Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + 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 + G(5')pppN
S-adenosyl-L-homocysteine + m7G(5')pppG
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
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
S-adenosyl-L-homocysteine + m7GpppA
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 + GpppAC4
S-adenosyl-L-homocysteine + 7mGpppAC4
S-adenosyl-L-methionine + GpppG
S-adenosyl-L-homocysteine + m7GpppG
S-adenosyl-L-methionine + GpppGAU-[RNA]
?
-
strong activity
-
-
?
S-adenosyl-L-methionine + GTP
S-adenosyl-L-homocysteine + m7GTP
S-adenosyl-L-methionine + guanylimidodiphosphate
?
-
-
-
-
?
S-adenosyl-L-methionine + guanylylimidodiphosphate
?
-
-
-
?
S-adenosyl-L-methionine + m7G(5')pppG
S-adenosyl-L-homocysteine + ?
-
-
-
?
S-adenosyl-L-methionine + mGpppGAU-[RNA]
?
-
strong activity
-
-
?
S-adenosyl-L-methionine + mGpppGmAmU-[RNA]
?
-
strong activity
-
-
?
S-adenosyl-L-methionine + mGpppGmAU-[RNA]
?
-
strong activity
-
-
?
S-adenosyl-L-methionine + pp(A)n
?
-
-
-
-
?
additional information
?
-
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 + GpppG
S-adenosyl-L-homocysteine + m7GpppG
-
-
-
-
?
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
?
-
-
GDP, GTP, G(5')ppppG
-
-
?
additional information
?
-
-
the enzyme is responsible for guanine-N7 methylation of recapped mRNAs
-
-
-
additional information
?
-
-
no activity with 7mGpppA
-
-
-
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2-[4-[(4-chlorophenyl)(phenyl)methyl]piperazin-1-yl]ethoxy)acetic acid
-
-
(2R,6S)-2,6-dimethyl-4-[2-methyl-3-[4-(2-methylbutan-2-yl)phenyl]propyl]morpholine
-
-
1,8-dihydroxyanthracen-9(10H)-one
1-(4-tert-butylphenyl)-N-methyl-N-[(naphthalen-1-yl)methyl]methanamine
1-(diphenylmethyl)-4-methylpiperazine hydrochloride (1:1)
-
-
1-(diphenylmethyl)-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
1-[(4-chlorophenyl)(phenyl)methyl]-4-methylpiperazine
-
-
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
2,3,7,8-tetrahydroxy[1]benzopyrano[5,4,3-cde][1]benzopyran-5,10-dione
-
-
2-(2-[4-[(4-chlorophenyl)(phenyl)methyl]piperazin-1-yl]ethoxy)ethan-1-ol
-
-
3,3',4',5,5',7-hexahaxdroxyflavone
3,3',4',5,7-pentahydroxyflavone
3,4',5,7-tetrahydroxyflavone
3,8-diamino-5-[3-[diethyl(methyl)azaniumyl]propyl]-6-phenylphenanthridin-5-ium
3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate
-
i.e. CHAPS, strong inhibition
5',N8-Adenosyl-alpha,beta-diaminobutyric acid
-
moderate
amino acid modified structure analogue of adenosyl-L-homocysteine
-
i.e. A9145C, strong
-
aza-S-adenosyl-L-methionine
-
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
carbocyclic aza-S-adenosyl-L-methionine
-
Cd2+
about 17 % residual activity at 5 mM
Co2+
about 20 % residual activity at 5 mM
cycloheximide
-
inhibits protein synthesis in infected BHK cells
deoxycholate
-
inactivation
Digitonin
-
strong inhibition
EDTA
12% residual activity at 5 mM
GpppG
-
inhibits binding of the enzyme to RNA
N,N-bis-(3-D-gluconamidopropyl)-deoxycholamide
-
strong inhibition
N-(2-[[(4-methoxyphenyl)methyl](pyrimidin-2-yl)amino]ethyl)-N,N-dimethylhexadecan-1-aminium
n-octyl-beta-D-gluconpyranoside
-
i.e. octylglucoside, strong inhibition
N-tetradecyl-N,N-dimethyl-3-ammonio-1-propane sulfonate
-
i.e. zwittergent 3-14, strong inhibition
Ni2+
about 25 % residual activity at 5 mM
Oligoadenylic acid mono- and triphosphates
-
S-(2-azaadenosyl)-L-homocysteine
-
