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Information on EC 2.7.7.50 - mRNA guanylyltransferase and Organism(s) Vaccinia virus and UniProt Accession P04298
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2.7.7.50 mRNA guanylyltransferaseIUBMB Comments
The human enzyme is a multi domain protein that also has the activity of EC 3.6.1.74, mRNA 5'-phosphatase.
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Word Map
- 2.7.7.50
- cyclin
- photosystem
- thylakoids
-
photoinhibition
- chloroplast
- cyanobacterium
- chlorophyll
- synechocystis
-
photodamage
-
photochemical
- triphosphatase
- retinoblastoma
-
cyclin-dependent
- vaccinia
- reinhardtii
-
high-light
-
photoprotection
- 5'-triphosphatase
- qa
-
mantle
- plastoquinone
- synechococcus
-
oxygen-evolving
-
thermoluminescence
-
photoinactivation
-
xanthophyl
- 7-methylguanosine
- atrazine
-
water-splitting
- p-tefb
- lhcii
-
non-photochemical
-
alpha-32pgtp
-
water-oxidizing
-
chloroplast-encoded
- biotechnology
- vp3
- diuron
- nsp1
-
low-light
- lincomycin
-
grana
-
herbicide-resistant
- analysis
- psbo
- reoviridae
-
cap-binding
- spt5
-
photoinhibitory
-
flash-induced
-
uncapped
- thermosynechococcus
The taxonomic range for the selected organisms is: Vaccinia virus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
d1 protein, guanylyltransferase, capping enzyme, mrna capping enzyme, rna guanylyltransferase, mrna guanylyltransferase, rna capping enzyme, prntase, mrna-cap, mrna-capping enzyme, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ceg1
-
-
-
-
messenger RNA guanylyltransferase
-
-
-
-
mRNA capping enzyme
protein lambda2
-
-
-
-
RNGTT
-
-
-
-
additional information
mRNA capping enzyme
-
activities associated with vaccinia capping enzyme complex: 1. GTP-RNA guanylyltransferase, 2. RNA (guanine-7)-methyltransferase, 3. RNA triphosphatase, 4. GTP-PPi exchange, 5. nucleoside triphosphate phosphorylase
additional information
-
activities associated with vaccinia capping enzyme complex: 1. GTP-RNA guanylyltransferase, 2. RNA (guanine-7)-methyltransferase, 3. RNA triphosphatase, 4. GTP-diphosphate exchange, 5. nucleoside triphosphate phosphorylase
additional information
-
activities associated with vaccinia capping enzyme complex: 1. GTP-RNA guanylyltransferase, 2. RNA (guanine-7)-methyltransferase, 3. RNA triphosphatase, 4. GTP-diphosphate exchange, 5. nucleoside triphosphate phosphorylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
active domain between residues 520 and 545, comprises both activities, the ATPase and guanylyltransferase activity
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
mRNA containing a guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
GTP:mRNA guanylyltransferase
The human enzyme is a multi domain protein that also has the activity of EC 3.6.1.74, mRNA 5'-phosphatase.
CAS REGISTRY NUMBER
COMMENTARY
56941-23-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + ppApG
G(5')ppp(5')ApG + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + ppGpC
G(5')ppp(5')GpC + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + ppp(5')ApG
G(5')pppp(5')ApG + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
-
-
deoxyguanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
-
-
deoxyguanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the acceptor is unmethylated vaccinia virus mRNA
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
specific for GTP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
specific for GTP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
no apparent base specificity for the penultimate nucleotide, a variety of synthetic homoribopolymers and naturally occuring mRNAs are effective substrates, vaccinia virus
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
only the alpha-phosphate is transferred
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
the acceptor is diphosphate terminated poly(A)
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
enzyme can modify synthetic poly(A) to form the structure m7G(5')ppp(5')AmP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
-
specifically requires 5'-triphosphate-terminated RNA chains
-
-
r
additional information
?
-
-
activities associated with vaccinia capping enzyme complex: 1. GTP-RNA guanylyltransferase, 2. RNA (guanine-7)-methyltransferase, 3. RNA triphosphatase, 4. GTP-diphosphate exchange, 5. nucleoside triphosphate phosphorylase
-
-
?
additional information
?
-
-
activities associated with vaccinia capping enzyme complex: 1. GTP-RNA guanylyltransferase, 2. RNA (guanine-7)-methyltransferase, 3. RNA triphosphatase, 4. GTP-diphosphate exchange, 5. nucleoside triphosphate phosphorylase
-
-
?
additional information
?
