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Information on EC 2.1.1.56 - mRNA (guanine-N7)-methyltransferase
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2.1.1.56 mRNA (guanine-N7)-methyltransferaseIUBMB Comments
The terminal N7-methylguanosine facilitates gene expression in eukaryotic cells and is recognized by cap-binding proteins.
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Word Map
- 2.1.1.56
- dengue
- viruses
- influenza
- flavivirus
- pandemic
-
sars-cov
- coronaviruses
- encephalitis
- mtases
- covid-19
- exoribonuclease
-
guanylyltransferase
-
proofreading
-
replicase
-
anti-ns1
- rig-i
-
denv-1
-
mosquito-borne
- sinefungin
-
ns1-specific
-
chikv
- bluetongue
-
anti-denv
- coronaviridae
-
arthropod-borne
- gpppg
-
anti-dengue
- remdesivir
- analysis
- synthesis
- drug development
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
(guanine-N7)-methyltransferase, Abd1, alphavirus capping enzyme, cap methyltransferase, cap N7-MTase, cap N7MTase, cap-methyltransferase, DENV methyltransferase, DENV-4 NS5, Ecm1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(guanine-N7)-methyltransferase
cap methyltransferase
cap N7-MTase
cap-methyltransferase
guanine-7-methyltransferase
-
-
-
-
guanine-N7 methyltransferase
messenger ribonucleate guanine 7-methyltransferase
-
-
-
-
messenger RNA guanine 7-methyltransferase
-
-
-
-
methyltransferase, messenger ribonucleate guanine 7-
-
-
-
-
mRNA cap (guanine N-7) methyltransferase
mRNA cap (guanine-N7) methyltransferase
mRNA cap methyltransferase
N7 methyltransferase
N7 MTase
N7-MTase
NS5
-
the nonstrucutural protein NS5 has dual functions as both an N7 methyltransferase and a nucleoside 2'-O methyltransferase
NS5MTase
-
the protein contains mRNA cap (guanine N-7) methyltransferase and (nucleoside-2'O)-methyltransferase activities
nsp14
RNA N7-MTase
RNMT
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
subunit interaction in vitro and in vivo is a necessary condition for full enzyme activity
-
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-N7-)methyltransferase form the mRNA capping enzyme complex consiting of a small and a large subunit
-
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-N7-)methyltransferase form the mRNA capping enzyme complex consiting of a small and a large subunit
-
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-N7-)methyltransferase form the mRNA capping enzyme complex consiting of a small and a large subunit
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
substrate binding sites
-
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
active site is located at His682 and Tyr683
-
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
R may be guanosine or adenosine
-
-
-
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
lipid-binding site, membrane binding activity of wild-type and diverse mutants
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S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
in-line mechanism of methyl transfer without direct contact between the enzyme and the N7 atom of guanine, which is the attacking nucleophile, the methyl carbon of S-adenosyl-L-methionine, or the sulfur of S-adenosyl-L-methionine/S-adenosyl-L-homocysteine, enzyme-ligand structures, active site structure
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:mRNA (guanine-N7)-methyltransferase
The terminal N7-methylguanosine facilitates gene expression in eukaryotic cells and is recognized by cap-binding proteins.
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CAS REGISTRY NUMBER
COMMENTARY
56941-25-4
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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
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-methionine + G(5')pppA
S-adenosyl-L-homocysteine + m7G(5')pppA
-
-
-
?
S-adenosyl-L-methionine + G(5')pppG
S-adenosyl-L-homocysteine + m7G(5')pppG
and dGTP, best substrates
-
-
?
S-adenosyl-L-methionine + GDP
S-adenosyl-L-homocysteine + m7GDP
-
-
-
?
S-adenosyl-L-methionine + Gppp-RNA
S-adenosyl-L-homocysteine + m7Gppp-RNA
-
-
-
-
?
S-adenosyl-L-methionine + GpppA-RNA
S-adenosyl-L-homocysteine + m7GpppA-RNA
-
-
-
-
?
S-adenosyl-L-methionine + GpppAC3
S-adenosyl-L-homocysteine + m7GpppAC3
-
is efficiently methylated at the guanine-N7 position
-
-
?
S-adenosyl-L-methionine + m7G(5')pppG
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
-
-
-
?
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
-
-
?
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
the enzyme methylates the guanosine cap on the N-7 position to create the cap structure, m7G(5)ppp(5)X
-
-
?
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
-
-
-
?
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
-
-
-
?
S-adenosyl-L-methionine + dGTP
S-adenosyl-L-homocysteine + m7dGTP
-
-
-
?
S-adenosyl-L-methionine + dGTP
S-adenosyl-L-homocysteine + m7dGTP
and G(5')pppG, best substrates
-
-
?
S-adenosyl-L-methionine + G(5')pppN
S-adenosyl-L-homocysteine + m7G(5')pppG
-
N: G
-
?
