Abstract:
:A GTP:RNA guanylyltransferase or capping enzyme has been purified approximately 2000-fold from wheat germ. The enzyme catalyzes the transfer of the GMP residue from GTP to the 5' end of RNA or synthetic polyribonucleotides. Diphosphate-ended polymers were capped more efficiently than molecules with triphosphate ends, and molecules with monophosphate ends were not capped at all. There appears to be little specificity since RNAs with purine or pyrimidine ends served as acceptors. Other features of the wheat germ RNA guanylyltransferase include relatively low Km values for GTP (2.7 microM) and ppA (pA)n (14.2 nM), a divalent cation requirement satisfied by low (0.5 mM) concentrations of MnCl2 or higher (5 mM) concentrations of MgCl2, and a pH optimum around neutrality.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Keith JM,Venkatesan S,Gershowitz A,Moss Bdoi
10.1021/bi00531a020subject
Has Abstractpub_date
1982-01-19 00:00:00pages
327-33issue
2eissn
0006-2960issn
1520-4995journal_volume
21pub_type
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