Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Developing a Collection of Immobilized Nucleoside Phosphorylases for the Preparation of Nucleoside Analogues: Enzymatic Synthesis of Arabinosyladenine and 2,3-Dideoxyinosine

Serra, Immacolata ; Ubiali, Daniela ; Piskur, Jure LU ; Christoffersen, Stig LU ; Lewkowicz, Elizabeth S. ; Iribarren, Adolfo M. ; Albertini, Alessandra M. and Terreni, Marco (2013) In Collection of Czechoslovak Chemical Communications 78(2). p.157-165
Abstract
The use of nucleoside phosphorylases (NPs; EC 2.4.2.n) represents a convenient alternative to the chemical route for the synthesis of natural and modified nucleosides. We purified four recombinantly expressed nucleoside phosphorylases from the bacterial pathogens Citrobacter koseri, Clostridium perfringens, and Streptococcus pyogenes (CkPNPI, CkPNPII, CpUP, SpUP) and their substrate specificity was investigated towards either natural pyrimidine or purine nucleosides and some analogues, namely, arabinosyladenine (araA) and 2,3-dideoxyinosine (ddI). A 23% activity towards these latter compounds (compared to the natural substrates) was observed. Enzyme activities were compared to the specificities obtained for the enzymes pyrimidine... (More)
The use of nucleoside phosphorylases (NPs; EC 2.4.2.n) represents a convenient alternative to the chemical route for the synthesis of natural and modified nucleosides. We purified four recombinantly expressed nucleoside phosphorylases from the bacterial pathogens Citrobacter koseri, Clostridium perfringens, and Streptococcus pyogenes (CkPNPI, CkPNPII, CpUP, SpUP) and their substrate specificity was investigated towards either natural pyrimidine or purine nucleosides and some analogues, namely, arabinosyladenine (araA) and 2,3-dideoxyinosine (ddI). A 23% activity towards these latter compounds (compared to the natural substrates) was observed. Enzyme activities were compared to the specificities obtained for the enzymes pyrimidine nucleoside phosphorylase from Bacillus subtilis (BsPyNP) and purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNPII) previously reported by some of the authors. The enzymes displaying the suitable specificity for the synthesis of araA and ddI were immobilized on aldehydeagarose. The immobilized preparations were highly stable at alkaline pH and in the presence of methanol or acetonitrile as cosolvent. They were used in the synthesis of araA and ddI by a one-pot, bienzymatic transglycosylation achieving 74 and 44% conversion, respectively. (Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
biocatalysis, enzymes, immobilization, nucleosides, transglycosylation
in
Collection of Czechoslovak Chemical Communications
volume
78
issue
2
pages
157 - 165
publisher
Institute of Organic Chemistry and Biochemistry
external identifiers
  • wos:000315117100005
  • scopus:84874143770
ISSN
2192-6506
DOI
10.1002/cplu.201200278
language
English
LU publication?
yes
id
7d598c00-8176-48a0-bcf6-b5c40ab5aac6 (old id 3674574)
date added to LUP
2016-04-01 09:59:33
date last changed
2022-04-27 17:34:37
@article{7d598c00-8176-48a0-bcf6-b5c40ab5aac6,
  abstract     = {{The use of nucleoside phosphorylases (NPs; EC 2.4.2.n) represents a convenient alternative to the chemical route for the synthesis of natural and modified nucleosides. We purified four recombinantly expressed nucleoside phosphorylases from the bacterial pathogens Citrobacter koseri, Clostridium perfringens, and Streptococcus pyogenes (CkPNPI, CkPNPII, CpUP, SpUP) and their substrate specificity was investigated towards either natural pyrimidine or purine nucleosides and some analogues, namely, arabinosyladenine (araA) and 2,3-dideoxyinosine (ddI). A 23% activity towards these latter compounds (compared to the natural substrates) was observed. Enzyme activities were compared to the specificities obtained for the enzymes pyrimidine nucleoside phosphorylase from Bacillus subtilis (BsPyNP) and purine nucleoside phosphorylase from Aeromonas hydrophila (AhPNPII) previously reported by some of the authors. The enzymes displaying the suitable specificity for the synthesis of araA and ddI were immobilized on aldehydeagarose. The immobilized preparations were highly stable at alkaline pH and in the presence of methanol or acetonitrile as cosolvent. They were used in the synthesis of araA and ddI by a one-pot, bienzymatic transglycosylation achieving 74 and 44% conversion, respectively.}},
  author       = {{Serra, Immacolata and Ubiali, Daniela and Piskur, Jure and Christoffersen, Stig and Lewkowicz, Elizabeth S. and Iribarren, Adolfo M. and Albertini, Alessandra M. and Terreni, Marco}},
  issn         = {{2192-6506}},
  keywords     = {{biocatalysis; enzymes; immobilization; nucleosides; transglycosylation}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{157--165}},
  publisher    = {{Institute of Organic Chemistry and Biochemistry}},
  series       = {{Collection of Czechoslovak Chemical Communications}},
  title        = {{Developing a Collection of Immobilized Nucleoside Phosphorylases for the Preparation of Nucleoside Analogues: Enzymatic Synthesis of Arabinosyladenine and 2,3-Dideoxyinosine}},
  url          = {{http://dx.doi.org/10.1002/cplu.201200278}},
  doi          = {{10.1002/cplu.201200278}},
  volume       = {{78}},
  year         = {{2013}},
}