S-adenosyl-L-methionine + G(5')pppN
S-adenosyl-L-homocysteine + m7G(5')pppG
-
unmethylated cap analogue, serves as in vitro substrate
-
?
S-adenosyl-L-methionine + G(5')pppN
S-adenosyl-L-homocysteine + m7G(5')pppG
-
N: G
-
?
S-adenosyl-L-methionine + G(5')pppN
S-adenosyl-L-homocysteine + m7G(5')pppG
-
N: G
-
-
?
S-adenosyl-L-methionine + G(5')pppN
S-adenosyl-L-homocysteine + m7G(5')pppG
-
N: A
-
-
?
S-adenosyl-L-methionine + G(5')pppN
S-adenosyl-L-homocysteine + m7G(5')pppG
-
TbCmt1
-
-
?
S-adenosyl-L-methionine + G(5')pppN
S-adenosyl-L-homocysteine + m7G(5')pppG
-
N: A
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
essential and defining step in the eukaryotic mRNA synthesis
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
enzyme contains the conserved S-adenosyl-L-methionine-binding motif VLDLGXGXG, structural features for cap guanine specificity
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
mRNA, synthetic polyribonucleotides terminating in a dinucleoside triphosphate
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
specific for mRNAs with 5'-terminal sequence G(5')pppA- and G(5')pppG-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, methyl acceptors are unmethylated vaccinia virus mRNAs
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
active also on E. coli tRNA
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
free G(5')pppG is utilized, G(5')ppG is a poor substrate, while GTP, GDP, and G(5')ppppG are no substrates
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
essential for cell viability
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
unmethylated mRNA of reovirus and poly A(+) RNA
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
associated with mRNA-guanylyltransferase
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
methylates also undermethylated poly(A)-rich mRNA
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
methylates also undermethylated poly(A)-rich mRNA
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
in infected BHK cells
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
acceptor substrate specificity, overview
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
transfers methyl group from S-adenosyl-L-methionine specifically to position 7 of terminal guanosine
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
transfers methyl group from S-adenosyl-L-methionine specifically to position 7 of terminal guanosine
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
utilizes GMP, GDP, guanosine, ITP as substrates
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
mRNA, synthetic polyribonucleotides terminating in a dinucleoside triphosphate
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
specific for mRNAs with 5'-terminal sequence G(5')pppA- and G(5')pppG-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
specific for mRNAs with 5'-terminal sequence G(5')pppA- and G(5')pppG-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, methyl acceptors are unmethylated vaccinia virus mRNAs
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, methyl acceptors are unmethylated vaccinia virus mRNAs
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, methyl acceptors are unmethylated vaccinia virus mRNAs
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
the presence of the small one is required for methylase activity, the large subunit bears functional domains for binding of the small subunit and for methylase activity
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
guanylyltransferase and RNA-triphosphatase are located on the large subunit
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
one of a series of three reactions in capping of vaccinia virus mRNA catalyzed by one enzyme, which is a heterodimer: no methylase activity with one of the subunits alone
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, involved in synthesis of methylated capped structure at 5'-terminal of viral mRNA
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
transfers methyl group from S-adenosyl-L-methionine specifically to position 7 of terminal guanosine
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
acceptor substrate specificity, overview
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
utilizes GMP, GDP, guanosine, ITP as substrates
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
mRNA, synthetic polyribonucleotides terminating in a dinucleoside triphosphate
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
specific for mRNAs with 5'-terminal sequence G(5')pppA- and G(5')pppG-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, methyl acceptors are unmethylated vaccinia virus mRNAs
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, involved in synthesis of methylated capped structure at 5'-terminal of viral mRNA
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, methyl acceptors are unmethylated vaccinia virus mRNAs
R may be guanosine or adenosine, mRNA containing an N7-methylguanine cap
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
?
S-adenosyl-L-methionine + GpppA
S-adenosyl-L-homocysteine + m7GpppA
-
-
-
?
S-adenosyl-L-methionine + GpppA
S-adenosyl-L-homocysteine + m7GpppA
-
-
-
-
?
S-adenosyl-L-methionine + GpppA
S-adenosyl-L-homocysteine + m7GpppA
-
-
-
-
?
S-adenosyl-L-methionine + GpppA
S-adenosyl-L-homocysteine + m7GpppA
-
TbCmt1
-
-
?
S-adenosyl-L-methionine + GpppAC4
S-adenosyl-L-homocysteine + 7mGpppAC4
-
-
-
-
?
S-adenosyl-L-methionine + GpppAC4
S-adenosyl-L-homocysteine + 7mGpppAC4
-
-
-
-
?
S-adenosyl-L-methionine + GpppG
S-adenosyl-L-homocysteine + m7GpppG
-
TbCmt1
-
-
?
S-adenosyl-L-methionine + GTP
S-adenosyl-L-homocysteine + m7GTP
-
-
-
?
S-adenosyl-L-methionine + GTP
S-adenosyl-L-homocysteine + m7GTP
-
-
-
?
S-adenosyl-L-methionine + GTP
S-adenosyl-L-homocysteine + m7GTP
-
-
-
?
S-adenosyl-L-methionine + GTP
S-adenosyl-L-homocysteine + m7GTP
-
viral, not host enzyme
-
?
S-adenosyl-L-methionine + GTP
S-adenosyl-L-homocysteine + m7GTP
-
-
-
?
S-adenosyl-L-methionine + GTP
S-adenosyl-L-homocysteine + m7GTP
-
-
-
-
?
additional information
?
-
-
enzyme sequentially methylates the guanine N-7 and ribose 2'-O positions of viral RNA cap. The order of two methylations is determined by the preference of 2'-O methylation for substrate m7GpppA-RNA to GpppA-RNA, and the 2'-O methylation is not absolutely dependent on the prior N-7 methylation
-
-
?
additional information
?
-
does not methylate ATP, CTP, UTP, ITP, or m7GTP
-
-
?
additional information
?
-
-
does not methylate ATP, CTP, UTP, ITP, or m7GTP
-
-
?
additional information
?
-
-
no substrates are poly-(A) terminating in a single phosphate or a diphosphate
-
-
?
additional information
?
-
-
the enzyme is responsible for guanine-N7 methylation of recapped mRNAs
-
-
-
additional information
?
-
no substrates: ATP, CTP, UTP, dATP, dCTP, dUTP or cap analog m7GpppA
-
-
?
additional information
?
-
-
no substrates: ATP, CTP, UTP, dATP, dCTP, dUTP or cap analog m7GpppA
-
-
?
additional information
?
-
-
no activity with 7mGpppA
-
-
-
additional information
?
-
-
the protein reveals cap-independent methyltransferase activities targeting internal adenosine residues. Besides this, the enzyme domain also methylates the N7 position of the cap guanosine. The enzyme preferentially methylates adenosine residues and is not active on poly G, C and U RNAs
-
-
-
additional information
?
-
-
ATP, XTP, CTP, UTP, and guanosine containing compounds with phospho groups in either position 2' or 3' or in 3'-5'phosphodiester linkage
-
-
?
additional information
?
-
-
isolated methyltransferase domain shows a lower but kinetically equivalent activity than the complete enzyme, which is highly enhanced by association with the D12 subunit
-
-
?
additional information
?
-
-
isolated methyltransferase domain shows a lower but kinetically equivalent activity than the complete enzyme, which is highly enhanced by association with the D12 subunit
-
-
?
additional information
?
-
-
no substrates are poly-(A) terminating in a single phosphate or a diphosphate
-
-
?
additional information
?
-
-
no methylation of internal or conventional 5'-terminal guanosine residues
-
-
?
additional information
?
-
-
ATP, XTP, CTP, UTP, and guanosine containing compounds with phospho groups in either position 2' or 3' or in 3'-5'phosphodiester linkage
-
-
?
additional information
?
-
-
no substrates are poly-(A) terminating in a single phosphate or a diphosphate
-
-
?
additional information
?
-
methylation of the cap structure is also implicated in polyadenylation-mediated translational activation during Xenopus oocyte maturation
-
-
?
additional information
?
-
methylation of the cap structure is also implicated in polyadenylation-mediated translational activation during Xenopus oocyte maturation
-
-
?
additional information
?
-
methylation of the cap structure is also implicated in polyadenylation-mediated translational activation during Xenopus oocyte maturation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
-
-
-
?
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
-
-
?
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
the enzyme methylates the guanosine cap on the N-7 position to create the cap structure, m7G(5)ppp(5)X
-
-
?
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
-
-
-
?
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
essential and defining step in the eukaryotic mRNA synthesis
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
essential for cell viability
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
associated with mRNA-guanylyltransferase
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
in infected BHK cells
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
the presence of the small one is required for methylase activity, the large subunit bears functional domains for binding of the small subunit and for methylase activity
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
guanylyltransferase and RNA-triphosphatase are located on the large subunit
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
one of a series of three reactions in capping of vaccinia virus mRNA catalyzed by one enzyme, which is a heterodimer: no methylase activity with one of the subunits alone
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, involved in synthesis of methylated capped structure at 5'-terminal of viral mRNA
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
-
-
-
?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
-
R may be guanosine or adenosine, involved in synthesis of methylated capped structure at 5'-terminal of viral mRNA
-
-
?
additional information
?
-
-
the enzyme is responsible for guanine-N7 methylation of recapped mRNAs
-
-
-
additional information
?
-
methylation of the cap structure is also implicated in polyadenylation-mediated translational activation during Xenopus oocyte maturation
-
-
?
additional information
?
-
methylation of the cap structure is also implicated in polyadenylation-mediated translational activation during Xenopus oocyte maturation
-
-
?
additional information
?
-
methylation of the cap structure is also implicated in polyadenylation-mediated translational activation during Xenopus oocyte maturation
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KCl
Mg2+
Mn2+
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R,6S)-2,6-dimethyl-4-[2-methyl-3-[4-(2-methylbutan-2-yl)phenyl]propyl]morpholine
-
-
2,3,7,8-tetrahydroxy[1]benzopyrano[5,4,3-cde][1]benzopyran-5,10-dione
-
-
3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate
-
i.e. CHAPS, strong inhibition
amino acid modified structure analogue of adenosyl-L-homocysteine
-
i.e. A9145C, strong
-
bis[6-(dimethylamino)-2-[(E)-2-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)ethenyl]-1-methylquinolin-1-ium] 4-[(3-carboxy-2-oxidonaphthalen-1-yl)methyl]-3-hydroxynaphthalene-2-carboxylate
N-(2-[[(4-methoxyphenyl)methyl](pyrimidin-2-yl)amino]ethyl)-N,N-dimethylhexadecan-1-aminium
N-tetradecyl-N,N-dimethyl-3-ammonio-1-propane sulfonate
-
i.e. zwittergent 3-14, strong inhibition
Triton X-100
-
inactivation, reversible by addition of lipids: cardiolipin, phosphatidylglycerol, and especially phosphatidylserine
1-(4-tert-butylphenyl)-N-methyl-N-[(naphthalen-1-yl)methyl]methanamine
-
-
1-(diphenylmethyl)-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
-
-
1-[(4-chlorophenyl)(phenyl)methyl]-4-[(3-methylphenyl)methyl]piperazine
-
-
1-[bis(4-fluorophenyl)methyl]-4-[(2,3,4-trimethoxyphenyl)methyl]piperazine
-
-
1-[bis(4-fluorophenyl)methyl]-4-[(2Z)-3-phenylprop-2-en-1-yl]piperazine
-
-
3,8-diamino-5-[3-[diethyl(methyl)azaniumyl]propyl]-6-phenylphenanthridin-5-ium
-
-
3,8-diamino-5-[3-[diethyl(methyl)azaniumyl]propyl]-6-phenylphenanthridin-5-ium
-
-
bis[6-(dimethylamino)-2-[(E)-2-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)ethenyl]-1-methylquinolin-1-ium] 4-[(3-carboxy-2-oxidonaphthalen-1-yl)methyl]-3-hydroxynaphthalene-2-carboxylate
-
-
bis[6-(dimethylamino)-2-[(E)-2-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)ethenyl]-1-methylquinolin-1-ium] 4-[(3-carboxy-2-oxidonaphthalen-1-yl)methyl]-3-hydroxynaphthalene-2-carboxylate
-
-
N-(2-[[(4-methoxyphenyl)methyl](pyrimidin-2-yl)amino]ethyl)-N,N-dimethylhexadecan-1-aminium
-
-
N-(2-[[(4-methoxyphenyl)methyl](pyrimidin-2-yl)amino]ethyl)-N,N-dimethylhexadecan-1-aminium
-
-
Oligoadenylic acid mono- and triphosphates
-
2'-5'-linked, with varying numbers of phosphate groups, methylated in the 3'-terminal hydroxy group or all three 3'-hydroxy groups, different types of inhibition of viral and L-cell enzyme
-
Oligoadenylic acid mono- and triphosphates
-
2'-5'-linked, with varying numbers of phosphate groups, methylated in the 3'-terminal hydroxy group or all three 3'-hydroxy groups, different types of inhibition of viral and L-cell enzyme
-
S-adenosyl-L-homocysteine
inhibits methylation of GTP in the presence of 0.005 mM S-adenosyl-L-methionine
S-adenosyl-L-homocysteine
-
inhibits in a concentration-dependent fashion in the presence of 0.025 mM [3H-CH3]S-adenosyl-L-methionine
sinefungin
-
extremely potent inhibitor, binds 900fold more avidly than S-adenosylhomocysteine or S-adenosylmethionine, sensitivity to growth inhibition is diminished when Abd1 is overexpressed
sinefungin
IC50 value 0.00169 microM in yeast cell-based assay
sinefungin
-
98.2% inhibition at 0.05 mM
additional information
-
no inhibition by S-uridinyl-L-homocysteine, S-cytidinyl-L-homocysteine; S-guanosyl-L-homocysteine
-
additional information
-
detergents prevent the association of S-adenosyl-L-methionine with the enzyme
-
additional information
-
nilutamide and PPDNS do not display efficient inhibition at 0.025 and 0.125 mM
-
additional information
-
inhibition by a natural low-molecular-weight inhibitor in the crude extract, removed during purification
-
additional information
-
no inhibition by S-uridinyl-L-homocysteine, S-cytidinyl-L-homocysteine
-
additional information
-
nilutamide and PPDNS do not display efficient inhibition at 0.025 and 0.125 mM
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
importin-alpha
-
enhances specific binding of the enzyme to RNA, enhances RNA modification activity in vivo and in vitro
-
RNMT-activating miniprotein
RNMT-activating miniprotein stabilizes the enzyme and enhances the active site conformations promoting the substrates binding
-
RNMT-activating miniprotein
-
the presence of RNMT-activating miniprotein is required for cytoplasmic cap methyltransferase activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.023
G(5')pppR-RNA
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.031
G(5')pppR-RNA
-
mutant enzyme K607A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.05
G(5')pppR-RNA
-
