The Enzyme Database

Your query returned 1 entry.    printer_iconPrintable version

EC 2.7.7.88     
Accepted name: GDP polyribonucleotidyltransferase
Reaction: 5′-triphospho-mRNA + GDP = diphosphate + guanosine 5′-triphospho-mRNA
Systematic name: 5′-triphospho-mRNA:GDP 5′-phosphopolyribonucleotidyltransferase [G(5′)ppp-mRNA-forming]
Comments: The enzyme from rhabdoviruses transfers 5′-monophosphorylated (p-)mRNA from 5′-triphosphorylated (ppp-)mRNA to GDP to form 5′-capped mRNA (GpppmRNA) in a viral mRNA-start sequence-dependent manner. The (p-)mRNA transfer reaction proceeds through a covalent enzyme-pmRNA intermediate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Ogino, T. and Banerjee, A.K. An unconventional pathway of mRNA cap formation by vesiculoviruses. Virus Res 162 (2011) 100–109. [PMID: 21945214]
2.  Ogino, T., Yadav, S.P. and Banerjee, A.K. Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase. Proc. Natl. Acad. Sci. USA 107 (2010) 3463–3468. [PMID: 20142503]
3.  Ogino, T. and Banerjee, A.K. The HR motif in the RNA-dependent RNA polymerase L protein of Chandipura virus is required for unconventional mRNA-capping activity. J. Gen. Virol. 91 (2010) 1311–1314. [PMID: 20107017]
4.  Ogino, T. and Banerjee, A.K. Formation of guanosine(5′)tetraphospho(5′)adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus. J. Virol. 82 (2008) 7729–7734. [PMID: 18495767]
5.  Ogino, T. and Banerjee, A.K. Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus. Mol. Cell 25 (2007) 85–97. [PMID: 17218273]
[EC 2.7.7.88 created 2015]
 
 


Data © 2001–2017 IUBMB
Web site © 2005–2017 Andrew McDonald