Engineering the specificity of trehalose phosphorylase as a general strategy for the production of glycosyl phosphates
(2014) CHEMICAL COMMUNICATIONS. 50(58). p.7834-7836- abstract
- A two-step process is reported for the anomeric phosphorylation of galactose, using trehalose phosphorylase as biocatalyst. The monosaccharide enters this process as acceptor but can subsequently be released from the donor side, thanks to the non-reducing nature of the disaccharide intermediate. A key development was the creation of an optimized enzyme variant that displays a strict specificity (99%) for beta-galactose 1-phosphate as product.
Please use this url to cite or link to this publication:
http://hdl.handle.net/1854/LU-4427715
- author
- Chao Chen UGent, Jef Van der Borght, Rob De Vreese, Matthias D'hooghe UGent, Wim Soetaert UGent and Tom Desmet UGent
- organization
- year
- 2014
- type
- journalArticle (original)
- publication status
- published
- subject
- keyword
- DIRECTED EVOLUTION, SUBSTRATE-SPECIFICITY, DISACCHARIDE PHOSPHORYLASES, SCHIZOPHYLLUM-COMMUNE, ENZYMATIC PRODUCTION, GALACTOKINASE, REGENERATION, STABILITY, MECHANISM, ANALOGS
- journal title
- CHEMICAL COMMUNICATIONS
- Chem. Commun.
- volume
- 50
- issue
- 58
- pages
- 7834 - 7836
- Web of Science type
- Article
- Web of Science id
- 000338296300022
- JCR category
- CHEMISTRY, MULTIDISCIPLINARY
- JCR impact factor
- 6.834 (2014)
- JCR rank
- 20/157 (2014)
- JCR quartile
- 1 (2014)
- ISSN
- 1359-7345
- DOI
- 10.1039/c4cc02202e
- project
- Biotechnology for a sustainable economy (Bio-Economy)
- language
- English
- UGent publication?
- yes
- classification
- A1
- copyright statement
- I have transferred the copyright for this publication to the publisher
- id
- 4427715
- handle
- http://hdl.handle.net/1854/LU-4427715
- date created
- 2014-06-24 13:16:36
- date last changed
- 2016-12-19 15:42:56
@article{4427715,
abstract = {A two-step process is reported for the anomeric phosphorylation of galactose, using trehalose phosphorylase as biocatalyst. The monosaccharide enters this process as acceptor but can subsequently be released from the donor side, thanks to the non-reducing nature of the disaccharide intermediate. A key development was the creation of an optimized enzyme variant that displays a strict specificity (99\%) for beta-galactose 1-phosphate as product.},
author = {Chen, Chao and Van der Borght, Jef and De Vreese, Rob and D'hooghe, Matthias and Soetaert, Wim and Desmet, Tom},
issn = {1359-7345},
journal = {CHEMICAL COMMUNICATIONS},
keyword = {DIRECTED EVOLUTION,SUBSTRATE-SPECIFICITY,DISACCHARIDE PHOSPHORYLASES,SCHIZOPHYLLUM-COMMUNE,ENZYMATIC PRODUCTION,GALACTOKINASE,REGENERATION,STABILITY,MECHANISM,ANALOGS},
language = {eng},
number = {58},
pages = {7834--7836},
title = {Engineering the specificity of trehalose phosphorylase as a general strategy for the production of glycosyl phosphates},
url = {http://dx.doi.org/10.1039/c4cc02202e},
volume = {50},
year = {2014},
}
- Chicago
- Chen, Chao, Jef Van der Borght, Rob De Vreese, Matthias D’hooghe, Wim Soetaert, and Tom Desmet. 2014. “Engineering the Specificity of Trehalose Phosphorylase as a General Strategy for the Production of Glycosyl Phosphates.” Chemical Communications 50 (58): 7834–7836.
- APA
- Chen, Chao, Van der Borght, J., De Vreese, R., D’hooghe, M., Soetaert, W., & Desmet, T. (2014). Engineering the specificity of trehalose phosphorylase as a general strategy for the production of glycosyl phosphates. CHEMICAL COMMUNICATIONS, 50(58), 7834–7836.
- Vancouver
- 1.Chen C, Van der Borght J, De Vreese R, D’hooghe M, Soetaert W, Desmet T. Engineering the specificity of trehalose phosphorylase as a general strategy for the production of glycosyl phosphates. CHEMICAL COMMUNICATIONS. 2014;50(58):7834–6.
- MLA
- Chen, Chao, Jef Van der Borght, Rob De Vreese, et al. “Engineering the Specificity of Trehalose Phosphorylase as a General Strategy for the Production of Glycosyl Phosphates.” CHEMICAL COMMUNICATIONS 50.58 (2014): 7834–7836. Print.