mutant enzyme F679L, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.074
G(5')pppR-RNA
-
mutant enzyme N570A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.143
G(5')pppR-RNA
-
mutant enzyme F679N, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.176
G(5')pppR-RNA
-
mutant enzyme F679I, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.183
G(5')pppR-RNA
-
mutant enzyme R632Q, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.2
G(5')pppR-RNA
-
mutant enzyme K607Q, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.218
G(5')pppR-RNA
-
mutant enzyme E763A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.255
G(5')pppR-RNA
-
mutant enzyme F679H, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.293
G(5')pppR-RNA
-
mutant enzyme F679V, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.314
G(5')pppR-RNA
-
mutant enzyme K607R, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.446
G(5')pppR-RNA
-
mutant enzyme N570D, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
1.8
G(5')pppR-RNA
-
pH 7.5, 20°C, Michaelis constants for S-adenosyl-methionine (AdoMet) in both reactions are about 10fold lower than for their respective RNA substrates, suggesting that the rate-limiting steps in methylase reactions are associated with RNA templates
0.003
S-adenosyl-L-methionine
-
intact mRNA capping enzyme and isolated methyltransferase domain
0.0075
S-adenosyl-L-methionine
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.008
S-adenosyl-L-methionine
-
mutant enzyme K607A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.0095
S-adenosyl-L-methionine
-
mutant enzyme N570A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.18
S-adenosyl-L-methionine
-
pH 7.5, 20°C, Michaelis constants for S-adenosyl-methionine (AdoMet) in both reactions are about 10fold lower than for their respective RNA substrates, suggesting that the rate-limiting steps in methylase reactions are associated with RNA templates
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0018
G(5')pppR-RNA
-
mutant enzyme K607R, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.0022
G(5')pppR-RNA
-
mutant enzyme E763A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.003
G(5')pppR-RNA
-
mutant enzyme F679H, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.003
G(5')pppR-RNA
-
mutant enzyme N570D, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.0035
G(5')pppR-RNA
-
mutant enzyme F679N, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.004
G(5')pppR-RNA
-
mutant enzyme F679I, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.004
G(5')pppR-RNA
-
mutant enzyme F679V, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.0057
G(5')pppR-RNA
-
mutant enzyme N570A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.0073
G(5')pppR-RNA
-
mutant enzyme R632Q, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.0095
G(5')pppR-RNA
-
mutant enzyme F679L, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.018
G(5')pppR-RNA
-
mutant enzyme K607Q, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.02
G(5')pppR-RNA
-
mutant enzyme K607A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.022
G(5')pppR-RNA
-
mutant enzyme E763A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.022
G(5')pppR-RNA
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.007
S-adenosyl-L-methionine
-
mutant enzyme N570A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.016
S-adenosyl-L-methionine
-
mutant enzyme K607A, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
0.022
S-adenosyl-L-methionine
-
wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 5 mM dithiothreitol, at 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00000018 - 0.00000134
amino acid modified structure analogue of adenosyl-L-homocysteine
-
0.00000018
amino acid modified structure analogue of adenosyl-L-homocysteine
-
-
-
0.00000134
amino acid modified structure analogue of adenosyl-L-homocysteine
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.1022
(2-[4-[(4-chlorophenyl)(phenyl)methyl]piperazin-1-yl]ethoxy)acetic acid
Homo sapiens
-
at pH 8.0 and 30°C
0.0184
(2R,6S)-2,6-dimethyl-4-[2-methyl-3-[4-(2-methylbutan-2-yl)phenyl]propyl]morpholine
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.159
1-(diphenylmethyl)-4-methylpiperazine hydrochloride (1:1)
Homo sapiens
-
at pH 8.0 and 30°C
0.2268
1-[(4-chlorophenyl)(phenyl)methyl]-4-methylpiperazine
Homo sapiens
-
at pH 8.0 and 30°C
0.0135 - 0.0137
1-[bis(4-fluorophenyl)methyl]-4-[(2,3,4-trimethoxyphenyl)methyl]piperazine
0.000019
2,3,7,8-tetrahydroxy[1]benzopyrano[5,4,3-cde][1]benzopyran-5,10-dione
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.03652
