Synthesis and enzymatic evaluation of the guanosine analogue 2-amino-6-mercapto-7-methylpurine ribonucleoside (MESG): insights into the phosphorolysis reaction mechanism based on the blueprint transition state: SN1 or SN2?

A modified experimental procedure for the synthesis of MESG (2-amino-6-mercapto-7-methylpurine ribonucleoside) 1 has been successfully performed and its full characterization is presented. High resolution ESI(+)-MSMS indicates both the nucleoside bond cleavage as the main fragmentation in the gas phase and a possible SN1 mechanism. Ab initio transition state calculations based on the blue print transition state support this mechanistic rationale and discard an alternative SN2 mechanism. Assays using purine nucleoside phosphorylase (PNP) enzyme (human and M. tuberculosis sources) indicate its efficiency in the phosphorolysis of MESG and allow the quantitative determination of inorganic phosphate in real time assay.

7. On the priority of "Genistion purgantis" Tüxen in Tüxen & Oberdorfer 1958 and "Senecioni-Genistetum purgantis" Tüxen & Oberdorfer 1958

In a recent review of which we were co-authors (Rivas-Martínez, Belmonte, Cantó, Fernández-González, Fuente, Moreno, Sánchez-Mata & Sancho, Lazaroa 7: 93-124. 1987), rejection of names Genistion purgantis Túxen in Túxen & Oberdorfer 1958 [Veróff. Geobot. Inst. Rúbel Zúrich 32: 228] and Senecio tournefortii-Genistapurgans Ass. Túxen & Oberdorfer 1958 [op. cit.: 229-230] versus Pino-Cytision purgantis Rivas-Martínez 1964 [Anales lnst. Bot. Cavanilles 22: 358] and Junipero nanae-Sarothamnetum purgantis Rivas-Martínez 1963 [Anales Inst. Bot. Cavanilles 21(1): 172-186] respectively, was proposed and adopted.