mycobacterial metabolism responds to environmental cues is limited by incomplete and sometimes incorrect functional gene annotation. Assigning enzymatic steps in lipid biosynthesis is a key step in creating a complete map of metabolic pathways and networks. This map will in turn help us achieve a systems-level understanding of how these microbes regulate their membranes in response to environmental insults or limitations. Our analysis of lipids from enzymatic reactions or bacterial extracts has been limited to shotgun lipidomics. Because the detection of low-abundance species suffers from ion suppression and lack of sensitivity, LC-MS/MS is required to assign putative intermediates. EMSL offers the ideal combination of user access and lipidomics expertise to achieve our goals.
Project Details
Project type
Limited Scope
Start Date
2013-02-11
End Date
2013-04-13
Status
Closed
Released Data Link
Team
Principal Investigator
Related Publications
Touchette MH, GR Bommineni, RJ Delle Bovi, J Gadbery, CD Nicora, AK Shukla, JE Kyle, TO Metz, DW Martin, NS Sampson, WT Miller, PJ Tonge, and JC Seeliger. 2015. "Diacyltransferase Activity and Chain Length Specificity of Mycobacterium tuberculosis PapA5 in the Synthesis of Alkyl ?-Diol Lipids." Biochemistry 54(35):5457-5468. doi:10. 1021/acs. biochem. 5b00455