Thermophilic nucleoside phosphorylases: Their properties, characteristics and applications.
Journal
Biochimica et biophysica acta. Proteins and proteomics
ISSN: 1878-1454
Titre abrégé: Biochim Biophys Acta Proteins Proteom
Pays: Netherlands
ID NLM: 101731734
Informations de publication
Date de publication:
02 2020
02 2020
Historique:
received:
31
07
2019
revised:
16
09
2019
accepted:
20
09
2019
pubmed:
7
11
2019
medline:
21
4
2020
entrez:
6
11
2019
Statut:
ppublish
Résumé
Nucleoside phosphorylases catalyze the reversible phosphorolysis of pyrimidine and purine nucleosides in the presence of phosphate. They are valuable catalysts in the synthesis of nucleosides and their analogues, which are often used as pharmaceuticals or their precursors. Thermostable nucleoside phosphorylases are promising biocatalysts, as they withstand harsh reaction conditions such as high pH or the addition of organic solvents. In this review, the characteristics and properties of thermostable nucleoside phosphorylases are described. Differences in amino acid content and protein structure were compared to their mesophilic homologues to identify features involved in thermostability. Substrate spectra of thermostable nucleoside phosphorylases were analyzed, and it is shown that thermostable nucleoside phosphorylases have a wider substrate spectrum than their mesophilic counterparts. Thus, thermostable nucleoside phosphorylases are interesting biocatalysts for industrial applications.
Identifiants
pubmed: 31689547
pii: S1570-9639(19)30190-6
doi: 10.1016/j.bbapap.2019.140304
pii:
doi:
Substances chimiques
Organic Chemicals
0
Pentosyltransferases
EC 2.4.2.-
nucleoside phosphorylase
EC 2.4.2.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
140304Informations de copyright
Copyright © 2019 Elsevier B.V. All rights reserved.