HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 2.1.1.56 - mRNA (guanine-N7)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.56
Word Map on EC 2.1.1.56
- 2.1.1.56
-
guanylyltransferase
- mtases
- dengue
- adomet
- coronaviruses
-
sars-cov
- exoribonuclease
-
guanine-n7-methyltransferase
- gpppa
-
adohcy
-
semliki
-
proofreading
- sinefungin
- flaviviruses
- 7-methylguanosine
- m7gtp
-
m7gpppn
-
sam-binding
-
positive-sense
- analysis
-
adomet-dependent
- drug development
- synthesis
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The enzyme appears in viruses and cellular organisms
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
2.1.1.56
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
mRNA (guanine-N7)-methyltransferase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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]
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; 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]
active site is located at His682 and Tyr683; RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-N7-)methyltransferase form the mRNA capping enzyme complex consiting of a small and a large subunit; 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; RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-N7-)methyltransferase form the mRNA capping enzyme complex consiting of a small and a large subunit; 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; substrate binding sites
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:mRNA (guanine-N7)-methyltransferase
The nucleoside next to the terminal guanosine may be either guanosine or adenosine.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
56941-25-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
485450, 485453, 485454, 485455, 485456, 485461, 485463, 485467, 485468, 485472, 677246, 690028, 706721
-
-
mRNA (guanine-7-)methyltransferase component of the capping enzyme
SwissProt
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
mutation defective in N-7 methylation but not 2-O'-methylation is lethal for DNV replication
physiological function
physiological function
-
N7 cap methylation is essential for viral replication
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + 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 + 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 + 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
-
-
-
?
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
-
-
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 + 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
-
viral, not host enzyme
-
?
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
?
-
-
no substrates: ATP, CTP, UTP, dATP, dCTP, dUTP or cap analog m7GpppA
-
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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 + 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
?
-
Q9I8S2
methylation of the cap structure is also implicated in polyadenylation-mediated translational activation during Xenopus oocyte maturation
-
-
-
additional information
?
-
Q9IA92
methylation of the cap structure is also implicated in polyadenylation-mediated translational activation during Xenopus oocyte maturation
-
-
-
additional information
?
-
Q9IA93
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.
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate
-
i.e. CHAPS, strong inhibition
amino acid modified structure analogue of adenosyl-L-homocysteine
-
i.e. A9145C, strong
-
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
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
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
-
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; 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; 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; 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.
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
0.0023
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
70% of total activity, 1/3 of which is losely associated to ribosomes
-
lipid-binding site, membrane binding activity of wild-type and diverse mutants
-
nuclear localization is required for cell viability, targeting localization signal sequences are 80KKRK, 103KKRKR, and 126KRK
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
