Conformation of the hypermodified purine queuine: Substrate for the enzyme transfer RNA—guanine transglycosylase

✍ Scribed by Hanna Sierzputowska-Gracz; Paul F. Agris; Jon R. Katze

• Book ID: 102523778
• Publisher: John Wiley and Sons
• Year: 1988
• Tongue: English
• Weight: 323 KB
• Volume: 26
• Category: Article
• ISSN: 0749-1581
• DOI: 10.1002/mrc.1260260103

✦ Synopsis

The hypermodified nucleotidyl purine queuine [7-(3,Qtrans-4,5-cis-dihydroxycyclopent-l~n-3-ylaminomethyl)-7deazaguaninel is a substrate for transfer ribonucleic acid (tRNA) enzymes replacing guanine at nucleotide position 34 of tRNAs for the amino acids aspartic acid, asparagine, histidine and tyrosine. The structure and conformation of native queuine was studied by one-dimensional 13C and 'H NMR spectroscopy and by two-dimensional NMR spectroscopy (COSY and NOESY). The structure in solution was found to be the 3,4truns-4,5-cisdihydroxycyclopent-l-ene form. The plane of the cyclopentene ring is probably perpendicular to that of the purine ring structure.