moderate
S-(3-Aminoadenosyl)-L-homocysteine
-
weak
S-(3-deazaadenosyl)-L-homocysteine
S-(8-azaadenosyl)-L-homocysteine
S-(N6-Dimethyl-3-deazaadenosyl)-L-homocysteine
-
weak
S-(N6-Methyladenosyl)-L-homocysteine
S-Adenosyl-D-homocysteine
S-adenosyl-homocysteine
-
-
S-adenosyl-L-homocysteine
S-Adenosyl-L-homocysteine structural analogues
S-Adenosyl-L-homocysteine sulfone
S-adenosyl-L-homocysteine sulfoxide
S-Aristeromycinyl-L-homocysteine
S-Inosyl-L-homocysteine
-
weak
S-Tubercidinyl-L-homocysteine
Thesit
-
strong inhibition
-
Triton X-100
-
inactivation, reversible by addition of lipids: cardiolipin, phosphatidylglycerol, and especially phosphatidylserine
1,8-dihydroxyanthracen-9(10H)-one
-
-
1,8-dihydroxyanthracen-9(10H)-one
-
-
1-(4-tert-butylphenyl)-N-methyl-N-[(naphthalen-1-yl)methyl]methanamine
-
-
1-(4-tert-butylphenyl)-N-methyl-N-[(naphthalen-1-yl)methyl]methanamine
-
-
1-(diphenylmethyl)-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
-
-
1-(diphenylmethyl)-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
-
-
1-[(4-chlorophenyl)(phenyl)methyl]-4-[(3-methylphenyl)methyl]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-[(2,3,4-trimethoxyphenyl)methyl]piperazine
-
-
1-[bis(4-fluorophenyl)methyl]-4-[(2Z)-3-phenylprop-2-en-1-yl]piperazine
-
-
1-[bis(4-fluorophenyl)methyl]-4-[(2Z)-3-phenylprop-2-en-1-yl]piperazine
-
-
3,3',4',5,5',7-hexahaxdroxyflavone
-
-
3,3',4',5,5',7-hexahaxdroxyflavone
-
-
3,3',4',5,7-pentahydroxyflavone
-
-
3,3',4',5,7-pentahydroxyflavone
-
-
3,4',5,7-tetrahydroxyflavone
-
-
3,4',5,7-tetrahydroxyflavone
-
-
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
-
-
aurintricarboxylic acid
-
aurintricarboxylic acid
-
strong inhibition at 0.025 mM
aurintricarboxylic acid
-
strong inhibition at 0.025 mM
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
-
-
Ca2+
about 10 % residual activity at 5 mM
Cu2+
about 18 % residual activity at 5 mM
Mg2+
-
strong
Mn2+
-
strong
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-(3-deazaadenosyl)-L-homocysteine
-
strong
S-(3-deazaadenosyl)-L-homocysteine
-
strong
S-(3-deazaadenosyl)-L-homocysteine
-
-
S-(8-azaadenosyl)-L-homocysteine
-
moderate
S-(8-azaadenosyl)-L-homocysteine
-
weak
S-(N6-Methyladenosyl)-L-homocysteine
-
moderate
S-(N6-Methyladenosyl)-L-homocysteine
-
-
S-Adenosyl-D-homocysteine
-
moderate
S-Adenosyl-D-homocysteine
-
weak
S-Adenosyl-D-homocysteine
-
-
S-adenosyl-L-cysteine
-
moderate
S-adenosyl-L-cysteine
-
-
S-adenosyl-L-homocysteine
-
product inhibition, competitive
S-adenosyl-L-homocysteine
inhibits methylation of GTP in the presence of 0.005 mM S-adenosyl-L-methionine
S-adenosyl-L-homocysteine
-
product inhibition, competitive
S-adenosyl-L-homocysteine
-
inhibits in a concentration-dependent fashion in the presence of 0.025 mM [3H-CH3]S-adenosyl-L-methionine
S-adenosyl-L-homocysteine
-
product inhibition, competitive
S-adenosyl-L-homocysteine
-
-
S-adenosyl-L-homocysteine
-
product inhibition, competitive
S-adenosyl-L-homocysteine
-
-
S-Adenosyl-L-homocysteine structural analogues
-
-
S-Adenosyl-L-homocysteine structural analogues
-
-
S-Adenosyl-L-homocysteine sulfone
-
strong
S-Adenosyl-L-homocysteine sulfone
-
weak
S-Adenosyl-L-homocysteine sulfone
-
-
S-adenosyl-L-homocysteine sulfoxide
-
strong
S-adenosyl-L-homocysteine sulfoxide
-
weak
S-adenosyl-L-homocysteine sulfoxide
-
-
S-Aristeromycinyl-L-homocysteine
-
-
S-Aristeromycinyl-L-homocysteine
-
-
S-Tubercidinyl-L-homocysteine
