Information on EC 2.7.7.50 - mRNA guanylyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
2.7.7.50
-
RECOMMENDED NAME
GeneOntology No.
mRNA guanylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
The enzyme can also modify synthetic poly(A) and poly(G) to form the structures m7G(5')ppp(5')An and m7G(5')ppp(5')Gn
-
-
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
mechanism of capping; mRNA containing a guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
mechanism of capping; mRNA containing a guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
mechanism of capping; mRNA containing a guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
active site
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
active domain between residues 520 and 545, comprises both activities, the ATPase and guanylyltransferase activity
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
conserved KXDG-motif; Lys294 is located in the active site in a KXDG-conserved motif
O55236
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
guanylyltransferase domain: residues 211-597
O55236
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
mechanism of intermediate formation
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
conserved KXDG-motif
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
active site; active site Lys190
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
active site Lys177; conserved KXDG-motif
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
ATP/GTP-binding-site motif A, residues 379-386
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
RNA guanylyltransferase activity is involved in the synthesis of the cap structure found at the 5' end of eukaryotic mRNAs. The RNA guanylyltransferase activity is a two-step ping-pong reaction in which the enzyme first reacts with GTP to produce the enzyme-GMP covalent intermediate with the concomitant release of diphosphate. In the second step of the reaction, the GMP moiety is then transferred to a diphosphorylated RNA. Both reactions are reversible. The second step comprises the limiting steps for both the direct and reverse overall reactions
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
GTP:RNA GTase, the GTase component of MimiCE, catalyzes a reversible two-step ping-pong reaction. The first step entails nucleophilic attack of the enzyme at the a phosphorus of GTP to form a covalent enzyme-(lysyl-N)-GMP intermediate plus pyrophosphate. In the second step, the beta-phosphate of 50 diphosphate-terminated RNA attacks the enzyme-GMP intermediate to form the GpppRNA cap and expel the lysine nucleophile
Q5UQX1
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
Q84424
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
ATP/GTP-binding-site motif A, residues 379-386
Avian orthoreovirus 1733
-
-
GTP + (5')ppPur-mRNA = diphosphate + G(5')pppPur-mRNA
show the reaction diagram
active site; active site Lys190
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
mRNA capping I
-
SYSTEMATIC NAME
IUBMB Comments
GTP:mRNA guanylyltransferase
The enzyme can also modify synthetic poly(A) and poly(G) to form the structures m7G(5')pppAn and m7G(5')pppGn.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
cap guanylyltransferase-methyltransferase
-
bifunctional capping enzyme consisting of an amino-terminal guanylyltransferase domain and a carboxyl-terminal methyltransferase domain
capping enzyme
O60942
-
capping enzyme
O55236
-
capping enzyme
-
-
capping enzyme guanylyltransferase
-
-
capping enzyme guanylyltransferase
Cyanidioschyzon merolae CMA035C
-
-
-
capping enzyme guanylyltransferase
-
-
CmCeg1
Cyanidioschyzon merolae CMA035C
-
-
-
D1 protein
-
-
guanylyltransferase mRNA capping
Q84424
-
HCE
O60942
-
mRNA capping enzyme
-
-
mRNA capping enzyme
-
has mRNA guanylyltransferase and RNA 5'-triphosphatase activity
mRNA capping enzyme
-
-
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
mRNA guanylyl transferase
-
-
mRNA-capping enzyme
-
-
protein lambda2
-
-
-
-
RNA capping enzyme
-
-
RNA guanylyltransferase
-
-
TTM-type RTPase-GTase
-
-
messenger RNA guanylyltransferase
-
-
-
-
additional information
bluetongue virus serotype 10
-
the capping enzyme complex contains RNA 5'-triphosphatase, RNA guanylyltransferase and pyrophosphatase activities
additional information
-
mRNA capping apparatus consists of separate triphosphatase and guanylyltransferase components (GlCeg1)
additional information
Cyanidioschyzon merolae CMA035C
-
mRNA capping apparatus consists of separate triphosphatase and guanylyltransferase components (GlCeg1)
-
additional information
-
mRNA capping apparatus consists of separate triphosphatase and guanylyltransferase components (GlCeg1)
additional information
O55236
enzyme is part of the bifunctional capping enzyme, which consists of autonomous and non-overlapping RNA 5'-triphosphatase and a RNA guanylyltransferase domain and activity
additional information
-
enzyme is part of the bifunctional capping enzyme, which consists of autonomous and non-overlapping RNA 5'-triphosphatase and a RNA guanylyltransferase domain and activity; RNA 5'-triphosphatase and a RNA guanylyltransferase form a heterodimeric complex
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
CAS REGISTRY NUMBER
COMMENTARY
56941-23-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
a giant virus of amoeba, e.g. isolated parasite of Acanthamoeba polyphaga
Uniprot
Manually annotated by BRENDA team
i.e. baculovirus; LEF-4 subunit of DNA-dependent RNA-polymerase
-
-
Manually annotated by BRENDA team
l3 genome segment, protein lambdaC; strain 1733
-
-
Manually annotated by BRENDA team
Avian orthoreovirus 1733
strain 1733
-
-
Manually annotated by BRENDA team
bluetongue virus serotype 10
from infected Spodoptera frugiperda cells via baculovirus; i.e. BTV serotype 10; mino core protein VP4
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
Cyanidioschyzon merolae CMA035C
CMA035C
-
-
Manually annotated by BRENDA team
viral polyprotein
UniProt
Manually annotated by BRENDA team
Dengue virus 16681
viral polyprotein
UniProt
Manually annotated by BRENDA team
Orf3p gene product
-
-
Manually annotated by BRENDA team
from infected mouse fibroblasts; strain Dearing
-
-
Manually annotated by BRENDA team
from infected Trichoplusia ni insect cells via baculovirus; strain Dearing
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
mRNA capping enzyme
SwissProt
Manually annotated by BRENDA team
crystal structure: Protein Data Bank 1CKO
-
-
Manually annotated by BRENDA team
gene CEG1, encoding the alpha-subunit
-
-
Manually annotated by BRENDA team
gene CEG1; RNA 5'-triphosphatase-deficient mutant strain
-
-
Manually annotated by BRENDA team
gene CEG1; temperature-sensitive growth defect mutant ceg1-25
-
-
Manually annotated by BRENDA team
pep4, protease-deficient mutant
-
-
Manually annotated by BRENDA team
from infected Nicotiana tabacum leaves; i.e. TMV
-
-
Manually annotated by BRENDA team
strain WR
-
-
Manually annotated by BRENDA team
strain WR
-
-
Manually annotated by BRENDA team
viral polyprotein
Uniprot
