5446-37-7Relevant articles and documents
Chemoenzymatic synthesis of cytokinins from nucleosides: Ribose as a blocking group
Oslovsky, Vladimir E.,Solyev, Pavel N.,Polyakov, Konstantin M.,Alexeev, Cyril S.,Mikhailov, Sergey N.
, p. 2156 - 2163 (2018/03/26)
Nucleoside phosphorylases are involved in the salvage pathways of nucleoside biosynthesis and catalyze the reversible reaction of a nucleobase with α-d-ribose-1-phosphate to yield a corresponding nucleoside and an inorganic phosphate. The equilibrium of these reactions is shifted towards nucleosides, especially in the case of purines. Purine nucleoside phosphorylase (PNP, EC 2.4.2.1) is widely used in labs and industry for the synthesis of nucleosides of practical importance. Bacterial PNPs have relatively broad substrate specificity utilizing a wide range of purines with different substituents to form the corresponding nucleosides. To shift the reaction in the opposite direction we have used arsenolysis instead of phosphorolysis. This reaction is irreversible due to the hydrolysis of the resulting α-d-ribose-1-arsenate. As a result, heterocyclic bases are formed in quantitative yields and can be easily isolated. We have developed a novel method for the preparation of cytokinins based on the enzymatic cleavage of the N-glycosidic bond of N6-substituted adenosines in the presence of PNP and Na2HAsO4. According to the HPLC analysis the conversion proceeds in quantitative yields. In the proposed strategy the ribose residue acts as a protective group. No contamination of the final products with AsO43- has been detected via HPLC-HRMS; simple analytical arsenate detection via ESI-MS has been proposed.
Chemical modification of the plant isoprenoid cytokinin N6-isopentenyladenosine yields a selective inhibitor of human enterovirus 71 replication
Tararov, Vitali I.,Tijsma, Aloys,Kolyachkina, Svetlana V.,Oslovsky, Vladimir E.,Neyts, Johan,Drenichev, Mikhail S.,Leyssen, Pieter,Mikhailov, Sergey N.
, p. 406 - 413 (2015/05/04)
In this study, we demonstrate that N6-isopentenyladenosine, which essentially is a plant cytokinin-like compound, exerts a potent and selective antiviral effect on the replication of human enterovirus 71 with an EC50 of 1.0 ± 0.2 mM and a selectivity index (SI) of 5.7. The synthesis of analogs with modification of the N6-position did not result in a lower EC50 value. However, in particular with the synthesis of N6-(5-hexene-2-yne-1-yl)adenosine (EC50 = 4.3 ± 1.5 mM), the selectivity index was significantly increased: because of a reduction in the adverse effect of this compound on the host cells, an SI 101 could be calculated. With this study, we for the first time provide proof that a compound class that is based on the plant cytokinin skeleton offers an interesting starting point for the development of novel antivirals against mammalian viruses, in the present context in particular against enterovirus 71.
Studies towards the synthesis of atp analogs as potential glutamine synthetase inhibitors
Salisu, Sheriff,Kenyon, Colin,Kaye, Perry T.
experimental part, p. 2216 - 2225 (2011/06/28)
In research directed at the development of adenine triphosphate (ATP) analogs as potential glutamine synthetase (GS) inhibitors, adenine and allopurinol derivatives have been synthesized either as novel ATP analogs or as scaffolds for the construction of
