KEGG ENZYME: 2.7.7.88

KEGG

ENZYME: 2.7.7.88

Entry

EC 2.7.7.88                 Enzyme

Name

GDP polyribonucleotidyltransferase;
PRNTase;
5'-triphospho-mRNA:GDP 5'-phosphopolyribonucleotidyltransferase [G(5')ppp-mRNA-forming]

Class

Transferases;
Transferring phosphorus-containing groups;
Nucleotidyltransferases

Sysname

(5')pppAACA-[mRNA]:GDP 5'-phosphopolyribonucleotidyltransferase [(5')pppAACA-[mRNA]-forming]

Reaction(IUBMB)

(5')pppAACA-[mRNA] + GDP = diphosphate + G(5')pppAACA-[mRNA] (overall reaction);
(1a) (5')pppAACA-[mRNA] + [protein L]-L-histidine = diphosphate + [protein L]-L-histidyl-(5')phosphonato-AACA-[mRNA] + H2O;
(1b) [protein L]-L-histidyl-(5')phosphonato-AACA-[mRNA] + GDP + H2O = [protein L]-L-histidine + G(5')pppAACA-[mRNA]

Reaction(KEGG)

(other) R11203

Substrate

5'-triphospho-mRNA [CPD:C20864];
GDP [CPD:C00035]

Product

diphosphate [CPD:C00013];
G(5')pppAACA-[mRNA];
[protein L]-L-histidyl-(5')phosphonato-AACA-[mRNA];
H2O [CPD:C00001];
[protein L]-L-histidine

Comment

The enzyme from non-segmented negative strain (NNS) viruses (e.g. rhabdoviruses and lyssaviruses) is specific for mRNAs with sequences starting with AACA. cf. EC 2.7.7.50, mRNA guanylyltransferase.

History

EC 2.7.7.88 created 2015, modified 2020

Orthology

Morbillivirus RNA-directed RNA polymerase L

Lyssavirus RNA-directed RNA polymerase L

Ebolavirus RNA-directed RNA polymerase L

Marburgvirus RNA-directed RNA polymerase L

Respirovirus RNA-directed RNA polymerase L

Henipavirus RNA-directed RNA polymerase L

Orthorubulavirus/Pararubulavirus RNA-directed RNA polymerase L

Pneumoviridae RNA-directed RNA polymerase L

Rhabdoviridae RNA-directed RNA polymerase L

Novirhabdovirus RNA-directed RNA polymerase L

Reference

1 [PMID:17218273]

Authors

Ogino T, Banerjee AK

Title

Unconventional mechanism of mRNA capping by the RNA-dependent RNA polymerase of vesicular stomatitis virus.

Journal

Mol Cell 25:85-97 (2007)
DOI:10.1016/j.molcel.2006.11.013

Reference

2 [PMID:18495767]

Authors

Ogino T, Banerjee AK

Title

Formation of guanosine(5')tetraphospho(5')adenosine cap structure by an unconventional mRNA capping enzyme of vesicular stomatitis virus.

Journal

J Virol 82:7729-34 (2008)
DOI:10.1128/JVI.00326-08

Reference

3 [PMID:20142503]

Authors

Ogino T, Yadav SP, Banerjee AK

Title

Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase.

Journal

Proc Natl Acad Sci U S A 107:3463-8 (2010)
DOI:10.1073/pnas.0913083107

Reference

4 [PMID:20107017]

Authors

Ogino T, Banerjee AK

Title

The HR motif in the RNA-dependent RNA polymerase L protein of Chandipura virus is required for unconventional mRNA-capping activity.

Journal

J Gen Virol 91:1311-4 (2010)
DOI:10.1099/vir.0.019307-0

Reference

5 [PMID:21945214]

Authors

Ogino T, Banerjee AK

Title

An unconventional pathway of mRNA cap formation by vesiculoviruses.

Journal

Virus Res 162:100-9 (2011)
DOI:10.1016/j.virusres.2011.09.012

Sequence

Reference

6 [PMID:27213429]

Authors

Ogino M, Ito N, Sugiyama M, Ogino T.

Title

The Rabies Virus L Protein Catalyzes mRNA Capping with GDP Polyribonucleotidyltransferase Activity.

Journal

Viruses 8:E144 (2016)
DOI:10.3390/v8050144

Other DBs

ExplorEnz - The Enzyme Database:

IUBMB Enzyme Nomenclature:

ExPASy - ENZYME nomenclature database:

BRENDA, the Enzyme Database:

DBGET integrated database retrieval system