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
no activity
-
-
-
dGTP + pp(5')RNA
dG(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
low activity
deoxyguanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
show the reaction diagram
-
-
-
-
r
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
show the reaction diagram
-
-
-
-
?
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
show the reaction diagram
Q5UQX1
-, active site structure, overview
-
-
r
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
show the reaction diagram
-
two-step reaction, usage of a synthetic RNA substrate of 81 nucleotides from a PCR template encoding the 5' terminal portion of the PBCV-1 DNA polymerase gene, with a T7 RNA polymerase promoter, assay method development and evaluation, overview
-
-
r
GTP + pp(5')ApGp
G(5')ppp(5')ApGp + diphosphate
show the reaction diagram
-
-
-
-
ir
GTP + pp(5')ApGp
G(5')ppp(5')ApGp + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + pp(5')ApGp
G(5')ppp(5')ApGp + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
?
GTP + pp(5')GpCpC
G(5')ppp(5')GpCpC + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + pp(5')GpXp
G(5')ppp(5')GpXp + diphosphate
show the reaction diagram
bluetongue virus serotype 10
-
-
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
show the reaction diagram
-
-
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
Q9INI4
-
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
O55236
-
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
show the reaction diagram
O60942
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
specific for GTP
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
show the reaction diagram
-
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
show the reaction diagram
-
reversible formation of a covalent intermediate enzyme-GMP
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
show the reaction diagram
-
reversible formation of a covalent intermediate enzyme-GMP
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
show the reaction diagram
-
reversible formation of a covalent intermediate enzyme-GMP
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
show the reaction diagram
bluetongue virus serotype 10
-
reversible formation of a covalent intermediate enzyme-GMP
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the acceptor is diphosphate terminated poly(A)
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
show the reaction diagram
-
the acceptor is diphosphate terminated poly(A)
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir, r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
the acceptor is diphosphate terminated poly(A)
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
show the reaction diagram
-
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
show the reaction diagram
-
GMP is linked to the enzyme via a phosphoamide bond to the epsilon-amino group of Lys70
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
show the reaction diagram
O55236
the enzymes isolated guanylyltransferase domian, residues 211-597, is catalytically active in vitro
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
show the reaction diagram
-
GMP is linked to the enzyme via a phosphoamide bond
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
show the reaction diagram
bluetongue virus serotype 10
-
GMP is linked to the enzyme via a phosphoamide bond
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
show the reaction diagram
-
GMP is linked to the enzyme via a phosphoamide bond
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
show the reaction diagram
-
enzyme can transfer its bound GMP to GDP
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
show the reaction diagram
-
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 + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
formation of a covalent intermediate enzyme-GMP
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
show the reaction diagram
-
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
formation of a covalent intermediate enzyme-GMP
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
show the reaction diagram
O55236
formation of a covalent intermediate enzyme-GMP
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
show the reaction diagram
-
formation of a covalent intermediate enzyme-GMP
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
show the reaction diagram
-
interaction of RNA 5'-triphosphatase and mRNA guanylyltransferase of the capping enzyme complex is essential for function and viability in vivo
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
interaction of RNA 5'-triphosphatase and mRNA guanylyltransferase of the capping enzyme complex is essential for function and viability in vivo, yeast RNA 5'-triphosphatase enzyme can be substituted by the enzyme of Candida albicans, but not by the human enzyme, to function in the capping enzyme complex together with the mRNA guanylyltransferase
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
show the reaction diagram
-
mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
O55236
mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo
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
show the reaction diagram
-
molecular basis of substrate recognition by the RNA-capping enzyme
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
the forward guanylylation reaction of the capping enzyme is in equilibrium with the reverse diphosphorolysis reaction, in which diphosphate attacks the enzyme-GMP complex to regenerate GMP
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
the forward guanylylation reaction of the capping enzyme is in equilibrium with the reverse pyrophosphorolysis reaction, in which diphosphate attacks the enzyme-GMP complex to regenerate GMP
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
Cyanidioschyzon merolae CMA035C
-
-, the forward guanylylation reaction of the capping enzyme is in equilibrium with the reverse diphosphorolysis reaction, in which diphosphate attacks the enzyme-GMP complex to regenerate GMP
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
Avian orthoreovirus 1733
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
reversible formation of a covalent intermediate enzyme-GMP
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
show the reaction diagram
-
GMP is linked to the enzyme via a phosphoamide bond, enzyme can transfer its bound GMP to GDP, formation of a covalent intermediate enzyme-GMP
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + ppApG
G(5')ppp(5')ApG + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
r
GTP + ppGpC
G(5')ppp(5')GpC + diphosphate
show the reaction diagram
-
-
-
ir
GTP + ppGpC
G(5')ppp(5')GpC + diphosphate
show the reaction diagram
-
-
-
ir
GTP + ppGpC
G(5')ppp(5')GpC + diphosphate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
-
-
ir
GTP + ppp(5')ApG
G(5')pppp(5')ApG + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
GTP + ppp(5')ApGp
G(5')pppp(5')ApGp + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
?
