Description
- Abstract:
- The S-palmitoylated signal-transducing rat sarcoma GTPase (Ras), which plays important roles in cellular growth, division, and differentiation, is frequently mutated in various types of cancer. Dynamic palmitoylation and depalmitoylation of Ras confers proper localization and signaling in cells. So far, only two enzymes have been characterized as being involved in depalmitoylation: including acyl protein thioesterase 1 and acyl protein thioesterase 2. To decipher the physiological functions of the enzymes involved in S-depalmitoylation, we have designed a clickable activity-based probe for acyl protein thioesterases. The probe consists of a palmitoylated serine substrate linked to a trapping moiety that becomes reactive after enzymatic hydrolysis. This activity-based probe is critical for profiling the activities of thioesterases in biological systems and for inhibitor screening.
- Notes:
- Thesis (Ph.D. -- Brown University (2016)
Access Conditions
- Rights
- In Copyright
- Restrictions on Use
- Collection is open for research.
Citation
Chen, Yiming,
"AN ACTIVITY-BASED PROBE FOR THE ACYL PROTEIN THIOESTERASES"
(2016).
Chemistry Theses and Dissertations.
Brown Digital Repository. Brown University Library.
https://doi.org/10.7301/Z0PC30SH
