- PhD, Stanford University, 2013
- BA, Williams College, 2007
Chemical biology, small-molecule synthesis, intramembrane hydrolases
Enzyme-mediated hydrolysis is a ubiquitous component of numerous metabolic pathways in the body. Nature has developed a number of chemistries within hydrolase active sites to cleave a diverse array of biological substrates. The Parsons lab studies enzymes that use serine and threonine residues to catalyze turnover of their substrates. A subset of these enzymes with intramembrane active sites are of particular interest due to their unique biochemistry as well as their involvement in pathways underlying metabolic and neurological diseases, including Parkinson’s disease and type 2 diabetes.
The Parsons lab exploits the active site chemistry of these hydrolases to create new chemical probes for this enzyme class. Drawing upon methodology from synthetic chemistry, biochemistry, molecular biology, and medicinal chemistry, research in the Parsons lab focuses on the development of small molecule tools to study the physiological roles of intramembrane hydrolases.
- Ertunc, M.E.; Kok, B.P.; Parsons, W.H.; Wang, J.G.; Tan, D.; Donaldson, C. J.; Pinto, A.F.M.; Vaughan, J.M.; Ngo, N.; Lum, K.M.; Henry, C.L., Coppola, A.R.; Niphakis, M.J.; Cravatt, B.F.; Saez, E.; Saghatelian, A. “AIG1 and ADTRP are endogenous FAHFA hydrolases.” J. Biol. Chem. 2020, 295, 5891–5905.
- Chen, A.L.; Lum, K.M.; Lara-Gonzalez, P.; Ogasawara, D.; Cognetta, A.B.; To, A.; Parsons, W.H.; Simon, G.M.; Desai, A.; Petrascheck, M.; Bar-Peled, L.; Cravatt, B.F. “Pharmacological convergence reveals a lipid pathway that regulates C. elegans lifespan.” Nat. Chem. Biol. 2019, 15, 453–462.
- Ogura, Y.; Parsons, W.H.; Kamat, S.S.; Cravatt, B.F. “A calcium-dependent acyltransferase that produces N-acyl phosphatidylethanolamines.” Nat. Chem. Biol. 2016, 12, 669-671.
- Parsons, W.H.*; Kolar, M.J.*; Kamat, S.S.; Cognetta, III, A.B.; Hulce, J.J.; Saez, E.; Kahn, B.B; Saghatelian, A.; Cravatt, B.F. “AIG1 and ADTRP are atypical integral membrane hydrolases that degrade bioactive FAHFAs.” Nat. Chem. Biol. 2016, 12, 367-372.
- Parsons, W.H.; Du Bois, J. “Maleimide conjugates of saxitoxin as covalent inhibitors of voltage-gated sodium channels.” J. Am. Chem. Soc. 2013, 135, 10582-10585.