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
show the reaction diagram
-
-
-
-
?
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
ir
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
?
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
show the reaction diagram
-
-
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
show the reaction diagram
-
specifically requires 5'-triphosphate-terminated RNA chains
-
-
r
GTP + pppGpCpC
G(5')pppp(5')GpCpC + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
GTPgammaS + pp(5')RNA
?
show the reaction diagram
-
-
-
-
r
GTPgammaS + pp(5')RNA
?
show the reaction diagram
-
no activity
-
-
-
ITP + pp(5')RNA
I(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
inosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
NTP + H2O
NDP + phosphate
show the reaction diagram
-
-
-
-
?
pppG + ppp(5')A(pA)n
?
show the reaction diagram
-
-
-
-
?
ITP + pp(5')RNA
I(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
inosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
additional information
?
-
-
specificity overview
-
-
-
additional information
?
-
-
specificity overview
-
-
-
additional information
?
-
-
specificity overview
-
-
-
additional information
?
-
-
specificity overview
-
-
-
additional information
?
-
-
no activity with ATP
-
-
-
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
?
-
-
no activity with GMP, no acceptor: RNA with 5'-hydroxyl terminus
-
-
-
additional information
?
-
-
no activity with GDP
-
-
-
additional information
?
-
-
no activity with GDP
-
-
-
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: ppGp, in absence of acceptor RNA, the enzyme forms a nucleotidyl intermediate by phosphoamidate linkage of GMP
-
-
-
additional information
?
-
-
no activity with m7GTP
-
-
-
additional information
?
-
O55236
enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
-
-
-
additional information
?
-
O60942
enzyme also contains RNA 5'-triphosphatase activity, located at the N-terminus
-
-
-
additional information
?
-
-
autoguanylylation
-
-
-
additional information
?
-
-
autoguanylylation
-
-
-
additional information
?
-
-
little sequence specificity for RNA acceptor
-
-
-
additional information
?
-
-
no donor: 7-methylGTP
-
-
-
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
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
-
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
-
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
-
additional information
?
-
bluetongue virus serotype 10
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
-
additional information
?
-
-
enzyme forms a covalent enzyme-GTP intermediate of apparent MW 45000
-
-
-
additional information
?
-
-
no activity with ATP, CTP, UTP
-
-
-
additional information
?
-
-
no activity with ATP, CTP, UTP
-
-
-
additional information
?
-
-
no activity with ATP, CTP, UTP
-
-
-
additional information
?
-
O55236
phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
-
-
-
additional information
?
-
-
mRNA capping enzyme
-
-
-
additional information
?
-
-
mRNA capping enzyme
-
-
-
additional information
?
-
-
mRNA capping enzyme
-
-
-
additional information
?
-
-
RNA polymerase II primary transcripts are substrates for the cellular capping enzyme
-
-
-
additional information
?
-
-
specific post-transcriptional modification of the 5'-terminus of mRNA
-
-
-
additional information
?
-
Q5UQX1
the virus possesses a trifunctional capping enzyme composed of a metal-dependent RTPase module fused to guanylyltransferase and guanine-N7 methyltransferase domains with a minimized tunnel fold and an active site strikingly similar to that of yeast Cet1. GTP:RNA GTase is the GTase component of MimiCE, detection of GTase activity by label transfer from radiolabeled GTP to the enzyme, formation of an SDS-stable about 75 kDa nucleotidyl-protein adduct
-
-
-
additional information
?
-
-
bifunctional enzyme catalyzing GTP methylation and subsequent transfer of the m7GMP moiety from m7GTP to the 5'-diphosphate end of viral RNA
-
-
-
additional information
?
-
Avian orthoreovirus 1733
-
autoguanylylation
-
-
-
additional information
?
-
-
enzyme also catalyzes GTP-diphosphate exchange
-
-
-
additional information
?
