16975-94-3Relevant articles and documents
Conformationally restricted nucleosides. The reaction of adenosine deaminase with substrates built on a bicyclo[3.1.0]hexane template
Marquez, Victor E.,Russ, Pamela,Alonso, Randolph,Siddiqui, Maqbool A.,Shin, Kye-Jung,George, Clifford,Nicklaus, Marc C.,Dai, Fang,Ford Jr., Harry
, p. 521 - 530 (1999)
Adenosine deaminase (ADA) can discriminate between two distinct (North and South), conformationally rigid substrate conformers. (N)-methanocarba- 2'dA (4) is deaminated 100 times faster than the antipodal (S)-methanocarba- 2'dA (5), whereas a nonrigid analogue, aristeromycin (6), is deaminated at an intermediate rate. These results are in agreement with crystallographic data from ADA-ribonucleoside complexes showing the furanose ring of the bound purine in a C3'-endo (North) conformation. The data presented here suggests that 4 and 5 are useful probes to ascertain conformational preferences by purine metabolizing enzymes.
Resolution of racemic carbocyclic analogues of purine nucleosides through the action of adenosine deaminase. Antiviral activity of the carbocyclic 2'-deoxyguanosine enantiomers
Secrist III.,Montgomery,Shealy,O'Dell,Clayton
, p. 746 - 749 (2007/10/02)
The action of adenosine deaminase on racemic carbocyclic analogues of 6-aminopurine nucleosides was investigated. When either racemic carbocyclic adenosine [(±)-C-Ado] or the racemic carbocyclic analogue [(±)-C-2,6-DAP-2'-dR] of 2,6-diaminopurine 2'-deoxyribofuranoside was incubated with this enzyme, approximately half of the material was deaminated rapidly. From the resulting solution, the D isomers of the deaminated carbocyclic analogues (D-carbocyclic inosine, D-C-Ino, or D-carbocyclic 2'-deoxyguanosine, D-2'-CDG) and the L isomers of the undeaminated carbocyclic analogues were isolated. At higher concentrations of the enzyme, deamination of (L)-C-Ado and (L)-C-2,6-DAP-2'dR proceeded slowly, thus also making the other enantiomers accessible. In tests in vitro against herpes simplex virus, types 1 and 2, D-2'-CDG was as active and potent as (±)-2'-CDG, whereas L-2'-CDG displayed only modest activity. In contrast to the previously reported high activity and potency of (±)-C-2,6-DAP-2'-dR against these two viruses, (L)-C-2,6-DAP-2'-dR was inactive.