Dengue virus type 1 (strain Nauru/West Pac/1974)
Dengue virus type 1 (strain Nauru/West Pac/1974)
Dengue virus type 2 (strain Puerto Rico/PR159-S1/1969)
Dengue virus type 2 (strain Thailand/NGS-C/1944)
Vesicular stomatitis Indiana virus (strain Mudd-Summers)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
-
small subunit of mRNA capping enzyme , gel filtration, SDS-PAGE
97000
-
large subunit of mRNA capping enzyme, gel filtration, SDS-PAGE
120000 - 129000
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
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
-
the methyl/guanylyltransferase complex on vaccinia virus dissociates into two subunits of MW 31400 and 95000 by action of SDS-PAGE
additional information
-
subunit organisation of the mRNA capping enzyme complex
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
-
the methyl/guanylyltransferase complex on vaccinia virus dissociates into two subunits of MW 31400 and 95000 by action of SDS-PAGE
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
small and large subunit of the mRNA capping enzyme are not stable and active when isolated, respectively
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, several months
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA-agarose affinity chromatography
His6-Smt3-Abd1 by nickel-nitrilotriacetic acid fast flow column chromatography, Abd1 free of the tag by gel filtration, to homogeneity
-
methyltransferase domain, and small subunit of mRNA capping enzyme, recombinant from E. coli
-
recombinant Ecm1 mutant proteins, by nickel-agarose chromatography
-
recombinant from E. coli and recombinant from in vitro transcription and translation
-
recombinant N-terminally His6-tagged enzyme as Smt3-fusion protein from Escherichia coli strain BL21(DE3), removal of His-Smt3 tag by specific protease Ulp1, purification by metal affinity chromatography and gel filtration
-
small and large subunit of mRNA capping enzyme , recombinant from E. coli
-
TbCmt1 protein purified from soluble extract by nickel-agarose, followed by phosphocellulose chromatography
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 carboxyl-truncated versions of the large subunit of the mRNA capping enzyme, expression in Escherichia coli; coexpression of genes D1 and D12 from 1 plasmid; vaccinia virus genes D1 and D12 encoding the large and the small subunit of the mRNA capping enzyme, respectively, individual overexpression in Escherichia coli BL21
-
2 carboxyl-truncated versions of the large subunit of the mRNA capping enzyme, expression in Escherichia coli; vaccinia virus genes D1 and D12 encoding the large and the small subunit of the mRNA capping enzyme, respectively, individual overexpression in Escherichia coli BL21
-
as a His6-Smt3 fusion protein in Escherichia coli BL21(DE3) CodonPlus RIL using a pET-based pSmt3-TOPO vector
-
complementation of knock-down HeLa S3 cells with enzymatically active N-truncated enzyme comprising residues 120-476 and being located at the nucleus, no complementation of knock-down HeLa S3 cells with enzymatically active N-truncated enzyme comprising residues 144-476 and being loacetd mainly in the cytoplasm, truncated enzymes are expresss in fusion with GFP
-
D1 fragment, amino acids 498 to 844; expression of D1 fragment mutants in Escherichia coli; individual and coexpression of His-tagged D1 large subunit fragment, being the methyltransferase domain of the enzyme, and of D12 small subunit in Escherichia coli
-
D1 fragment, amino acids 498 to 844; individual and coexpression of His-tagged D1 large subunit fragment, being the methyltransferase domain of the enzyme, and of D12 small subunit in Escherichia coli
-
D1 fragment, amino acids 520-844; individual and coexpression of His-tagged D1 large subunit fragment, being the methyltransferase domain of the enzyme, and of D12 small subunit in Escherichia coli
-
expression in Escherichia coli, His-tagged; expression in Escherichia coli, His-tagged, amino acid sequence analysis; expression in Escherichia coli, His-tagged, amino acid sequence analysis
expression in Escherichia coli; in vitro transcription and translation in presence of liposomes, enzyme is attached to the liposomes surface
-
expression in Saccharomyces cerevisiae, His-tagged, amino acid sequence analysis