-
-
autoguanylylation
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
show the reaction diagram
-
-
-
-
r
GTP + (5')ppPur-mRNA
diphosphate + G(5')pppPur-mRNA
show the reaction diagram
Q5UQX1
-
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
-
-
r
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue
ir
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
interaction of RNA 5'-triphosphatase and mRNA guanylyltransferase of the capping enzyme complex is essential for function and viability in vivo
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
-
interaction of RNA 5'-triphosphatase and mRNA guanylyltransferase of the capping enzyme complex is essential for function and viability in vivo, yeast RNA 5'-triphosphatase enzyme can be substituted by the enzyme of Candida albicans, but not by the human enzyme, to function in the capping enzyme complex together with the mRNA guanylyltransferase
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
show the reaction diagram
-
mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo
-
-
?
GTP + pp(5')RNA
G(5')ppp(5')RNA + diphosphate
show the reaction diagram
O55236
mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo
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
show the reaction diagram
Cyanidioschyzon merolae CMA035C
-
-
-
-
r
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
ir
NTP + H2O
NDP + phosphate
show the reaction diagram
-
-
-
-
?
GTP + ppp(5')RNA
G(5')pppp(5')RNA + diphosphate
show the reaction diagram
-
-
guanosine residue linked 5' through four phosphates to the 5' position of the terminal residue
r
additional information
?
-
O55236
phosphorylated C-terminal domain of RNA polymerase II couples capping to transcription elongation, which results in selective capping of RNA polymerase II transcripts
-
-
-
additional information
?
-
-
mRNA capping enzyme
-
-
-
additional information
?
-
-
mRNA capping enzyme
-
-
-
additional information
?
-
-
mRNA capping enzyme
-
-
-
additional information
?
-
-
RNA polymerase II primary transcripts are substrates for the cellular capping enzyme
-
-
-
additional information
?
-
-
specific post-transcriptional modification of the 5'-terminus of mRNA
-
-
-
additional information
?
-
Q5UQX1
the virus possesses a trifunctional capping enzyme composed of a metal-dependent RTPase module fused to guanylyltransferase and guanine-N7 methyltransferase domains with a minimized tunnel fold and an active site strikingly similar to that of yeast Cet1. GTP:RNA GTase is the GTase component of MimiCE
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
can partially replace Mg2+ in activation
Co2+
Q5UQX1
30% of the activity with Mg2+
K+
-
stimulates, maximal activation at 6 mM KCl
Mg2+
-
25% of the activity with Mn2+; can partially replace Mn2+ in activation; required
Mg2+
-
can partially replace Mn2+ in activation
Mg2+
-
maximal activity at 3 mM; required
Mg2+
-
maximal activity at 0.5 mM; required
Mg2+
-
can partially replace Mn2+ in activation
Mg2+
-
can partially replace Mn2+ in activation; maximal activity at 2-5 mM
Mg2+
-
maximal activity at 0.5-2 mM; required
Mg2+
O55236
enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred; optimal at 5-10 mM
Mg2+
-
enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred; maximal at 20-40 mM, LEF-4 subunit
Mg2+
-
required
Mg2+
Q9INI4
required
Mg2+
-
required
Mg2+
Q5UQX1
both reaction steps are dependent on divalent metal ions
Mg2+
Q84424
magnesium binding likely activates the lysine nucleophile by increasing its acidity and by biasing the deprotonated nucleophile into conformations conducive to intermediate formation
Mn2+
-
11% of the activity with Mg2+; can partially replace Mg2+ in activation
Mn2+
-
can partially replace Mg2+ in activation; maximal activity at 2 mM; required
Mn2+
-
can partially replace Mg2+ in activation; required
Mn2+
-
10% of the activity with Mg2+; can partially replace Mg2+ in activation; inhibits in presence of Mg2+; maximal activity at 1 mM
Mn2+
-
required
Mn2+
-
maximal activity at 2 mM; required
Mn2+
-
can partially replace Mg2+ in activation
Mn2+
O55236
enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred; optimal at 1-2 mM
Mn2+
-
enzyme-GMP intermediate formation is strictly dependent on divalent cations, satisfied by Mn2+ or Mg2+, Mn2+ is slightly preferred; maximal at 5 mM, LEF-4 subunit
Mn2+
-
Mn2+ is a more effective cofactor than Mg2+ at concentrations below 0.5 mM but is progressively less at higher concentrations
Na+
-
stimulates, maximal activation at 50-75 mM NaCl
Mn2+
Q5UQX1
30% of the activity with Mg2+
additional information
-
no activation by Ca2+ or Zn2+
additional information
-
requirement for divalent cations
additional information
O55236
requirement for divalent cations
additional information
-
requirement for divalent cations
additional information
-
Ca2+, Cu2+, and Zn2+ do not support the activity at 2 mM
additional information
Q5UQX1
Cd2+, Ca2+, and Zn2+ are less effective, no activity with Cu2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-[(5Z)-5-(2,3-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-, P29990
-
3-[(5Z)-5-(2,3-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
P03314, -
-
3-[(5Z)-5-(2,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-, P29990
-
3-[(5Z)-5-(2,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
P03314, -
-
3-[(5Z)-5-(4-tert-butylbenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-, P29990
compound shows significant antiviral activity in a dengue virus subgenomic replicon assay and is able to reduce the replication of infectious West Nile virus and yellow fever virus in cell culture with low toxicity
3-[(5Z)-5-(4-tert-butylbenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
P03314, -
compound shows significant antiviral activity in a dengue virus subgenomic replicon assay and is able to reduce the replication of infectious West Nile virus and yellow fever virus in cell culture with low toxicity
Co2+
-
above 0.1 mM
diphosphate
-
-
diphosphate
-
-
diphosphate
-
strong product inhibition
diphosphate
-
50% at 0.005 mM, complete at 0.05 mM
diphosphate
-
50% at 0.005 mM, complete at 0.05 mM
diphosphate
-
95% inhibition at 0.5 mM
mizoribine 5'-phosphate
-
compound can inhibit the formation of the RNA cap structure catalyzed by human capping enzyme. In the presence of mizoribine 5'-phosphate, the RNA 5'-triphosphatase activity appears to be relatively unaffected while the RNA guanylyltransferase activity is inhibited. Mizoribine 5'-phosphate is a non-competitive inhibitor that likely targets an allosteric site
N-ethylmaleimide
-
-
NaCl
-
90% inhibition at 0.3 M
phosphate
-
above 20 mM
phosphate
-
weak
ribavirin triphosphate
-
concentration 200fold more than the GTP input, 50% inhibition
sodium phosphonoformate
-
foscarnet, inhibition of the formation of the covalent intermediate at 5 mM
tetrapotassium diphosphate
-
inhibition of the formation of the covalent intermediate at 5 mM
Zn2+
-
above 10 mM
[(5Z)-4-oxo-5-(4-phenoxybenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-, P29990
-
[(5Z)-4-oxo-5-(4-phenoxybenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
P03314, -
-
[(5Z)-5-(3,5-diiodo-2-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-, P29990
-
[(5Z)-5-(3,5-diiodo-2-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
P03314, -
-
[(5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-, P29990
-
[(5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
P03314, -
-
Mn2+
-
can partially replace Mg2+ in activation, inhibits in presence of Mg2+
additional information
-
no inhibition by alpha-amanitin
-
additional information
-
no inhibition by S-adenosylmethionine and S-adenosylhomocysteine
-
additional information
-
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Bovine serum albumin
-
stimulates
-
RNA 5'-triphosphatase
-
binding in the capping enzyme complex stimulates the mRNA guanylyltransferase by 10fold, icreases affinity for GTP
-
S-adenosylmethionine
-
stimulates up to 2fold
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2
-
diphosphate
-
pH 7.0, 37C
0.019
-
diphosphate terminated poly(A) with an average chain length of 2000 nucleotides
-
-
-
0.000019
-
diphosphate-ended poly(A)
-
pH 7.5, 37C
-
0.0011
-
GTP
-
pH 7.5, 37C
0.0027
-
GTP
-
pH 7.9, 37C
0.013
-
GTP
-
pH 8.0, 37C, guanylyltransferase activity, holoenzyme capping enzyme
0.015
-
GTP
-
pH 7.8, 37C
0.0155
-
GTP
-
pH 8.0, 37C, guanylyltransferase activity, D1R domain, residues 1-545
0.017
-
GTP
-
pH 7.8, 37C
0.000014
-
pp(5')A(pA)n
-
pH 7.9, 37C
-
0.000285
-
pp(5')ApGp
-
pH 7.8, 37C
-
0.000285
-
pp(5')ApGp
-
pH 7.5, 37C
-
0.0005
-
pp(5')GCC(A2,U2G)n
-
2 Km values: 0.0005 and 0.004 mM, pH 7.0, 37C
-
0.004
-
pp(5')GCC(A2,U2G)n
-
2 Km values: 0.0005 and 0.004 mM, pH 7.0, 37C
-
0.00025
-
RNA
-
pH 8.0, 37C, guanylyltransferase activity, holoenzyme capping enzyme
0.0003
-
RNA
-
pH 8.0, 37C, guanylyltransferase activity, D1R domain, residues 1-545
0.0002
-
termini of 5'-triphosphate poly(A)
-
pH 7.8, 37C
-
0.00014
-
lambdac17RNA
-
pH 7.5, 37C
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
half-maximal guanylylation is achieved at 0.00009 mM GTP
-
additional information
-
additional information
-
kinetic analysis of forward and reverse reactions by real-time fluorescence spectroscopy and radioactive kinetic assays, thermodynamics, overview
-
additional information
-
additional information
Q5UQX1
kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0233
-
GTP
-
pH 8.0, 37C, guanylyltransferase activity, holoenzyme capping enzyme
0.0267
-
GTP
-
pH 8.0, 37C, guanylyltransferase activity, D1R domain, residues 1-545
0.0147
-
RNA
-
pH 8.0, 37C, guanylyltransferase activity, D1R domain, residues 1-545
0.0187
-
RNA
-
pH 8.0, 37C, guanylyltransferase activity, holoenzyme capping enzyme
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0099
-
3-[(5Z)-5-(2,3-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-, P29990
37C, pH not specified in the publication
0.016
-
3-[(5Z)-5-(2,3-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
P03314, -
37C, pH not specified in the publication
0.009
-
3-[(5Z)-5-(2,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
P03314, -
37C, pH not specified in the publication
0.0098
-
3-[(5Z)-5-(2,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-, P29990
37C, pH not specified in the publication
0.0075
-
3-[(5Z)-5-(4-tert-butylbenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-, P29990
37C, pH not specified in the publication