-
strong
S-Tubercidinyl-L-homocysteine
-
weak
S-Tubercidinyl-L-homocysteine
-
-
sinefungin
-
sinefungin
inhibits Ecm1 with modest potency
sinefungin
-
98.2% inhibition at 0.05 mM
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
sinefungin
-
i.e. A9145, strong
Zn2+
about 30 % residual activity at 5 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
-
2'-AMP, 3'-AMP
-
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
-
2'-AMP, 3'-AMP
-
additional information
-
nilutamide and PPDNS do not display efficient inhibition at 0.025 and 0.125 mM
-
additional information
-
GTP and GpppA do not inhibit N7 MTase activity
-
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.
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.
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.
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
0.00005 - 0.002
1,8-dihydroxyanthracen-9(10H)-one
0.00128 - 0.011
1-(4-tert-butylphenyl)-N-methyl-N-[(naphthalen-1-yl)methyl]methanamine
0.159
1-(diphenylmethyl)-4-methylpiperazine hydrochloride (1:1)
Homo sapiens
-
at pH 8.0 and 30°C
0.0091 - 0.0168
1-(diphenylmethyl)-4-[(2E)-3-phenylprop-2-en-1-yl]piperazine
0.2268
1-[(4-chlorophenyl)(phenyl)methyl]-4-methylpiperazine
Homo sapiens
-
at pH 8.0 and 30°C
0.0062 - 0.0088
1-[(4-chlorophenyl)(phenyl)methyl]-4-[(3-methylphenyl)methyl]piperazine
0.0135 - 0.0137
1-[bis(4-fluorophenyl)methyl]-4-[(2,3,4-trimethoxyphenyl)methyl]piperazine
0.0073 - 0.0143
1-[bis(4-fluorophenyl)methyl]-4-[(2Z)-3-phenylprop-2-en-1-yl]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
0.00032 - 0.00074
3,3',4',5,5',7-hexahaxdroxyflavone
0.0004 - 0.0013
3,3',4',5,7-pentahydroxyflavone
0.01 - 0.0237
3,4',5,7-tetrahydroxyflavone
0.0055 - 0.031
3,8-diamino-5-[3-[diethyl(methyl)azaniumyl]propyl]-6-phenylphenanthridin-5-ium
0.0023 - 0.00572
aurintricarboxylic acid
0.1
aza-S-adenosyl-L-methionine
Encephalitozoon cuniculi
-
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
0.035
carbocyclic aza-S-adenosyl-L-methionine
Encephalitozoon cuniculi
-
0.001 - 0.0015
N-(2-[[(4-methoxyphenyl)methyl](pyrimidin-2-yl)amino]ethyl)-N,N-dimethylhexadecan-1-aminium
1.18
ribavirin
Chikungunya virus
at pH 7.3 and 25°C
0.00177
S-adenosyl-homocysteine
Dengue virus
-
pH 7.5, 20°C
0.004 - 0.021
S-adenosyl-L-homocysteine
0.000021 - 0.00269
sinefungin
0.00005
1,8-dihydroxyanthracen-9(10H)-one
Homo sapiens
-
at pH 8.0 and 30°C
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
0.00032
3,3',4',5,5',7-hexahaxdroxyflavone
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
0.0004
3,3',4',5,7-pentahydroxyflavone
Homo sapiens
-
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
0.01
3,4',5,7-tetrahydroxyflavone
Homo sapiens
-
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
0.00572
aurintricarboxylic acid
Chikungunya virus
at pH 7.3 and 25°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
0.004
S-adenosyl-L-homocysteine
Encephalitozoon cuniculi
-
0.021
S-adenosyl-L-homocysteine
Saccharomyces cerevisiae
-
-
0.000021
sinefungin
Saccharomyces cerevisiae
-
-
0.00003
sinefungin
Dengue virus
-
pH 7.5, 20°C
0.000112
sinefungin
Severe acute respiratory syndrome-related coronavirus
-
at pH 8.0 and 30°C
0.0015
sinefungin
Encephalitozoon cuniculi
-
0.00269
sinefungin
Chikungunya virus
at pH 7.3 and 25°C
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.
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.
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.