expression of 2 different variants, each with and without His-tag, in Escherichia coli, amino acid sequence analysis
-
expression of full length and 2 truncated genes in Saccharomyces cerevisiae and Escherichia coli, location of methyltransferase activity
-
expression of full length enzyme and truncated enzyme in yeast and in HeLa cells, His-tagged, as GFP-fusion protein, or cMyc-tagged
-
expression of N-terminally His6-tagged enzyme, residues 1-298, as Smt3-fusion protein in Escherichia coli strain BL21(DE3) or strain B834DE3, expression of wild-type and mutant alleles under control of a yeast promotor in a Saccharomyces cerevisiae abd1DELTA null mutant strain
-
His6-tagged proteins are expressed in Escherichia coli BL21(DE3) cells and in Saccharomyces cerevisiae strain YBS40
-
inserted into vector pET16b and transformed into Escherichia coli BL21(DE3), yeast strain YBS40 transformed with CEN TRP1 plasmids containing the wild-type and mutant alleles of ECM1
-
TbCmt1 inserted into an inducible T7 RNA polymerase-based pET vector and introduced into Escherichia coli BL21(DE3)Gold
-
the MTase domain, representing the N-terminal 272 amino acids of DENV-4 NS5 is cloned and purified
-
vaccinia virus genes D1 and D12 encoding the large and the small subunit of the mRNA capping enzyme, respectively, individual overexpression in Escherichia coli BL21
-
wild-type or mutant vD12, into the pRS413T vector, expressed in Saccharomyces cerevisiae strain YBS40
-
yeast strain YBS40 transformed with CEN TRP1 plasmids containing the wild-type and mutant alleles of ECM1, the pET16-Ecm1 plasmids introduced into Escherichia coli BL21(DE3)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
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
D78A
D78E
D78N
D94A
D94E
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
K75A
K81A
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
P175A
-
grows as well as the wild-type ECM1 strain at all temperatures
R106A
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
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
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
C382Y
C414R
D243A
D331A
D331Y
D352A
D90A/E92A
F73A
G333A
H268L
I332A
K336A
P335A
R310A
R84A
T428A
W86A
Y368A
Y420A
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
-
grows slowly at 19 and 30°C and fails to grow at 34°C or higher; temperature-sensitive vD12 allele, does not grow above 34°C
H260A/S261A
-
modest defect, grows well at 19, 30 and 34°C, but very slowly at 37°C
H682A
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
R280A-R281A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
S186A/D187A
-
modest defect, grows well at 19, 30 and 34°C, but very slowly at 37°C
Y258A-V259A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
Y683A
-
in D1 fragment, amino acids 498-844, 0.05% activity remaining, unable to crosslink the cap in presence of S-adenosyl-L-homocysteine
Y683S
-
in D1 fragment, amino acids 498-844, catalytically defective, unable to crosslink the cap in presence of S-adenosyl-L-homocysteine
E1764A
-
mutation abolishes both guanine-N-7 (G-N-7) and ribose 2'-O methylation methylation
F1691A
-
mutation abolishes both guanine-N-7 (G-N-7) and ribose 2'-O methylation. Alanine substitution results in recombinant virus that does not form plaques and significant diminished viral replication
F1691W
-
mutation does not significantly affect the size of viral plaques. Mutant replicates as wild-type VSV. Mutant exhibits 82% of wild-type guanine-N-7 (G-N-7) methylation
F1691Y
-
mutation does not significantly affect the size of viral plaques. Mutant replicates as wild-type VSV. Mutant exhibits 85% of wild-type guanine-N-7 (G-N-7) methylation
F1745A
-
mutant shows a moderate defect in guanine-N-7 (G-N-7) methylation
F1816A
-
mutant does not show a significant defect in guanine-N-7 (G-N-7) methylation
L1757A
-
mutant does not show a significant defect in guanine-N-7 (G-N-7) methylation
N1692A
-
mutant shows a moderate defect in guanine-N-7 (G-N-7) methylation
P1709A
-
mutant does not show a significant defect in guanine-N-7 (G-N-7) methylation
S1693A
-
mutant shows a moderate defect in guanine-N-7 (G-N-7) methylation
S1827A
-
mutant shows a moderate defect in guanine-N-7 (G-N-7) methylation
W1744A
-
