53-83-8Relevant articles and documents
Thermophilic phosphoribosyltransferases Thermus thermophilus HB27 in nucleotide synthesis
Fateev, Ilja V.,Sinitsina, Ekaterina V.,Bikanasova, Aiguzel U.,Kostromina, Maria A.,Tuzova, Elena S.,Esipova, Larisa V.,Muravyova, Tatiana I.,Kayushin, Alexei L.,Konstantinova, Irina D.,Esipov, Roman S.
, p. 3098 - 3105 (2019/01/21)
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 HB27 were expressed in E.coli strains and purified by chromatographic methods with yields of 10-13 mg per liter of culture. The activity dependence of TthAPRT and TthHPRT on different factors was investigated along with the substrate specificity towards different heterocyclic bases. The kinetic parameters for TthHPRT with natural substrates were determined. Two nucleotides were synthesized: 9-(β-D-ribofuranosyl)-2-chloroadenine 5'-monophosphate (2-l-AMP) using TthAPRT and 1-(β-Dribofuranosyl)pyrazolo[3,4-d]pyrimidine-4-one 5'-monophosphate (Allop-MP) using TthPRT.
Five-component cascade synthesis of nucleotide analogues in an engineered self-immobilized enzyme aggregate
Scism, Robert A.,Bachmann, Brian O.
scheme or table, p. 67 - 70 (2010/10/20)
(Chemical Equation Presented) Pathway in a particle: A five-enzyme biosynthetic pathway was self-immobilized to form a single biocatalyst for generation of purine nucleotide analogues from d-ribose. This method provides an alternative to engineering biosynthetic pathways in whole cells that obviates problems associated with toxicity, transport and genetic regulation.
Nucleosides and nucleotides. XIII. Synthesis of thiopurine nucleosides from adenosine and guanosine derivatives by the sulfhydrolysis
Miura,Ueda
, p. 2064 - 2069 (2007/10/04)
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