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.
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.
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.
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.
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
E225D
growth at all temperatures
E225Q
growth at all temperatures
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
F214L
growth at all temperatures, slow growth at 37°C
H144A/Y145F
fully functional
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
K75Q
slow growth at all temperatures
K75R
growth at all temperatures
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
P175A
grows as well as the wild-type ECM1 strain at all temperatures
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
Y124F
growth at all temperatures, slow growth at 37°C
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
Y212F
growth at all temperatures
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
C416R
mutation abolishes the N7-MTase activity on GTP
D273A
97% of wild-type methylation activity
D331E
70% of wild-type methylation activity
G416R
45% of wild-type methylation activity
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
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
D144A
-
TbCmt1 mutant shows 5% of wild-type activity
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
F171A
-
TbCmt1 mutant displays near-wild-type activity
H174A
-
TbCmt1 mutant displays near-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
V241A
-
TbCmt1 mutant displays near-wild-type activity
V242A
-
TbCmt1 mutant displays near-wild-type activity
Y175A
-
TbCmt1 mutant shows 3% of wild-type activity
Y246A
-
TbCmt1 mutant shows 2% of 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
D545A
-
the mutant has 102% of wild type activity
D598E
-
the mutant enzyme has 1% of wild type activity
D598N
-
the mutant enzyme hasless than 1% of wild type activity
D604E
-
the mutant enzyme has 112% of wild type activity
D604N
-
the mutant enzyme has less than 1% of wild type activity
D620E
-
the mutant enzyme has 59% of wild type activity
D620N
-
the mutant enzyme has 11% of wild type activity
D657A
-
the mutant enzyme has 112% of wild type activity
D676A
-
the mutant enzyme has less than 1% of wild type activity
D676E
-
the mutant enzyme has 40% of wild type activity
D676N
-
the mutant enzyme has less than 1% of wild type activity
E104A/G11A
-
modest defect, grows well at 19, 30 and 34 °C, but slowly at 37°C
E24A-25A
-
temperature-sensitive vD12 allele, does not grow at 37°C
E275A/N276A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
E763A
-
the mutant enzyme has 16% of wild type activity
E763D
-
the mutant enzyme has 1% of wild type activity
E763Q
-
the mutant enzyme has 32% of wild type activity
E816A
-
the mutant enzyme has 76% of wild type activity
F176A/K177A
-
lethal at all temperatures
F44A/L45A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
F556A
-
the mutant has 1% of wild type activity
F556L
-
the mutant has 3% of wild type activity
F609A
-
the mutant enzyme has 117% of wild type activity
F659A
-
the mutant enzyme has 96% of wild type activity
F679A
-
the mutant enzyme has 5% of wild type activity
F679H
-
the mutant enzyme has 13% of wild type activity
F679I
-
the mutant enzyme has 18% of wild type activity
F679L
-
the mutant enzyme has 55% of wild type activity
F679N
-
the mutant enzyme has 18% of wild type activity
