Thermophilic phosphoribosyltransferases Thermus thermophilus HB27 in nucleotide synthesis

• Ilja V. Fateev,
• Ekaterina V. Sinitsina,
• Aiguzel U. Bikanasova,
• Maria A. Kostromina,
• Elena S. Tuzova,
• Larisa V. Esipova,
• Tatiana I. Muravyova,
• Alexei L. Kayushin,
• Irina D. Konstantinova and
• Roman S. Esipov

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 hypoxanthine phosphoribosyltransferase (TthHPRT) from Thermus thermophilus

• synthesis, where enzymes of thermophilic microorganisms Thermus thermophilus HB27 (phosphoribosylpyrophosphate synthetase – PRPPS and adenine phosphoribosyltransferase – APRT) and Thermus sp. 2.9 (ribokinase – RK) carry out successive transformations of ribose and adenine heterocyclic bases into the

• influence of temperature and Mg2+ concentration on the activity of TthHPRT was investigated. The results were compared with data for adenine phosphoribosyltransferase Thermus thermophilus, obtained earlier [1]. The TthAPRT is active over a wide temperature range (Figure 3). A maximal activity of TthHPRT