Photo of Will Parsons
  • Assistant Professor of Chemistry and Biochemistry


  • 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 and better understand the biological fates of their substrates.

Fall 2019

  • CHEM 101: Structure and Reactivity in Chemistry (lecture)
  • CHEM 205: Principles of Organic Chemistry (lab)

Spring 2020

  • CHEM 205: Principles of Organic Chemistry (lecture & lab)

  • 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.
  • Hoehne, A.*; Behera, D.*; Parsons, W.H.*; James, M.L.; Shen, B.; Borgohain, P.; Bodapati, D.; Prabhakar, A.; Gambhir, S.S.; Yeomans, D.C.; Biswal, S.; Chin, F.T.; Du Bois, J. “A 18F-saxitoxin derivative for in vivo PET-MR imaging of voltage-gated sodium channel expression following nerve injury.” J. Am. Chem. Soc. 2013, 135, 18012-18015.
  • 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.


This Week in Photos: January 22

January 22, 2020
In this photo series, we explore the art of cinema storytelling; go to an entrepreneurial boot camp; get intense with strings and Greek; go back to high school in Berkeley; stop by the freezer section in Kim’s Grocery & Carryout; get involved with dark matter; learn R for SPSS; join a dance class; design an archeological exhibit; get cozy with a wild beast; and much more.