F679V
-
the mutant enzyme has 20% of wild type activity
F814A
-
the mutant enzyme has 99% of wild type activity
F815A
-
the mutant enzyme has 92% of wild type activity
G600A
-
in D1 fragment, amino acids 498-844, 4% activity remaining
H260A/S261A
-
modest defect, grows well at 19, 30 and 34°C, but very slowly at 37°C
H682N
-
the mutant enzyme has 1% of wild type activity
H682Q
-
the mutant enzyme has 4% of wild type activity
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
K156A
-
viable at 19°C and 30°C, but fails to grow at 34°C
K156A/L157A
-
lethal at all temperatures
K223A/D223A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
K573A
-
the mutant enzyme has less than 1% of wild type activity
K573Q
-
the mutant enzyme has less than 1% of wild type activity
K573R
-
the mutant enzyme has 1% of wild type activity
K607A
-
the mutant enzyme has101% of wild type activity
K607Q
-
the mutant enzyme has 74% of wild type activity
K607R
-
the mutant enzyme has 13% of wild type activity
L167A
-
viable at 19°C and 30°C, but fails to grow at 34°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
N42A-Y43A
-
temperature-sensitive vD12 allele, does not grow at 37°C
N54A/R55A
-
modest defect, grows well at 19 and 30°C, but slowly at 34 and very slowly at 37°C
N550A
-
the mutant has 3% of wild type activity
N550D
-
the mutant has 19% of wild type activity
N550Q
-
the mutant has 10% of wild type activity
N570A
-
the mutant enzyme has 37% of wild type activity
N570D
-
the mutant enzyme has 21% of wild type activity
N570Q
-
the mutant enzyme has 73% of wild type activity
N601A
-
the mutant enzyme has 32% of wild type activity
P158A/T159A
-
temperature-sensitive vD12 allele, only grows at 19°C
P35A/S36A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
Q678A
-
the mutant enzyme has 55% of wild type activity
R280A-R281A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
R548A
-
the mutant has 59% of wild type activity
R560A
-
the mutant has 18% of wild type activity
R560K
-
the mutant has 84% of wild type activity
R560Q
-
the mutant has 84% of wild type activity
R562A
-
the mutant has 10% of wild type activity
R562K
-
the mutant has 25% of wild type activity
R562Q
-
the mutant has 23% of wild type activity
R632K
-
the mutant enzyme has 72% of wild type activity
R632Q
-
the mutant enzyme has 58% of wild type activity
R655A
-
the mutant has 31% of wild type activity
R794A
-
the mutant has 124% of wild type activity
R808A
-
the mutant has 142% of wild type activity
S186A/D187A
-
modest defect, grows well at 19, 30 and 34°C, but very slowly at 37°C
S569A
-
the mutant enzyme has 39% of wild type activity
V750A
-
the mutant enzyme has 59% of wild type activity
W189A/L190A
-
temperature-sensitive vD12 allele, does not grow at 37°C
W677A
-
the mutant enzyme has 4% of wild type activity
Y258A-V259A
-
modest defect, grows well at 19, 30 and 34°C, but slowly at 37°C
Y39A/G40A
-
temperature-sensitive vD12 allele, does not grow at 37°C
Y555A
-
the mutant has 2% of wild type activity
Y555F
-
the mutant has 94% of wild type activity
Y555L
-
the mutant has 2% of wild type activity
Y555S
-
the mutant has 4% of wild type activity
Y608A
-
the mutant enzyme has 3% of wild type activity
Y608F
-
the mutant enzyme has 74% of wild type activity
Y608L
-
the mutant enzyme has 62% of wild type activity
Y608S
-
the mutant enzyme has 2% of wild type activity
Y683A
-
