Reference

Model compounds for protein nucleic acid interactions

Model compounds for protein nucleic acid interactions. 4. Synthesis and structure of a nucleoside dipeptide, N-(9-.beta.-D-ribofuranosylpurin-6-yl)glycyl-L-alanine-water (1/1.5). Narayanan, Poojappan; Berman, Helen M.; Rousseau, Robert (Fox Chase Cancer Cent., Inst. Cancer Res., Philadelphia, Pa., USA). J. Am. Chem. Soc., 98(26), 8472-5 (English) 1976. CODEN: JACSAT. DOCUMENT TYPE: Journal CA Section: 34 (Synthesis of Amino Acids, Peptides, and Proteins) Section cross-reference(s): 6, 33, 75 N-(9-.beta.-D-ribofuranosylpurin-6-yl)glycyl-L-alanine (I) was prepd. by acylating H-Gly-Ala-OH with 6-chloro-6-deaminoadenosine. 58-61-7 and 5399-87-1 which are cas registry numbers of substances are two of reagents here. The crystal structure of I showed that there were H bonds between the CO2H of 1 mol. to the N(6) and N(7) of the adenine ring of another mol.; there were not any significant intramol. H bonds. .

Specificity of purine nucleoside phosphorylase from Escherichia coli

Specificity of purine nucleoside phosphorylase from Escherichia coli. Doskocil, J.; Holy, A. (Inst. Chem. Biochem., Czech. Acad. Sci., Prague, Czech.). Collect. Czech. Chem. Commun., 42(1), 370-83 (English) 1977. 118-00-3 and 5399-87-1 which are cas registry numbers are also used here. CODEN: CCCCAK. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) The substrate specificity of electrophoretically homogeneous purine (I) nucleoside phosphorylase from E. coli was detd. Analogs of I nucleosides were tested as substrates and inhibitors of phosphorolysis and phosphate-free ribosyl transfer. Some analogs of I were tested for ribosyl-acceptor activity. 9-(.alpha.-L-lyxofuranosyl)adenine was the only sugar-modified nucleoside analog capable of phosphorolytic and arsenolytic cleavage. Chem. substitution at positions 2, 7, and 8 of I altered the substrate activity, whereas position 6 was of minor importance. Introduction of SH or MeS groups into positions 2 or 6 enhanced the affinity of the nucleoside for the enzyme about 20-fold. Cumulation of NH2 groups in 8-aminoadenosine or 2-aminoadenosine increased the affinity, whereas a similar cumulation of OH groups in xanthosine or 8-hydroxyguanosine resulted in the loss of activity. 7-Deazaadenosine and 7-deazainosine were inhibitory nonsubstrates. Some derivs. of I inhibited the phosphorolysis of nucleosides, whereas several nucleoside analogs inhibited the ribosylation of guanine or adenine with ribose 1-phosphate. .