Beilstein J. Org. Chem.2018,14, 3098–3105, doi:10.3762/bjoc.14.289
, 117997, Russia 10.3762/bjoc.14.289 Abstract Phosphoribosyltransferases are the tools that allow the synthesis of nucleotide analogues using multi-enzymatic cascades. The recombinant adenine phosphoribosyltransferase (TthAPRT) and hypoxanthinephosphoribosyltransferase (TthHPRT) from Thermus thermophilus
phosphoribosyltransferase; catalysis; enzyme; hypoxanthinephosphoribosyltransferase; multi-enzyme cascade; nucleotides; thermophiles; Introduction
Bacterial phosphoribosyltransferases are used in multi-enzymatic cascades that perform nucleotide synthesis de novo [1][2]. Recently, we reported on the possibility of cascade
way, with a yield of 32%.
Conclusion
The recombinant adenine phosphoribosyltransferase and hypoxanthinephosphoribosyltransferase from Thermus thermophilus HB27 were purificated with yields no less than 10–13 mg per litre of culture. A comparative study of substrate specificity of these enzymes
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Graphical Abstract
Figure 1:
A multi-enzymatic synthesis of modified adenosine -5'-monophosphates.