in D1 fragment, amino acids 498-844, 0.05% activity remaining, unable to crosslink the cap in presence of S-adenosyl-L-homocysteine
Y683F
-
in D1 fragment, amino acids 498-844, 4% activity remaining
Y683S
-
in D1 fragment, amino acids 498-844, catalytically defective, unable to crosslink the cap in presence of S-adenosyl-L-homocysteine
Y764A
-
the mutant enzyme has 18% of wild type activity
Y836A
-
the mutant enzyme has 15% of wild type activity
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
H42A
-
the mutant shows wild type N7 MTase activity
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
T216A
-
the mutant shows wild type N7 MTase activity
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
D70A
lethal
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
D70E
growth at all temperatures
D70N
lethal
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
D78E
growth at all temperatures except at 37°C
D78N
growth at all temperatures
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
D94E
growth at all temperatures
D94N
lethal
E225A
growth at all temperatures except at 37°C
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
F214A
growth at all temperatures except at 37°C
H144A
growth at all temperatures
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
K267A
growth at all temperatures
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
K54Q
lethal
K54R
lethal
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
K81Q
lethal
K81R
lethal
N51A
-
site-directed mutagenesis, no complementation of the yeast abd1DELTA mutant at 25°C and 30°C, not at 37°C
N51D
lethal
R106A
-
site-directed mutagenesis, only slight complementation of the yeast abd1DELTA mutant at 25°C and 30°C, not at 37°C
R106K
lethal
R106Q
lethal
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
R59A
growth at all temperatures
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
R84A
growth at all temperatures
Y124A
-
site-directed mutagenesis, complementation of the yeast abd1DELTA mutant at 25°C and 30°C, not at 37°C, temperature-sensitive phenotype
Y145A
lethal
Y145F
grows as well as the wild-type ECM1 strain at all temperatures
Y145F
growth at all temperatures
Y145L
grows as well as the wild-type ECM1 strain at all temperatures
Y145L
growth at all temperatures
Y145S
lethal
Y212A
growth at all temperatures except at 37°C
C382Y
15-50% of wild-type activity
C382Y
72% of wild-type methylation activity
C414R
complete loss of methylation activity
C414R
mutation abolishes the N7-MTase activity on GTP
D243A
-
the point mutation in the ExoN domain does not significantly interfere with the N7-MTase function
D243A
79% of wild-type methylation activity
D331A
-
the mutation destroys the MTase activity of nsp14 in vivo
D331A
complete loss of methylation activity
D331A
mutation abolishes the N7-MTase activity on GTP
D331Y
complete loss of methylation activity
D331Y
mutation abolishes the N7-MTase activity on GTP
D352A
15-50% of wild-type activity
D352A
47% of wild-type methylation activity
D90A/E92A
-
the point mutation in the ExoN domain does not significantly interfere with the N7-MTase function
D90A/E92A
93% of wild-type methylation activity
F73A
91% of wild-type methylation activity
F73A
mutation abolishes the N7-MTase activity on GTP
G333A
complete loss of methylation activity
G333A
mutation abolishes the N7-MTase activity on GTP
H268L
-
the point mutation in the ExoN domain does not significantly interfere with the N7-MTase function
