Issue 46, 2010
From the journal:

Chemical Communications

O-Glycoligases, a new category of glycoside bond-forming mutant glycosidases, catalyse facile syntheses of isoprimeverosides†‡

Young-Wan Kim,ab   Ran Zhang,a   Hongming Chena  and  Stephen G. Withers*a  

* Corresponding authors

a Department of Chemistry, University of British Columbia, Vancouver, British Columbia, Canada
E-mail: withers@chem.ubc.ca
Fax: +1 604 822 2847
Tel: +1 604 822 3299

b Department of Food and Biotechnology, Korea University, Jochiwon, Korea

Abstract

A mutant α-xylosidase that lacks its catalytic acid/base residue efficiently catalyses the synthesis of O-linked isoprimeverosides (Xyl-α-1,6GlcOR) in near quantitative yields.

Graphical abstract: O-Glycoligases, a new category of glycoside bond-forming mutant glycosidases, catalyse facile syntheses of isoprimeverosides

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C0CC03168B
Article type
Communication
Submitted
11 Aug. 2010
Accepted
05 Okt. 2010
First published
28 Okt. 2010

Chem. Commun., 2010,46, 8725-8727

Permissions

Request permissions

O-Glycoligases, a new category of glycoside bond-forming mutant glycosidases, catalyse facile syntheses of isoprimeverosides

Y. Kim, R. Zhang, H. Chen and S. G. Withers, Chem. Commun., 2010, 46, 8725 DOI: 10.1039/C0CC03168B

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements