13146-72-0Relevant articles and documents
Synthesis of 2' and 3' deoxyinosines
Yamazaki,Akiyama,Kumashiro,Ikehara
, p. 1143 - 1146 (1973)
-
Deamination of 6-aminodeoxyfutalosine in menaquinone biosynthesis by distantly related enzymes
Goble, Alissa M.,Toro, Rafael,Li, Xu,Ornelas, Argentina,Fan, Hao,Eswaramoorthy, Subramaniam,Patskovsky, Yury,Hillerich, Brandan,Seidel, Ron,Sali, Andrej,Shoichet, Brian K.,Almo, Steven C.,Swaminathan, Subramanyam,Tanner, Martin E.,Raushel, Frank M.
, p. 6525 - 6536 (2013)
Proteins of unknown function belonging to cog1816 and cog0402 were characterized. Sav2595 from Steptomyces avermitilis MA-4680, Acel0264 from Acidothermus cellulolyticus 11B, Nis0429 from Nitratiruptor sp. SB155-2 and Dr0824 from Deinococcus radiodurans R1 were cloned, purified, and their substrate profiles determined. These enzymes were previously incorrectly annotated as adenosine deaminases or chlorohydrolases. It was shown here that these enzymes actually deaminate 6-aminodeoxyfutalosine. The deamination of 6-aminodeoxyfutalosine is part of an alternative menaquinone biosynthetic pathway that involves the formation of futalosine. 6-Aminodeoxyfutalosine is deaminated by these enzymes with catalytic efficiencies greater than 10 5 M-1 s-1, Km values of 0.9-6.0 μM, and kcat values of 1.2-8.6 s-1. Adenosine, 2′-deoxyadenosine, thiomethyladenosine, and S-adenosylhomocysteine are deaminated at least an order of magnitude slower than 6-aminodeoxyfutalosine. The crystal structure of Nis0429 was determined and the substrate, 6-aminodeoxyfutalosine, was positioned in the active site on the basis of the presence of adventitiously bound benzoic acid. In this model, Ser-145 interacts with the carboxylate moiety of the substrate. The structure of Dr0824 was also determined, but a collapsed active site pocket prevented docking of substrates. A computational model of Sav2595 was built on the basis of the crystal structure of adenosine deaminase and substrates were docked. The model predicted a conserved arginine after β-strand 1 to be partially responsible for the substrate specificity of Sav2595.
APPLICATION OF 3'-DEOXYINOSINE IN PREPARATION OF DRUG, FOOD OR HEALTH PRODUCT FOR MULTIPLE DISEASE
-
Page/Page column 9, (2020/05/13)
The present invention relates to the field of drug, provides an application of 3'-deoxyinosine in the preparation of food, drug or health products for the prevention or treatment of diet-induced obesity or hyperlipidemia, provides an application of 3'-deoxyinosine in the preparation of food, drug or health products for the prevention of hypertension or arteriosclerosis, and further provides an application of 3'-deoxyinosine in the preparation of skin care products. Studies of the present invention have indicated that 3'-deoxyinosine plays a significant role in treating hyperlipidemia and reducing weights of patients with diet-induced obesity, overcoming the existing technical prejudice. Moreover, 3'-deoxyinosine has a more extensive effect on preventing or treating hyperlipidemia compared with the existing medications. Meanwhile, 3'-deoxyinosine is able to effectively prevent the development of hypertension and arteriosclerosis by reducing serum lipid content and high-density lipoprotein (HDL) content.
The Chemoenzymatic Synthesis of 2-Chloro- and 2-Fluorocordycepins
Denisova, Alexandra O.,Tokunova, Yulia A.,Fateev, Ilja V.,Breslav, Alexandra A.,Leonov, Vladimir N.,Dorofeeva, Elena V.,Lutonina, Olga I.,Muzyka, Inessa S.,Esipov, Roman S.,Kayushin, Alexey L.,Konstantinova, Irina D.,Miroshnikov, Anatoly I.,Stepchenko, Vladimir A.,Mikhailopulo, Igor A.
, p. 4853 - 4860 (2017/10/06)
Two approaches to the chemoenzymatic synthesis of 2-fluorocordycepin and 2-chlorocordycepin were studied: (i) the use of 3′-deoxyadenosine (cordycepin) and 3′-deoxyinosine (3′dIno) as donors of 3-deoxy- d -ribofuranose in the transglycosylation of 2-fluoro- (2F Ade) and 2-chloroadenine (2Cl Ade) catalyzed by the recombinant E. coli purine nucleoside phosphorylase (PNP), and (ii) the use of 2-fluoroadenosine and 3′-deoxyinosine as substrates of the cross-glycosylation and PNP as a biocatalyst. An efficient method for 3′-deoxyinosine synthesis starting from inosine was developed. However, the very poor solubility of 2Cl Ade and 2F Ade is the limiting factor of the first approach. The second approach enables this problem to be overcome and it appears to be advantageous over the former approach from the viewpoint of practical synthesis of the title nucleosides. The 3-deoxy-α- d -ribofuranose-1-phosphate intermediary formed in the 3′dIno phosphorolysis by PNP was found to be the weak and marginal substrate of E. coli thymidine (TP) and uridine (UP) phosphorylases, respectively. Finally, one-pot cascade transformation of 3-deoxy- d -ribose in cordycepin in the presence of adenine and E. coli ribokinase, phosphopentomutase, and PNP was tested and cordycepin formation in ca. 3.4% yield was proved.