H268L
85% of wild-type methylation activity
I332A
15-50% of wild-type activity
I332A
83% of wild-type methylation activity
K336A
15-50% of wild-type activity
K336A
50% of wild-type methylation activity
P335A
61% of wild-type methylation activity
P335A
mutation abolishes the N7-MTase activity on GTP
R310A
complete loss of methylation activity
R310A
mutation abolishes the N7-MTase activity on GTP
R84A
6% of wild-type methylation activity
R84A
mutation abolishes the N7-MTase activity on GTP
T428A
15-50% of wild-type activity
T428A
27% of wild-type methylation activity
W86A
complete loss of methylation activity
W86A
mutation abolishes the N7-MTase activity on GTP
Y368A
complete loss of methylation activity
Y368A
mutation abolishes the N7-MTase activity on GTP
Y420A
15-50% of wild-type activity
Y420A
5% of wild-type methylation activity
F141A/R142A
-
grows slowly at 19 and 30°C and fails to grow at 34°C or higher
F141A/R142A
-
temperature-sensitive vD12 allele, does not grow above 34°C
H682A
-
in D1 fragment, amino acids 498-844, 4% activity remaining, unable to crosslink the cap in presence of S-adenosyl-L-homocysteine
H682A
-
the mutant enzyme has less than 1% of wild type activity
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
-
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
-
exchange of 8 residues for alanine in the D1 fragment, amino acids 498-844
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
-
construction of carboxyl-truncated D1 genes, amino acid 1-666 and 1-425: 347 residues are sufficient for activity
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Pugh, C.S.G.; Borchardt, R.T.
Effects of S-adenosylhomocysteine analogues on vaccinia viral messenger ribonucleic acid synthesis and methylation
Biochemistry
21
1535-1541
1982
Vaccinia virus
brenda
Cross, R.K.
Identification of a unique guanine-7-methyltransferase in Semliki Forest virus (SFV) infected cell extracts
Virology
130
452-463
1983
Semliki forest virus
brenda
Martin, S.A.; Paoletti, E.; Moss, B.
Purification of mRNA guanylyltransferase and mRNA (guanine-7-) methyltransferase from vaccinia virions
J. Biol. Chem.
250
9322-9329
1975
Vaccinia virus, Vaccinia virus WR
brenda
Martin, S.A.; Moss, B.
Modification of RNA by mRNA guanylyltransferase and mRNA (guanine-7-)methyltransferase from vaccinia virions
J. Biol. Chem.
250
9330-9335
1975
Vaccinia virus
brenda
Ensinger, M.J.; Martin, S.A.; Paoletti, E.; Moss, B.
Modification of the 5-terminus of mRNA by soluble guanylyl and methyl transferases from vaccinia virus
Proc. Natl. Acad. Sci. USA
72
2525-2529
1975
Vaccinia virus
brenda
Cong, P.; Shuman, S.
Methyltransferase and subunit association domains of vaccinia virus mRNA capping enzyme
J. Biol. Chem.
267
16424-16429
1992
Vaccinia virus
brenda
Higman, M.A.; Bourgeois, N.; Niles, E.G.
The vaccinia virus mRNA (guanine-N7-)-methyltransferase requires both subunits of the mRNA capping enzyme for activity
J. Biol. Chem.
267
16430-16437
1992
Vaccinia virus
brenda
Ensinger, M.J.; Moss, B.
Modification of the 5 terminus of mRNA by an RNA (guanine-7-)-methyltransferase from HeLa cells
J. Biol. Chem.
251
5283-5291
1976
Homo sapiens
brenda
Martin, S.A.; Moss, B.
mRNA guanylyltransferase and mRNA (guanine-7-)-methyltransferase from vaccinia virions. Donor and acceptor substrate specificites
J. Biol. Chem.
251
7313-7321
1976
Vaccinia virus, Vaccinia virus WR
brenda
Pugh, C.S.; Borchardt, R.T.; Stone, H.O.