-
-
lacks strict sequence specificity, homoribonucleotides containing purines are preferred, in presence of diphosphate the enzyme catalyzes the phosphorolysis of the dinucleoside triphosphate G(5')pp(5')A but not of m7(5')pp(5')A
-
-
?
additional information
?
-
-
no acceptor: RNA with a single 5'-terminal phosphate
-
-
?
additional information
?
-
-
no acceptor: RNA with a single 5'-terminal phosphate
-
-
?
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
?
additional information
?
-
-
specific post-transcriptional modification of the 5'-terminus of mRNA
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
additional information
?
-
-
specific post-transcriptional modification of the 5'-terminus of mRNA
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ribavirin triphosphate
-
concentration 200fold more than the GTP input, 50% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.013
GTP
-
pH 8.0, 37°C, guanylyltransferase activity, holoenzyme capping enzyme
0.0155
GTP
-
pH 8.0, 37°C, guanylyltransferase activity, D1R domain, residues 1-545
0.00025
RNA
-
pH 8.0, 37°C, guanylyltransferase activity, holoenzyme capping enzyme
0.0003
RNA
-
pH 8.0, 37°C, guanylyltransferase activity, D1R domain, residues 1-545
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0233
GTP
-
pH 8.0, 37°C, guanylyltransferase activity, holoenzyme capping enzyme
0.0267
GTP
-
pH 8.0, 37°C, guanylyltransferase activity, D1R domain, residues 1-545
0.0147
RNA
-
pH 8.0, 37°C, guanylyltransferase activity, D1R domain, residues 1-545
0.0187
RNA
-
pH 8.0, 37°C, guanylyltransferase activity, holoenzyme capping enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
in Dts36, a temperature sensitive virus mutant affecting the large subunit of the capping enzyme, of the three enzymatic activities required for mRNA capping, the guanylyltransferase and methyltransferase activities are compromised while the triphosphatase activity and the D12 subunit interaction are unaffected. The mutant enzyme is also defective in stimulating early gene transcription termination and intermediate gene transcription initiation in vitro
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
-
copurifies with S-adenosylmethionine mRNA (guanine-7)-methyltransferase, sucrose density gradient centrifugation and gel filtration
26400
-
x * 95000, subunit containing the active site + x * 26400, transguanylyltransferase subunit, SDS-PAGE
59000
-
x * 59000, guanylyltransferase lacking 7-methyltransferase activity, SDS-PAGE
95000
additional information
-
the capping enzyme has 2 subunits: MW 95000 and 31000, the 95000 MW subunit of the vaccinia virus capping enzyme has guanylyltransferase activity, glycerol gradient centrifugation, the isolated 95000 MW guanylyltransferase can be converted to an active 60000 MW form in vitro by limited proteolysis with trypsin, the guanylyltransferase domain is localized to the amino two-thirds of the 95000 MW polypeptide
95000
-
x * 95000, subunit containing the active site + x * 26400, transguanylyltransferase subunit, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
x * 95000, subunit containing the active site + x * 26400, transguanylyltransferase subunit, SDS-PAGE
?
-
x * 59000, guanylyltransferase lacking 7-methyltransferase activity, SDS-PAGE
additional information
-
95 kDa subunit can be transformed into an active 60 kDa form by trypsin proteolysis
additional information
-
SDS-PAGE: 95000 MW and 31400 MW polypeptides are polypeptide components of the 127000 MW enzyme system
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of the complete heterodimer formed by polypeptides D1 and D12. The D1 subunit comprises an N-terminal RNA triphosphatase (TPase)-guanylyltransferase (GTase) module and a C-terminal guanine-N7-methyltransferase (MTase) module. The D12 subunit binds and allosterically stimulates the MTase module. An extensive TPase-GTase interface clamps the GTase nucleotidyltransferase and oligosaccharide-binding fold domains in a closed conformation around GTP
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E192A
113% of wild-type guanylyltransferase activity, 4% of wild-type RNA triphosphatase activity
K478A
1% of wild-type guanylyltransferase activity, 42% of wild-type RNA triphosphatase activity
L47A/L50A/T51A
1% of wild-type guanylyltransferase activity, 43% of wild-type RNA triphosphatase activity
N181A
48% of wild-type guanylyltransferase activity, 69% of wild-type RNA triphosphatase activity
R186A
51% of wild-type guanylyltransferase activity, 92% of wild-type RNA triphosphatase activity
T10A
19% of wild-type guanylyltransferase activity, 104% of wild-type RNA triphosphatase activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, 48 h, 90% loss of activity, 59000 MW protein which lacks 7-methyltransferase activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
copurifies with S-adenosylmethionine mRNA (guanine-7)-methyltransferase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of viral D1 and D12 orfs encoded subunits in Escherichia coli BL21(DE3)
-
mutant lacking the C-terminal domain, consisting of the D1R domain, residues 1-545, expression in Escherichia coli BL21(DE3)pLysS
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
-
enzyme can be used as a tool for specific 5'-end-labeling of mRNA
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Myette J.R.; Niles E.G.
