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Information on EC 2.7.7.50 - mRNA guanylyltransferase and Organism(s) Paramecium bursaria Chlorella virus 1 and UniProt Accession Q84424

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EC Tree
     2 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.50 mRNA guanylyltransferase
IUBMB 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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Paramecium bursaria Chlorella virus 1
UNIPROT: Q84424
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The taxonomic range for the selected organisms is: Paramecium bursaria Chlorella virus 1
The enzyme appears in selected viruses and cellular organisms
Synonyms
d1 protein, guanylyltransferase, capping enzyme, mrna capping enzyme, rna guanylyltransferase, mrna guanylyltransferase, prntase, rna capping enzyme, mrna-cap, mrna-capping enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanylyltransferase mRNA capping
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Ceg1
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messenger RNA guanylyltransferase
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-
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mRNA guanylyl transferase
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protein lambda2
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-
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RNA guanylyltransferase
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RNGTT
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
-
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PATHWAY SOURCE
PATHWAYS
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-
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 hide
56941-23-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-fluoro-2'-deoxy-GTP + pp(5')RNA
2'-fluoro-2'-deoxy-G(5')ppp(5')RNA + diphosphate
show the reaction diagram
0.16fold efficiency compared with substrate GTP
-
-
?
2-amino-6-chloropurine-beta-D-ribose triphosphate + pp(5')RNA
2-amino-6-chloropurine-beta-D-ribose-(5')ppp(5')RNA + diphosphate
show the reaction diagram
0.08fold efficiency compared with substrate GTP
-
-
?
3'-deoxy-GTP + pp(5')RNA
3'-deoxy-G(5')ppp(5')RNA + diphosphate
show the reaction diagram
0.15fold efficiency compared with substrate GTP
-
-
?
3'-O-methyl-GTP + pp(5')RNA
3'-O-methyl-G(5')ppp(5')RNA + diphosphate
show the reaction diagram
0.38fold efficiency compared with substrate GTP
-
-
?
6-methylthio-GTP + pp(5')RNA
6-methylthio-G(5')ppp(5')RNA + diphosphate
show the reaction diagram
0.07fold efficiency compared with substrate GTP
-
-
?
6-thio-GTP + pp(5')RNA
6-thio-G(5')ppp(5')RNA + diphosphate
show the reaction diagram
0.16fold efficiency compared with substrate GTP
-
-
?
8-bromo-GTP + pp(5')RNA
8-bromo-G(5')ppp(5')RNA + diphosphate
show the reaction diagram
0.40fold efficiency compared with substrate GTP
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-
?
8-iodoGTP + pp(5')RNA
8-iodo-G(5')ppp(5')RNA + diphosphate
show the reaction diagram
1.0fold efficiency compared with substrate GTP
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
-
?
ITP + pp(5')RNA
I(5')ppp(5')RNA + diphosphate
show the reaction diagram
1.3fold efficiency compared with substrate GTP
-
-
?
N1-methyl-GTP + pp(5')RNA
N1-methyl-G(5')ppp(5')RNA + diphosphate
show the reaction diagram
1.1fold efficiency compared with substrate GTP
-
-
?
O6-methyl-GTP + pp(5')RNA
O6-methyl-G(5')ppp(5')RNA + diphosphate
show the reaction diagram
0.48fold efficiency compared with substrate GTP
-
-
?
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
show the reaction diagram
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
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guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
additional information
?
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generation of RNAs harboring various different cap analogues. Cap-dependent translation can occur in the absence of theN7-methyl group on the cap structure provided that alternative modifications enable appropriate binding to eIF4E
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
show the reaction diagram
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-amino-6-chloropurine-ribose triphosphate
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sodium phosphonoformate
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foscarnet, inhibition of the formation of the covalent intermediate at 5 mM
tetrapotassium diphosphate
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inhibition of the formation of the covalent intermediate at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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kinetic analysis of forward and reverse reactions by real-time fluorescence spectroscopy and radioactive kinetic assays, thermodynamics, overview
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
inhibition kinetic analysis of both steps of forward and reverse reactions, overview
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
2'-fluoro-2'-deoxy-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.16
2-amino-6-chloropurine-ribose triphosphate
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.15
3'-deoxy-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.45
3'-O-Methyl-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.43
6-methylthio-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.22
6-thio-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
1.5
8-bromo-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.42
8-iodoGTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.1
GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.34
ITP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.08
N1-methyl-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
0.15
O6-methyl-GTP
Paramecium bursaria Chlorella virus 1
IC50 value for formation of enzyme-GMP-complex, pH 7.5, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MCE_PBCV1
330
0
37832
Swiss-Prot
other Location (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
empirical and thermodynamic integration pKa estimates, along with conventional molecular dynamics simulations based on PDB entries 1ckm and 1ckn. Magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation
crystals of RNA guanylyltransferase, i.e. capping enzyme, complexed with a mRNA cap analogue G(5')ppp(5')G, enzyme solution: 15 mg/ml, 1.3 mM GpppG, 50 mM Tris, pH 7.5, 0.4 M NaCl, 2 mM EDTA, 4 mM DTT, mixed with equal volume of equilibration solution: potassium phosphate 50 mM, pH 6.5, 5-10% PEG 8000, 2 mM ZnCl2, 24 h, X-ray structure determination and analysis
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged A103R protein from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene A103R, expression of His6-tagged A103R protein in Escherichia coli strain BL21(DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hakansson, K.; Wigley, D.B.
Structure of a complex between a cap analog and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping
Proc. Natl. Acad. Sci. USA
95
1505-1510
1998
Paramecium bursaria Chlorella virus 1
Manually annotated by BRENDA team
Souliere, M.F.; Perreault, J.P.; Bisaillon, M.
Kinetic and thermodynamic characterization of the RNA guanylyltransferase reaction
Biochemistry
47
3863-3874
2008
Paramecium bursaria Chlorella virus 1
Manually annotated by BRENDA team
Swift, R.V.; Ong, C.D.; Amaro, R.E.
Magnesium-induced nucleophile activation in the guanylyltransferase mRNA capping enzyme
Biochemistry
51
10236-10243
2012
Paramecium bursaria Chlorella virus 1 (Q84424)
Manually annotated by BRENDA team
Issur, M.; Bougie, I.; Despins, S.; Bisaillon, M.
Enzymatic synthesis of RNAs capped with nucleotide analogues reveals the molecular basis for substrate selectivity of RNA capping enzyme: impacts on RNA metabolism
PLoS ONE
8
e75310
2013
Paramecium bursaria Chlorella virus 1 (Q84424)
Manually annotated by BRENDA team