Literature DB >> 19003566

Substrate specificity of thymidine phosphorylase of E. coli: role of hydroxyl groups.

Natalya G Panova1, Cyril S Alexeev, Konstantin M Polyakov, Sergei A Gavryushov, Anatoliy M Kritzyn, Sergey N Mikhailov.   

Abstract

Substrate specificity of E. coli thymidine phosphorylase to pyrimidine nucleoside modified at 5'-, 3'-, and 2'-positions of sugar moiety has been studied. Equilibrium (K(eq)) and kinetics constants of phosphorolysis reaction of nucleosides were measured. The most important hydrogen bonds in enzyme-substrate complex have been determined.

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Year:  2008        PMID: 19003566     DOI: 10.1080/15257770802257895

Source DB:  PubMed          Journal:  Nucleosides Nucleotides Nucleic Acids        ISSN: 1525-7770            Impact factor:   1.381


  2 in total

1.  Enzymatic synthesis and phosphorolysis of 4(2)-thioxo- and 6(5)-azapyrimidine nucleosides by E. coli nucleoside phosphorylases.

Authors:  Vladimir A Stepchenko; Anatoly I Miroshnikov; Frank Seela; Igor A Mikhailopulo
Journal:  Beilstein J Org Chem       Date:  2016-12-01       Impact factor: 2.883

2.  Engineering of the Recombinant Expression and PEGylation Efficiency of the Therapeutic Enzyme Human Thymidine Phosphorylase.

Authors:  Christos S Karamitros; Catrina M Somody; Giulia Agnello; Scott Rowlinson
Journal:  Front Bioeng Biotechnol       Date:  2021-12-17
  2 in total

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