Enabling Glycosyltransferase Evolution: A Facile Substrate-Attachment Strategy for Phage-Display Enzyme Evolution

Phage‐bound. We report the first display of an active glycosyltransferase (Gtf), MurG, on phage along with an efficient selenocysteine‐based strategy for substrate immobilization. Phage‐display evolution of Gtfs could enable new approaches to the chemoenzymatic synthesis of glycoconjugates.

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Bibliographic Details
Published in:Chembiochem : a European journal of chemical biology 2006-05, Vol.7 (5), p.753-756
Main Authors: Love, Kerry Routenberg, Swoboda, Jonathan G, Noren, Christopher J, Walker, Suzanne
Format: Article
Language:English
Subjects:
Bacterial Outer Membrane Proteins - chemistry
Bacteriophages - chemistry
Carbohydrate Conformation
Catalysis
directed evolution
Directed Molecular Evolution - methods
Enzyme Activation
glycosyltransferases
N-Acetylglucosaminyltransferases - chemistry
Peptide Library
phage display
selenocysteine
Selenocysteine - chemistry
Time Factors
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Description
Summary:Phage‐bound. We report the first display of an active glycosyltransferase (Gtf), MurG, on phage along with an efficient selenocysteine‐based strategy for substrate immobilization. Phage‐display evolution of Gtfs could enable new approaches to the chemoenzymatic synthesis of glycoconjugates.
ISSN:1439-4227
1439-7633
DOI:10.1002/cbic.200600018