0.004
-
[(5Z)-4-oxo-5-(4-phenoxybenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-, P29990
37C, pH not specified in the publication
0.0077
-
[(5Z)-4-oxo-5-(4-phenoxybenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
P03314, -
37C, pH not specified in the publication
0.0015
-
[(5Z)-5-(3,5-diiodo-2-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-, P29990
37C, pH not specified in the publication
0.0046
-
[(5Z)-5-(3,5-diiodo-2-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
P03314, -
37C, pH not specified in the publication
0.0029
-
[(5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-, P29990
37C, pH not specified in the publication
0.0044
-
[(5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
P03314, -
37C, pH not specified in the publication
0.0095
-
3-[(5Z)-5-(4-tert-butylbenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
P03314, -
37C, pH not specified in the publication
additional information
-
additional information
-
inhibition kinetic analysis of both steps of forward and reverse reactions, overview
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1557
-
3-[(5Z)-5-(2,3-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-, P29990
37C, pH not specified in the publication
0.1557
-
3-[(5Z)-5-(2,3-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
P03314, -
37C, pH not specified in the publication
0.0026
-
3-[(5Z)-5-(2,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-, P29990
37C, pH not specified in the publication
0.0026
-
3-[(5Z)-5-(2,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
P03314, -
37C, pH not specified in the publication
0.0073
-
3-[(5Z)-5-(4-tert-butylbenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
-, P29990
37C, pH not specified in the publication
0.0073
-
3-[(5Z)-5-(4-tert-butylbenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]propanoic acid
P03314, -
37C, pH not specified in the publication
0.0088
-
[(5Z)-4-oxo-5-(4-phenoxybenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-, P29990
37C, pH not specified in the publication
0.0088
-
[(5Z)-4-oxo-5-(4-phenoxybenzylidene)-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
P03314, -
37C, pH not specified in the publication
0.0069
-
[(5Z)-5-(3,5-diiodo-2-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-, P29990
37C, pH not specified in the publication
0.0069
-
[(5Z)-5-(3,5-diiodo-2-methoxybenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
P03314, -
37C, pH not specified in the publication
0.0078
-
[(5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
-, P29990
37C, pH not specified in the publication
0.0078
-
[(5Z)-5-[4-(benzyloxy)benzylidene]-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]acetic acid
P03314, -
37C, pH not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00003
-
-
purified enzyme
0.00003
-
-
purified enzyme
0.000064
-
-
purified enzyme
0.000066
-
-
-
0.00007
-
-
purified enzyme
0.00027
-
-
-
0.0042
-
-
purified mutant, residues 1-545, D1R domain mutant, ATPase activity
0.00723
-
-
purified enzyme
0.03
-
-
purified enzyme
2.58
-
-
purified recombinant enzyme
7.27
-
-
purified enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
in 50 mM Tris-HCl
7.5
-
-
assay at
7.5
-
bluetongue virus serotype 10
-
assay at
7.8
-
-
assay at
7.8
-
-
assay at; Tris-HCl buffer
7.8
-
-
assay at
7.9
-
-
assay at
7.9
-
-
assay at
8
-
-
assay at
8
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
9.5
Q5UQX1
15% of maximal activity at pH 5.5, 45% at pH 9.5
6.4
7.9
-
pH 6.4: about 30% of activity maximum, pH 7.9: about 25% of activity maximum
6.5
8.5
-
pH 6.5: about 45% of activity maximum, pH 8.5: about 15% of activity maximum
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
bluetongue virus serotype 10
-
assay at
30
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
O55236
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
single recombinant LEF-4 subunit is cytosolic, but the whole RNA polymerase complex is targeted to the nucleus in baculovirus infected cells
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
28000
-
O55236
catalytically active residues 211-597, i.e. RNA guanylyltransferase domain, glycerol gradient sedimentation
42000
-
-
SDS-PAGE
46000
-
O55236
residues 1-210, i.e. RNA triphosphatase domain, glycerol gradient sedimentation
48500
-
-
sucrose density gradient sedimentation
54000
-
-
LEF-4 subunit at 0.4 M KCl, gel filtration
65000
-
-
gel filtration
68000
-
O55236
mRNA capping enzyme, glycerol density gradient sedimentation
114200
-
-
LEF-4 subunit forming dimers in solution by weak ionic interactions, gel filtration
120000
-
-
copurifies with S-adenosylmethionine mRNA (guanine-7)-methyltransferase, sucrose density gradient centrifugation and gel filtration
127000
-
-
gel filtration, sucrose density gradient sedimentation
130000
-
-
gel filtration
140000
-
-
glycerol density gradient sedimentation
180000
-
-
glycerol density gradient sedimentation
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
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 59000, guanylyltransferase lacking 7-methyltransferase activity, SDS-PAGE
?
-
x * 80000, beta, RNA 5'-triphosphatase + x * 52000, alpha, mRNA guanylyltransferase activity, SDS-PAGE
?
