(254b) Simulating the Mechanistic Pathway of Transglycosylation Via a Mutant Glycoside Hydrolase

Authors: 
Burgin, T., University of Michigan
Mayes, H., University of Michigan
There is scientific, industrial, and medical value in synthesis of bespoke oligosaccharides, but significant limitations exist to existing laboratory methods. A more desirable approach is to employ highly specific enzymes, but the glycosyltransferases nature employs to do this job are poorly suited to industrial use. An enzymatic alternative to glycosyltransferases is transglycosylation via mutated glycoside hydrolases. The Thermotoga maritima α-L-fucosidase (TmAfc) mutant D224G has been demonstrated to have good non-specific transglycosylation activity, but the molecular mechanism is not yet understood, hampering engineering efforts. In this talk, we describe transition path sampling simulations to elucidate the transglycosylation pathway of TmAfc D224G, and discuss our proposed mechanism’s implications for engineering improved activity and specificity in this class of enzymes in the future.

Checkout

This paper has an Extended Abstract file available; you must purchase the conference proceedings to access it.

Checkout

Do you already own this?

Pricing


Individuals

AIChE Members $150.00
AIChE Graduate Student Members Free
AIChE Undergraduate Student Members Free
Non-Members $225.00