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- Title
The Thermostability of Nucleoside Phosphorylases from Prokaryotes. I. The Role of the Primary Structure of the N-terminal fragment of the Protein in the Thermostability of Uridine Phosphorylases.
- Authors
Veiko, V. P.; Antipov, A. N.; Mordkovich, N. N.; Okorokova, N. A.; Safonova, T. N.; Polyakov, K. M.
- Abstract
Mutant uridine phosphorylase genes from Shewanella oneidensis MR-1 (S. oneidensis) were constructed by site-directed mutagenesis and strains-producers of the corresponding recombinant (F5I and F5G) proteins were obtained on the basis of Escherichia coli cells. The mutant proteins were purified and their physicochemical and enzymatic properties were studied. It was shown that the N-terminal fragment of uridine phosphorylase plays an important role in the thermal stabilization of the enzyme as a whole. The role of the aminoacid (a.a.) residue phenylalanine (F5) in the formation of thermotolerance of uridine phosphorylases from gamma-proteobacteria was revealed.
- Subjects
MUTANT proteins; SHEWANELLA oneidensis; PHOSPHORYLASES; SITE-specific mutagenesis; URIDINE; PROTEINS; ESCHERICHIA coli
- Publication
Applied Biochemistry & Microbiology, 2022, Vol 58, Issue 6, p744
- ISSN
0003-6838
- Publication type
Article
- DOI
10.1134/S0003683822060151