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Engineering the specificity of trehalose phosphorylase as a general strategy for the production of glycosyl phosphates

Chao Chen UGent, Jef Van der Borght, Rob De Vreese UGent, Matthias D'hooghe UGent, Wim Soetaert UGent and Tom Desmet UGent (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:
author
organization
year
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.