2-(2-[4-[(4-chlorophenyl)(phenyl)methyl]piperazin-1-yl]ethoxy)ethan-1-ol
Homo sapiens
-
at pH 8.0 and 30°C
0.0055 - 0.031
3,8-diamino-5-[3-[diethyl(methyl)azaniumyl]propyl]-6-phenylphenanthridin-5-ium
0.0045 - 0.0051
bis[6-(dimethylamino)-2-[(E)-2-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)ethenyl]-1-methylquinolin-1-ium] 4-[(3-carboxy-2-oxidonaphthalen-1-yl)methyl]-3-hydroxynaphthalene-2-carboxylate
0.001 - 0.0015
N-(2-[[(4-methoxyphenyl)methyl](pyrimidin-2-yl)amino]ethyl)-N,N-dimethylhexadecan-1-aminium
0.002
1,8-dihydroxyanthracen-9(10H)-one
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.00128
1-(4-tert-butylphenyl)-N-methyl-N-[(naphthalen-1-yl)methyl]methanamine
Homo sapiens
-
at pH 8.0 and 30°C
0.011
1-(4-tert-butylphenyl)-N-methyl-N-[(naphthalen-1-yl)methyl]methanamine
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0091
1-(diphenylmethyl)-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0168
1-(diphenylmethyl)-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
Homo sapiens
-
at pH 8.0 and 30°C
0.0062
1-[(4-chlorophenyl)(phenyl)methyl]-4-[(3-methylphenyl)methyl]piperazine
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0088
1-[(4-chlorophenyl)(phenyl)methyl]-4-[(3-methylphenyl)methyl]piperazine
Homo sapiens
-
at pH 8.0 and 30°C
0.0135
1-[bis(4-fluorophenyl)methyl]-4-[(2,3,4-trimethoxyphenyl)methyl]piperazine
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0137
1-[bis(4-fluorophenyl)methyl]-4-[(2,3,4-trimethoxyphenyl)methyl]piperazine
Homo sapiens
-
at pH 8.0 and 30°C
0.0073
1-[bis(4-fluorophenyl)methyl]-4-[(2Z)-3-phenylprop-2-en-1-yl]piperazine
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0143
1-[bis(4-fluorophenyl)methyl]-4-[(2Z)-3-phenylprop-2-en-1-yl]piperazine
Homo sapiens
-
at pH 8.0 and 30°C
0.00074
3,3',4',5,5',7-hexahaxdroxyflavone
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0013
3,3',4',5,7-pentahydroxyflavone
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0237
3,4',5,7-tetrahydroxyflavone
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0055
3,8-diamino-5-[3-[diethyl(methyl)azaniumyl]propyl]-6-phenylphenanthridin-5-ium
Homo sapiens
-
at pH 8.0 and 30°C
0.031
3,8-diamino-5-[3-[diethyl(methyl)azaniumyl]propyl]-6-phenylphenanthridin-5-ium
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0023
aurintricarboxylic acid
Dengue virus
-
in 50 mM Tris, pH 7.0, 50 mM NaCl, 2 mM dithiothreitol, at 22°C
0.0042
aurintricarboxylic acid
Wesselsbron virus
-
in 50 mM Tris, pH 7.0, 50 mM NaCl, 2 mM dithiothreitol, at 22°C
0.0045
bis[6-(dimethylamino)-2-[(E)-2-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)ethenyl]-1-methylquinolin-1-ium] 4-[(3-carboxy-2-oxidonaphthalen-1-yl)methyl]-3-hydroxynaphthalene-2-carboxylate
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0051
bis[6-(dimethylamino)-2-[(E)-2-(2,5-dimethyl-1-phenyl-1H-pyrrol-3-yl)ethenyl]-1-methylquinolin-1-ium] 4-[(3-carboxy-2-oxidonaphthalen-1-yl)methyl]-3-hydroxynaphthalene-2-carboxylate
Homo sapiens
-
at pH 8.0 and 30°C
0.001
N-(2-[[(4-methoxyphenyl)methyl](pyrimidin-2-yl)amino]ethyl)-N,N-dimethylhexadecan-1-aminium
Homo sapiens
-
at pH 8.0 and 30°C
0.0015
N-(2-[[(4-methoxyphenyl)methyl](pyrimidin-2-yl)amino]ethyl)-N,N-dimethylhexadecan-1-aminium
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.000112
sinefungin
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7.5
methyl transfer by Ecm1 declines sharply below pH 6.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
485450, 485453, 485454, 485455, 485456, 485461, 485463, 485467, 485468, 485472, 677246, 690028, 706721
-
-
brenda
mRNA (guanine-7-)methyltransferase component of the capping enzyme
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
lipid-binding site, membrane binding activity of wild-type and diverse mutants
brenda
-
70% of total activity, 1/3 of which is losely associated to ribosomes
brenda
-
nuclear localization is required for cell viability, targeting localization signal sequences are 80KKRK, 103KKRKR, and 126KRK
brenda
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
the enzyme in complex with RNMT-activating miniprotein catalyzes the formation of a N7-methylated guanosine cap structure on the 5' end of nascent RNA polymerase II transcripts. The mRNA cap protects the primary transcript from exonucleases and recruits cap binding complexes that mediate RNA processing, export and translation
physiological function
malfunction
-
mutation defective in N-7 methylation but not 2-O'-methylation is lethal for DNV replication
malfunction
-