mutant does not show a significant defect in guanine-N-7 (G-N-7) methylation
Y1650A
-
mutation abolishes both guanine-N-7 (G-N-7) and ribose 2'-O methylation. Alanine substitution results in recombinant virus that does not form plaques and significant diminished viral replication
Y1650F
-
mutation does not significantly affect the size of viral plaques. Mutant replicates as wild-type VSV. Mutant exhibits 88% of wild-type guanine-N-7 (G-N-7) methylation
Y1650W
-
mutation does not significantly affect the size of viral plaques. Mutant replicates as wild-type VSV. Mutant exhibits 90% of wild-type guanine-N-7 (G-N-7) methylation
Y1835A
-
mutant does not show a significant defect in guanine-N-7 (G-N-7) methylation
E149A
-
the mutant shows about 1% N7 MTase activity as compared to the wild type protein
E34A
-
the mutant shows about 70% N7 MTase activity as compared to the wild type protein
F133A
-
the mutant shows about 99% N7 MTase activity as compared to the wild type protein
K21A
-
the mutant shows about 95% N7 MTase activity as compared to the wild type protein
K41A
-
the mutant shows about 90% N7 MTase activity as compared to the wild type protein
K45A
-
the mutant shows about 105% N7 MTase activity as compared to the wild type protein
L16A
-
the mutant shows about 110% N7 MTase activity as compared to the wild type protein
L184A
-
the mutant shows about 85% N7 MTase activity as compared to the wild type protein
Q114A
-
the mutant shows about 97% N7 MTase activity as compared to the wild type protein
R213A
-
the mutant shows about 30% N7 MTase activity as compared to the wild type protein
R37A
-
the mutant shows about 5% N7 MTase activity as compared to the wild type protein
R44A
-
the mutant shows about 65% N7 MTase activity as compared to the wild type protein
R57A
-
the mutant shows about 10% N7 MTase activity as compared to the wild type protein
R84A
-
the mutant shows about 3% N7 MTase activity as compared to the wild type protein
V55A
-
the mutant shows about 50% N7 MTase activity as compared to the wild type protein
W87A
-
the mutant shows about 10% N7 MTase activity as compared to the wild type protein
Y220A
-
the mutant shows about 30% N7 MTase activity as compared to the wild type protein
Y254A
-
the mutant shows about 110% N7 MTase activity as compared to the wild type protein
additional information
D70A
-
lethal, suppresses methyltransferase activity to less than 3% of the wild-type level, in vivo lethality correlates with loss of catalytic activity
D70E
-
grows as well as the wild-type ECM1 strain at all temperatures
D78A
-
site-directed mutagenesis, no complementation of the yeast abd1DELTA mutant at 30°C and 37°C, but at 25°C
D78A
-
lethal, suppresses methyltransferase activity to less than 3% of the wild-type level, in vivo lethality correlates with loss of catalytic activity
D94A
-
site-directed mutagenesis, no complementation of the yeast abd1DELTA mutant, mutation is lethal in vivo
D94A
-
suppresses methyltransferase activity to less than 3% of the wild-type level, in vivo lethality correlates with loss of catalytic activity
D94E
-
grows as well as the wild-type ECM1 strain at all temperatures
F141A
-
site-directed mutagenesis, no complementation of the yeast abd1DELTA mutant, mutation is lethal in vivo
F141A
-
suppresses methyltransferase activity to less than 3% of the wild-type level, in vivo lethality correlates with loss of catalytic activity
H144A
-
no effect on yeast growth at 25 or 30°C, although it slowly grows at 37°C
K267A
-
grows as well as the wild-type ECM1 strain at all temperatures and is as active as wild-type Ecm1 in GpppA methylation in vitro
K54A
-
site-directed mutagenesis, no complementation of the yeast abd1DELTA mutant, inactive mutant in vivo
K54A
-
lethal, suppresses methyltransferase activity to less than 3% of the wild-type level, in vivo lethality correlates with loss of catalytic activity
K75A
-
site-directed mutagenesis, some complementation of the yeast abd1DELTA mutant at 25°C and 30°C, not at 37°C, temperature-sensitive phenotype
K81A
-
site-directed mutagenesis, no complementation of the yeast abd1DELTA mutant, mutation is lethal in vivo
N51A
-
site-directed mutagenesis, no complementation of the yeast abd1DELTA mutant at 25°C and 30°C, not at 37°C
R106A
-