Characterization of the vaccinia virus RNA 5-triphosphatase and nucleoside triphosphate phosphohydrolase activities
J. Biol. Chem.
271
11945-11952
1996
Vaccinia virus
Martin, S.A.; Paoletti, E.; Moss, B.
Purification of mRNA guanylyltransferase and mRNA (guanine-7-) methyltransferase from vaccinia virions
J. Biol. Chem.
250
9322-9329
1975
Vaccinia virus, Vaccinia virus WR
Martin, S.A.; Moss, B.
Modification of RNA by mRNA guanylyltransferase and mRNA (guanine-7-)methyltransferase from vaccinia virions
J. Biol. Chem.
250
9330-9335
1975
Vaccinia virus
Ensinger, M.J.; Martin, S.A.; Paoletti, E.; Moss, B.
Modification of the 5-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus
Proc. Natl. Acad. Sci. USA
72
2525-2529
1975
Vaccinia virus
Martin, S.A.; Moss, B.
mRNA guanylyltransferase and mRNA (guanine-7-)-methyltransferase from vaccinia virions. Donor and acceptor substrate specificites
J. Biol. Chem.
251
7313-7321
1976
Vaccinia virus
Monroy, G.; Spencer, E.; Hurwitz, J.
Purification of mRNA guanylyltransferase from vaccinia virions
J. Biol. Chem.
253
4481-4489
1978
Vaccinia virus
Shuman, S.; Hurwitz, J.
Capping enzyme
The Enzymes, 3rd. Ed. (Boyer, P. D. , ed. )
15
245-265
1982
Homo sapiens, Rattus norvegicus, Vaccinia virus
-
Shuman, S.
Catalytic activity of vaccinia mRNA capping enzyme subunits coexpressed in Escherichia coli
J. Biol. Chem.
265
11960-11966
1990
Vaccinia virus
Shuman, S.; Morham, S.G.
Domain structure of vaccinia virus mRNA capping enzyme. Activity of the Mr 95,000 subunit expressed in Escherichia coli
J. Biol. Chem.
265
11967-11972
1990
Vaccinia virus
Monroy, G.; Spencer, E.; Hurwitz, J.
Characteristics of reactions catalyzed by purified guanylyltransferase from vaccinia virus
J. Biol. Chem.
253
4490-4498
1978
Vaccinia virus
Myette, J.R.; Niles, E.g.
Domain structure of the vaccinia virus mRNA capping enzyme. Expression in Escherichia coli of a subdomain possessing the RNA 5'-triphosphatase and guanylyltransferase activities and a kinetic comparison to the full-size enzyme
J. Biol. Chem.
271
11936-11944
1996
Vaccinia virus
Bougie, I.; Bisaillon, M.
The broad spectrum antiviral nucleoside ribavirin as a substrate for a viral RNA capping enzyme
J. Biol. Chem.
279
22124-22130
2004
Vaccinia virus
Kyrieleis, O.J.; Chang, J.; de la Pena, M.; Shuman, S.; Cusack, S.
Crystal structure of vaccinia virus mRNA capping enzyme provides insights into the mechanism and evolution of the capping apparatus
Structure
22
452-465
2014
Vaccinia virus (P04298), Vaccinia virus, Vaccinia virus Western Reserve (P04298)
Tate, J.; Boldt, R.L.; McFadden, B.D.; DCosta, S.M.; Lewandowski, N.M.; Shatzer, A.N.; Gollnick, P.; Condit, R.C.
Biochemical analysis of the multifunctional vaccinia mRNA capping enzyme encoded by a temperature sensitive virus mutant
Virology
487
27-40
2016
Vaccinia virus (P04298), Vaccinia virus, Vaccinia virus IHDW (P04298)
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