-
x * 95000, subunit containing the active site + x * 26400, transguanylyltransferase subunit, SDS-PAGE
?
-
x * 95000 + x * 31000, SDS-PAGE
?
-
x * 45000-52000, SDS-PAGE
?
-
x * 65000, SDS-PAGE
?
-
1 * 54000, LEF-4 subunit, SDS-PAGE, monomeric in solution as recombinant protein, in vivo part of RNA polymerase
?
-
x * 67000, covalent enzyme-GMP complex, SDS-PAGE
?
-
x * 140000-142200, protein lambdaC, SDS-PAGE and amino acid sequence determination
?
-
x * 69000, SDS-PAGE
?
Avian orthoreovirus 1733
-
x * 140000-142200, protein lambdaC, SDS-PAGE and amino acid sequence determination
-
?
-
x * 59000, guanylyltransferase lacking 7-methyltransferase activity, SDS-PAGE
-
monomer
O55236
1 * 46000, catalytically active residues 211-597, i.e. guanylyltransferase domain, + 1 * 28000, residues 1-210, i.e. RNA triphosphatase domain, SDS-PAGE
monomer
-
the enzyme exists as a monomer in solution
monomer
-
1 * 42000, SDS-PAGE
oligomer
-
x * 45000, alpha + x * 39000, beta, SDS-PAGE, probably alpha2beta2
monomer
Cyanidioschyzon merolae CMA035C
-
the enzyme exists as a monomer in solution
-
additional information
-
SDS-PAGE: 95000 MW and 31400 MW polypeptides are polypeptide components of the 127000 MW enzyme system
additional information
-
95 kDa subunit can be transformed into an active 60 kDa form by trypsin proteolysis
additional information
-
native enzyme forms a pentamer, recombinant enzyme from vaccinia virus forms a monomer
additional information
-
subunit structure of capping enzyme
additional information
-
42000 kDa fragment harbors the autoguanylylation activity
additional information
Q5UQX1
domain structure of capping enzymes, structure-function relationship, detailed overview
additional information
-
42000 kDa fragment harbors the autoguanylylation activity; native enzyme forms a pentamer, recombinant enzyme from vaccinia virus forms a monomer
-
additional information
-
SDS-PAGE: 95000 MW and 31400 MW polypeptides are polypeptide components of the 127000 MW enzyme system
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
catalytically active native MimiCE-(1-237) protein by vapor diffusion against a precipitant solution containing PEG4000 plus citrate and acetate buffers, X-ray diffraction structure determination and analysis at 1.65-2.9 A resolution
Q5UQX1
structure of residues 229-567, comprising the minimum enzymatically active human guanylyltransferase domain, to 3.0 A
-
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
-
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
Q84424
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
7
-
the amount of G(5')ppp(5')RNA formed at pH 5.5 is 50% of the amount formed at pH 7
additional information
-
bluetongue virus serotype 10
-
enzyme-GMP complex is resistant to alkali, but is cleaved at acidic conditions with HCl or NH2OH
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
5 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
can be frozen and thawed several times without apparent loss of activity
-
stable after a few cycles of freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, stable for more than 6 months
-
-70C, stable for at least 9 months
-
-20C, 10 mM Tris-HCl buffer, pH 8, 10 mM 2-mercaptoethanol, 50% glycerol, 0.1 mg/ml gelatin, enzyme concentration: 0.1 mg/ml, stable
-
-80C, reaction intermediate enzyme-GMP, purified, stable for at least several weeks
-
-80C, stable for at least 6 months
-
-20C, stable for more than 6 months, considerably longer at -70C
-
0C, 48 h, 90% loss of activity, 59000 MW protein which lacks 7-methyltransferase activity
-
4C or -20C, purified enzyme, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant LEF-4 subunit from overexpressing Spodoptera frugiperda cells
-
recombinant from Spodoptera frugiperda cells after infection with baculovirus, to homogeneity
bluetongue virus serotype 10
-
recombinant protein
-
recombinant His-tagged wild-type and mutant K177A protein from Bacillus megaterium
-
recombinant from vaccinia virus grown in HeLa cells
-
recombinant wild-type and mutant K226A from Trichoplusia ni or Spodoptera frugiperda SF21 cells via baculovirus infection
-
recombinant His-tagged full length enzyme as well as the recombinant His-tagged N-terminal and C-terminal domains from Escherichia coli BL21(DE3)
O55236
recombinant truncated mutant, residues 438-597, His-tagged
O55236
recombinant His6-tagged A103R protein from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
231fold; contains little or no RNA 5'-triphosphatase or methyltransferase activity
-
800fold; partial; physically associated with mRNA 5'-triphosphatase activity
-
large scale, to homogeneity, enzyme has mRNA guanylyltransferase activity
-
physically associated with mRNA 5'-triphosphatase activity
-
physically associated with mRNA 5'-triphosphatase activity; to homogeneity
-
nickel-agarose chromatography
-
1000fold, recombinant from Escherichia coli
-
copurifies with S-adenosylmethionine mRNA (guanine-7)-methyltransferase
-
mutant enzyme C-terminally truncated to residues 1-545
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
overexpression of LEF-4 subunit in Spodoptera frugiperda cells by recombinant virus infection under control of polyhedrin promotor
-
RNA genome sequence determination and analysis, expression of lambdaC in Spodoptera frugiperda cells via baculovirus infection