site-directed mutagenesis, only slight complementation of the yeast abd1DELTA mutant at 25°C and 30°C, not at 37°C
R59A
-
grows as well as the wild-type ECM1 strain at all temperatures and is as active as wild-type Ecm1 in GpppA methylation in vitro
R84A
-
grows as well as the wild-type ECM1 strain at all temperatures and is as active as wild-type Ecm1 in GpppA methylation in vitro
Y124A
-
site-directed mutagenesis, complementation of the yeast abd1DELTA mutant at 25°C and 30°C, not at 37°C, temperature-sensitive phenotype
Y145F
-
grows as well as the wild-type ECM1 strain at all temperatures
Y145L
-
grows as well as the wild-type ECM1 strain at all temperatures
D243A
-
the point mutation in the ExoN domain does not significantly interfere with the N7-MTase function
D90A/E92A
-
the point mutation in the ExoN domain does not significantly interfere with the N7-MTase function
H268L
-
the point mutation in the ExoN domain does not significantly interfere with the N7-MTase function
H682A
-
in D1 fragment, amino acids 498-844, 4% activity remaining, unable to crosslink the cap in presence of S-adenosyl-L-homocysteine
additional information
-
mapping of lipid-binding site, membrane binding activity of wild-type and diverse constructed mutants
additional information
-
residues Lys-54, Asp-70, Asp-78, and Asp-94 that comprise the S-adenosyl-L-methionine-binding pocket are all essential for Ecm1 function in yeast, i.e. alanine substitutions at each of these positions are lethal, loss of function caused by the elimination of Phe-141 attests to the importance of its van der Waals interactions with the guanosine methyl acceptor seen in the Ecm1-GTP cocrystal
additional information
-
construction of knock-down HeLa cells S3, gene inactivation by small interference RNA in HeLa cells results in apoptosis
additional information
-
construction of carboxyl-truncated D1 genes, amino acid 1-666 and 1-425: 347 residues are sufficient for activity
additional information
-
exchange for alanine at single sites within the methyltransferase domain fragment of D1, loss of activity when exchanged hits His682 and Tyr683, active site
additional information
-
exchange of 8 residues for alanine in the D1 fragment, amino acids 498-844
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
-
cap methylation is a principal target of the antifungal activity of sinefungin
synthesis
combination of chemical synthesis and enzymatic methylation in order to produce large amounts of RNA oligonucleotides carrying a cap-0 or cap-1. Short RNAs are synthesized on solid support by the phosphoramidite 2'-O-pivaloyloxymethyl chemistry. The cap structure is then coupled by the addition of GDP after phosphorylation of the terminal 5'-OH and activation by imidazole. GpppN-RNAs or GpppN2'-Om-RNAs are purified before the N7-methyl group is added using the human (guanine-N7)-methyl transferase to yield 7mGpppN-RNAs (cap-0) or 7mGpppN29-Om-RNAs (cap-1)
analysis
-
cap methylation is a principal target of the antifungal activity of sinefungin
analysis
-
second Trypanosoma brucei RNA (guanine N-7) cap methyltransferase, named TbCgm1, TbCmt1 is homologous with TbCgm1, consisting of a C-terminal (guanine N-7) methyltransferase domain and an N-terminal guanylyltransferase domain, which contains signature motifs found in the nucleotidyl transferase superfamily
analysis
-
enzyme is composed of catalytic vD1 (498–844) and stimulatory vD12 subunits, yeast is a powerful system for suppressor analysis of interacting poxvirus proteins, screen of amino acids in vD1-C, at which mutations restore methyltransferase function in conjunction with defective vD12 proteins, reference to the crystal structure of the microsporidian cap methyltransferase suggests that distinct functional classes of suppressors are selected
analysis
-
yeast-based system for identifying and screening inhibitors against coronavirus N7-MTase using both 96-well and 384-well microtiter plates. Sinefungin effectively suppressed N7-MTase in the yeast system. The results validate the yeast assay system for inhibitor screening yet also demonstrate the difference between cell-based and in vitro biochemical assays. The yeast system is applied to the screening of 3000 natural product extracts
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.56)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
