Structural and biochemical characterization of thioesterases from pathogenic bacteria

Yogesh Khandokar

Research output: ThesisDoctoral Thesis


belongs to the TE11 family, and favours butyryl-CoA as a substrate. This study identifies residues Asn28, Asp43 and Thr60 as essential for the optimal activity, and Asn28 is a key residue in stabilising the hexameric assembly. This study also reports a common inhibitor of all SaACTs studied here, disulfide CoA and demonstrates a mechanism of inhibition through x-ray crystallographic structure determination.Finally, the thioesterase study from Neisseria meningitidis (NmACH) reports NmACH is a hexameric hotdog thioesterase and exhibits two binding domains for acetyl-CoA and GDP. Both Asn24 and Asp39 are crucial residues for activity of NmACH, and Arg93 and Arg138 are key residues for the GDP stability in the GDP binding domain. A novel mechanism has been explained in this study that indicates GDP enhances the activity of NmACH instead of inhibition. Overall, this thesis reports novel structural, functional and regulatory aspects of a number of families of thioesterases that will assist to understand importance of thioesterases as a potential drug target.
Original languageEnglish
QualificationDoctor of Philosophy
Awarding Institution
  • Charles Sturt University
Place of PublicationAustralia
Publication statusPublished - 2016

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