significant loss of RNA polymerase II gene occupancy is observed on enzyme suppression. Enzyme suppression inhibits transcriptional markers including histone H2BK120 ubiquitination, H3K4 and H3K36 methylation, RNA polymerase II C-terminal domain S5 and S2 phosphorylation, and PAFc recruitment
malfunction
-
when cellular enzyme activity is experimentally reduced by 50%, the proliferation rate of nontransformed mammary epithelial cells is unchanged, whereas a subset of breast cancer cell lines exhibit reduced proliferation and increased apoptosis
physiological function
-
mRNA guanosine cap by RNA guanine-7-methyltransferase is rate-limiting for cellular cap-methyltransferase activity, and enhancing this activity promotes cyclin D1 expression and cell formation
physiological function
-
N7 cap methylation is essential for viral replication
physiological function
-
the enzyme promotes RNA polymerase II-dependent transcription independent of mRNA capping and translation
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000 - 129000
33000
-
small subunit of mRNA capping enzyme , gel filtration, SDS-PAGE
97000
-
large subunit of mRNA capping enzyme, gel filtration, SDS-PAGE
additional information
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterodimer
-
the guanine-N7 methyltransferase domain of vaccinia virus mRNA capping enzyme is a heterodimer composed of a catalytic subunit and a stimulatory subunit, X-ray crystallography
monomer
additional information
additional information
-
primary sequence, sequence comparison with other species, enzyme-ligand structures
additional information
-
isolated methyltransferase domain shows a lower but kinetically equivalent activity than the complete enzyme, which is highly enhanced by association with the D12 subunit
additional information
-
isolated methyltransferase domain shows a lower but kinetically equivalent activity than the complete enzyme, which is highly enhanced by association with the D12 subunit
additional information
-
subunit organisation of the mRNA capping enzyme complex
additional information
-
the methyl/guanylyltransferase complex on vaccinia virus dissociates into two subunits of MW 31400 and 95000 by action of SDS-PAGE
additional information
-
the methyl/guanylyltransferase complex on vaccinia virus dissociates into two subunits of MW 31400 and 95000 by action of SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
6.5 mg/ml purified native or selenomethionine-labeled, or Hg-labeled enzyme in complex with S-adenosyl-L-methionine, S-adenosyl-L-homocysteine, or the cap guanylate plus S-adenosyl-L-homocysteine, in 20 mM Tris-HCl, pH 8.0, 220 mM NaCl, vapour diffusion against a well solution of 1.2 M sodium potassium tartrate, 50 mM bis(2-hydroxyethyl)amino-tris(hydroxymethyl)methane, pH 6.0-6.2, and 20 mM DTT, X-ray diffraction structure determination and analysis at 2.0-2.7 A resolution, modeling
-
Ecm1-aza-S-adenosyl-L-methionine binary complex, by vapor diffusion, reveals that the inhibitor occupies the same site as S-adenosyl-L-methionine
Ecm1-sinefungin binary complex, by vapor diffusion, to 2.6 A resolution
structure-function relationships of the N7-MTase. The ExoN domain is closely involved in the activity of the N7-MTase. Two of the 12 critical residues essential for the N7-MTase are located at the N terminus of the core ExoN domain, reinforcing a role of the ExoN domain in the N7-MTase activity of nsp14. The other 10 critical residues are distributed throughout the N7-MTase domain but localized mainly in the S-adenosyl-L-methionine-binding pocket
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D146A
-
mutant completely loses the N-7 activity (methylation of N-7 position of guanine) and 2'-O methylation activity. Mutation defective in N-7 methylation is lethal for DNV replication
E217A
-
mutants retains 59% of wild-type N-7 (methylation of N-7 position of guanine) activity
K181A
-
mutants retains 16% of wild-type N-7 (methylation of N-7 position of guanine) activity
K61A
-
mutants retains 34% of wild-type N-7 (methylation of N-7 position of guanine) activity
D122A/S123A
-
site-directed mutagenesis, complementation of the yeast abd1DELTA mutant at 25°C and 30°C, only slightly at 37°C
D70A
D70E
D70N
D78A
D78E
D78N
D94A
D94E
D94N
E225A
F141A
F141H
grows well at 25 and 30°C but forms pinpoint colonies at 37°C
F141I
grows well at 25 and 30°C but forms pinpoint colonies at 37°C
F141L
grows as well as the wild-type ECM1 strain at all temperatures
F141V
grows well at 25 and 30°C but forms pinpoint colonies at 37°C
F214A
H144A
H144A/Y145L
defective in vivo, fails to grow at 37°C, forms microcolonies at 30°C, and grows slowly at 25°C
I95A
-
site-directed mutagenesis, complementation of the yeast abd1DELTA mutant at 25°C, 30°C, and 37°C, no effect on enzyme function
