Ethan Guth

Ethan Guth

  • Associate Dean, College of Arts and Sciences
  • Chair, Chemistry and Biochemistry
  • Associate Professor

About

Dr. Ethan Guth is an Associate Professor and the Chair of the Chemistry & Biochemistry Department at Norwich University. He earned a Ph.D. in Biochemistry from the University of Vermont College of Medicine and a B.S. in Biochemistry from Goucher College. Since joining Norwich in 2011, he has taught courses ranging from Introduction to General Chemistry and Organic Chemistry to Biochemistry I & II.

Dr. Guth’s research centers on the intricate mechanism of enzyme catalysis. Early in his career, he dissected individual steps within the catalytic cycle; more recently, his work examines how subtle alterations in enzyme function impact cellular and whole-organism biology. A focal point of his work has been the human histidyl–tRNA synthetase (HARS), investigating how clinically relevant mutations affect its activity and stability.

Most notably, Dr. Guth contributed to a landmark 2017 study revealing that a mutation linked to Usher Syndrome IIIB — a disorder characterized by late-developing deafness and retinal degeneration — results in a HARS variant that, while retaining catalytic activity, is notably less thermostable. His findings offer crucial insight into the molecular basis of this rare genetic disease and lay the groundwork for developing targeted therapeutic strategies.

Education

Ph.D. College of Medicine, University of Vermont
B.S. Goucher College 

Courses Taught

CH324 Biochemistry I
CH325 Biochemistry II
CH422 Senior Synthesis and Examination
 

Publications

Abbott JA, Livingston NM, Egri SB, Guth E, Francklyn CS. (2016) Characterization of aminoacyl-tRNA synthetase stability and substrate interaction by differential scanning fluorimetry. Methods doi: 10.1016/j.ymeth.2016.10.013

Özcelik D, Barandun J, Schmitz N, Sutter M, Guth E, Damberger FF, Allain FH, Ban N, Weber-Ban E. (2012) Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway. Nature Communications doi: 10.1038/ncomms2009.

Guth EC, Thommen M, Weber-Ban E.  (2011)  Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated Pup intermediate. JBC, 286:4412-4419