-
expression in Saccharomyces cerevisiae
-
expression in Spodoptera frugiperda cells via infection with baculovirus
bluetongue virus serotype 10
-
DNA and amino acid sequence determination and analysis
-
expression in Escherichia coli
-
expression of wild-type and mutant K177A in Bacillus megaterium as His-tagged proteins
-
expression in HeLa cells via vaccinia virus strain WR into whose thymidine kinase gene the reovirus lambda2 genome segment has been inserted, possesses neither nucleoside nor RNA 5'-triphosphatase activity nor methyltransferase activity
-
gene L2, expression of wild-type and mutant K226A protein lambda2 in Trichoplusia ni or Spodoptera frugiperda SF21 cells via baculovirus infection
-
DNA and amino acid sequence determination and analysis, expression of truncation mutant in Escherichia coli BL21(DE3) and wild-type and mutant K294A enzyme in Saccharomyces haploid deficient mutant strain, functional complementation of the latter by wild-type enzyme; in vitro translation of wild-type and mutant enzyme
O55236
expression of His-tagged full length enzyme, residues 211-597, comprising the catalytical domain, and residues 1-210 in Escherichia coli BL21(DE3); expression of wild-type full length enzyme and catalytic domain in deficient Saccharomyces cerevisiae strain YBS2 as His-tagged protein, functional complementation by both of them; mRNA capping enzyme, DNA sequence determination and analysis
O55236
gene A103R, expression of His6-tagged A103R protein in Escherichia coli strain BL21(DE3)
-
expression of wild-type from plasmid in deficient mutant ceg1-25
-
gene CEG1 from genomic library, expression of catalytically active alpha-subunit in Escherichia coli, chromosome mapping
-
gene CEG1, guanylylpeptide, DNA and amino acid sequence determination
-
expressed in Escherichia coli BL21(ROS2) cells
-
expession in Escherichia coli
-
expression in Escherichia coli
-
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
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D468A
Q5UQX1
site-directed mutagenesis, inactive mutant
K292A
Q5UQX1
site-directed mutagenesis, inactive mutant
K496A
Q5UQX1
site-directed mutagenesis, inactive mutant
K498A
Q5UQX1
site-directed mutagenesis, inactive mutant
H68A
-
mutation enhances GTP methylation reaction but disables the following transguanylation reaction
D532A
-
inactive
E234A
-
mutation does not inhibit the formation of the phosphoamide intermediate
K458A
-
inactive
K460A
-
inactive
R528A
-
poor activity
R530A
-
inactive
K177A
-
site-directed mutagenesis, no activity
K171A
-
site-directed mutagenesis, 0.22% of wild-type autoguanylylation activity
K190A
-
site-directed mutagenesis, autoguanylylation inactive
K197A
-
site-directed mutagenesis, 7.5% of wild-type autoguanylylation activity
K226A
-
site-directed mutagenesis, unaltered properties
K44A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
K89A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
K94A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
K171A
-
site-directed mutagenesis, 0.22% of wild-type autoguanylylation activity
-
K190A
-
site-directed mutagenesis, autoguanylylation inactive
-
K44A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
-
K89A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
-
K94A
-
site-directed mutagenesis, approximately wild-type autoguanylylation activity levels
-
K294A
O55236
site-directed mutagenesis, no remaining guanylylation activity, no complementation of a deficient Saccharomyces mutant, RNA 5'-triphosphatase activity is retained
H68C
-
mutation results in a change in the nature nature of the bond linking the enzyme and m7GMP, suggesting that residue H68 covalently binds to m7GMP in the intermediate
additional information
-
residues Y126, F144, F161, Y192, Y203, Y213, and W222, are critical for GTP methylation and S-adenosylmethionine binding during the GTP methylation reaction
K533A
-
inactive
additional information
-
residues 229567 comprise the minimum enzymatically active human guanylyltransferase domain
K294A
O55236
inactive, no functional complementation of the deficient Saccharomyces cerevisiae mutant
additional information
O55236
construction of N-terminally truncated mutant consisting of residues 438-597, N-terminal truncation eliminates the RNA 5'-triphosphatase activity
additional information
-
CEG1 gene products with substitutions at Lys70 are unable to perform the reaction and support the viability in vivo
additional information
-
expression of recombinant Candida albicans RNA 5'-triphosphatase GST-fusion protein in yeast RNA 5'-triphosphatase-deficient mutant cells binds to the guanylyltransferase of Saccharomyces cerevisiae and complements the growth defect of the mutant, while the human enzyme does not
additional information
-
RNA 5'-triphosphatase, CET1 or CES5, expressed from high copy number plasmid in Saccharomyces cerevisiae, can compensate the growth defect caused by mutation ceg1-25 of the RNA guanylyltransferase
additional information
-
mutant consisting of the D1R domain, residues 1-545
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
valuable in a variety of analytical studies of RNA
biotechnology
-
enzyme can be used as a tool for specific 5'-end-labeling of mRNA