I95A/Y124A
-
site-directed mutagenesis, only slight complementation of the yeast abd1DELTA mutant at 25°C and 30°C, not at 37°C, growth defects
K267A
K54A
K54Q
K54R
K75A
K81A
K81Q
K81R
L216A
-
site-directed mutagenesis, complementation of the yeast abd1DELTA mutant at 25°C and 30°C, slightly reduced at 37°C, no effect on cell growth
N50A
-
site-directed mutagenesis, complementation of the yeast abd1DELTA mutant at 25°C and 30°C, slightly reduced at 37°C, only modest growth defects
N50A/Y284A
-
site-directed mutagenesis, no complementation of the yeast abd1DELTA mutant, mutation is lethal in vivo
N51A
N51D
P175A
grows as well as the wild-type ECM1 strain at all temperatures
R106A
R106K
R106Q
R47A
-
site-directed mutagenesis, complementation of the yeast abd1DELTA mutant at 25°C and 30°C, slightly reduced at 37°C
R47A/K75A
-
site-directed mutagenesis, no complementation of the yeast abd1DELTA mutant, mutation is lethal in vivo
R59A
R84A
Y124A
Y145A
Y145F
Y145H
grows as well as the wild-type ECM1 strain at all temperatures
Y145I
intermediate phenotype of slow growth at 25 and 30°C and microcolony formation at 37°C
Y145L
Y145S
Y212A
Y284A
-
site-directed mutagenesis, some complementation of the yeast abd1DELTA mutant at 25°C and 30°C, not at 37°C, slow growth phenotype
D330A
-
the mutation does not affect viral replication, sensitivity to mutagen, or inhibition by interferon-beta compared to the wild type
G332A
-
the mutant displays delayed replication kinetics and decreased peak titers relative to the wild type virus. In addition, replication of mutant virus is diminished following treatment of cells with interferon-beta, and mutant genomes are translated less efficiently both in vitro and during viral infection
C382Y
C414R
C416R
mutation abolishes the N7-MTase activity on GTP
D243A
D273A
97% of wild-type methylation activity
D331A
D331E
70% of wild-type methylation activity
D331Y
D352A
D90A/E92A
F73A
G333A
G416R
45% of wild-type methylation activity
H268L
I332A
K336A
K61A
97% of wild-type methylation activity
L419A
complete loss of methylation activity
L419R
15-50% of wild-type activity
N256A
97% of wild-type methylation activity
N334A
89% of wild-type methylation activity
N388A
83% of wild-type methylation activity
P335A
R310A
R84A
T428A
W86A
Y368A
Y420A
D1924A
-
the mutant shows severely reduced activity compared to the wild type enzyme
E1996A
-
the mutant shows severely reduced activity compared to the wild type enzyme
K1813A
-
the mutant shows severely reduced activity compared to the wild type enzyme
K1959A
-
the mutant shows severely reduced activity compared to the wild type enzyme
D80A
-
TbCmt1 mutant is unable to support methylation at levels of input protein sufficient to convert all the input substrate to the methylated form by wild-type TbCmt1, specific activity is less than 0.1% of the wild-type activity
E258A
-
TbCmt1 mutant is unable to support methylation at levels of input protein sufficient to convert all the input substrate to the methylated form by wild-type TbCmt1, specific activity is less than 0.1% of the wild-type activity
K83A
-
TbCmt1 mutant is unable to support methylation at levels of input protein sufficient to convert all the input substrate to the methylated form by wild-type TbCmt1, specific activity is less than 0.1% of the wild-type activity
C173A/S174A
-
modest defect, grows well at 19, 30 and 34°C, but very slowly at 37°C
D192A/S193A
-
temperature-sensitive vD12 allele, near-lethality, only grows very slowly at 19°C
D52A/L53A
-
modest defect, grows well at 30°C, but slowly at 34°C and not at 37°C
E104A/G11A
-
modest defect, grows well at 19, 30 and 34 °C, but slowly at 37°C
E275A/N276A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
F141A/R142A
F44A/L45A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
H260A/S261A
-
modest defect, grows well at 19, 30 and 34°C, but very slowly at 37°C
H682A
I47A/S48A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
K111A/R112A
-
modest defect, grows well at 19, 30 and 34°C, but very slowly at 37°C
K223A/D223A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
L16A/P17A
-
temperature-sensitive vD12 allele, forms small colonies at 19°C and fails to grow at 30°C or higher
N120A/N121A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
N126A/N127A
-
modest defect, grows well at 19, 30 and 34°C, but very slowly at 37°C
N54A/R55A
-
modest defect, grows well at 19 and 30°C, but slowly at 34 and very slowly at 37°C
P35A/S36A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
R280A-R281A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
S186A/D187A