Substrate specificity ofE. coliuridine phosphorylase. Further evidences of high-synconformation of the substrate in uridine phosphorolysis-Reference-Cited by-同舟云学术

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Substrate specificity ofE. coliuridine phosphorylase. Further evidences of high-synconformation of the substrate in uridine phosphorolysis

Published:2016-11-15 Issue:2 Volume:36 Page:107-121
ISSN:1525-7770
Container-title:Nucleosides, Nucleotides and Nucleic Acids
language:en
Short-container-title:Nucleosides, Nucleotides and Nucleic Acids

Author:

Alexeev C. S.¹,Sivets G. G.²,Safonova T. N.³,Mikhailov S. N.¹

Affiliation:

1. Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia

2. Institute of Bioorganic Chemistry, National Academy of Sciences of Belarus, Minsk, Belarus

3. Bach Institute of Biochemistry, Russian Academy of Sciences, Moscow, Russia

Publisher

Informa UK Limited

Subject

Genetics,Molecular Medicine,Biochemistry,General Medicine

Link

https://www.tandfonline.com/doi/pdf/10.1080/15257770.2016.1223306

Reference40 articles.

1. Structural analyses reveal two distinct families of nucleoside phosphorylases

2. Nucleoside Phosphorylases

3. Uridine phosphorylase in breast cancer: a new prognostic factor?

4. Enzymatic preparation of nucleoside antibiotics

5. Industrial biocatalysis

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