Inhibition of Newcastle disease virion messenger RNA (guanine-7-)-methyltransferase by analogues of S-adenosylhomocysteine
Biochemistry
16
3928-3932
1977
Avian orthoavulavirus 1
brenda
Germershausen, J.; Goodman, D.; Somberg, E.W.
5 Cap methylation of homologous poly A(+) RNA by a RNA (guanine-7) methyltransferase from Neurospora crassa
Biochem. Biophys. Res. Commun.
82
871-878
1978
Neurospora crassa
brenda
Goswami, B.B.; Crea, R.; Van Boom, J.H.; Sharma, O.K.
2-5-Linked oligo(adenylic acid) and its analogs. A new class of inhibitors of mRNA methylation
J. Biol. Chem.
257
6867-6870
1982
Mus musculus, Vaccinia virus
brenda
Locht, C.; Beaudart, J.L.; Delcour, J.
Partial purification and characterization of mRNA (guanine-7-) methyltransferase from the yeast Saccharomyces cerevisiae
Eur. J. Biochem.
134
117-121
1983
Saccharomyces cerevisiae, Saccharomyces cerevisiae VY1160
brenda
Guo, P.; Moss, B.
Interaction and mutual stabilization of the two subunits of vaccinia virus mRNA capping enzyme coexpressed in Escherichia coli
Proc. Natl. Acad. Sci. USA
87
4023-4027
1990
Vaccinia virus
brenda
Monroy, G.; Spencer, E.; Hurwitz, J.
Purification of mRNA guanylyltransferase from vaccinia virions
J. Biol. Chem.
253
4481-4489
1978
Vaccinia virus, Vaccinia virus WR
brenda
Ramadevi, N.; Burroughs, N.J.; Mertens, P.P.C.; Jones, I.M.
Capping and methylation of mRNA by purified recombinant VP4 protein of bluetongue virus
Proc. Natl. Acad. Sci. USA
95
13537-13542
1998
bluetongue virus
brenda
Ahola, T.; Lampio, A.; Auvinen, P.; Kaariainen, L.
Semliki forest virus mRNA capping enzyme requires association with anionic membrane phospholipids for activity
EMBO J.
18
3164-3172
1999
Semliki forest virus
brenda
Higman, M.A.; Christen, L.A.; Niles, E.G.
The mRNA (guanine-7-)methyltransferase domain of the vaccinia virus mRNA capping enzyme. Expression in Escherichia coli and structural and kinetic comparison to the intact capping enzyme
J. Biol. Chem.
269
14974-14981
1994
Vaccinia virus
brenda
Mao, X.; Shuman, S.
Intrinsic RNA (guanine-7) methyltransferase activity of the vaccinia virus capping enzyme D1 subunit is stimulated by the D12 subunit. Identification of amino acid residues in the D1 protein required for subunit association and methyl group transfer
J. Biol. Chem.
269
24472-24479
1994
Vaccinia virus
brenda
Tsukamoto, T.; Shibagaki, Y.; Niikura, Y.; Mizumoto, K.
Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase
Biochem. Biophys. Res. Commun.
251
27-34
1998
Homo sapiens, Saccharomyces cerevisiae (P32783)
brenda
Yokoska, J.i.; Tsukamoto, T.; Miura, K.i.; Shiokawa, K.; Mizumoto, K.
Cloning and characterization of mRNA capping enzyme and mRNA (guanine-7-)-methyltransferase cDNAs from Xenopus laevis
Biochem. Biophys. Res. Commun.
268
617-624
2000
Xenopus laevis (Q9I8S2), Xenopus laevis (Q9IA92), Xenopus laevis (Q9IA93)
brenda
Wen, Y.; Shatkin, A.J.
Cap methyltransferase selective binding and methylation of GpppG-RNA are stimulated by importin-alpha
Genes Dev.
14
2944-2949
2000
Homo sapiens
brenda
Mao, X.; Shuman, S.
Vaccinia virus mRNA (guanine-7-)methyltransferase: mutational effects on cap methylation and AdoHcy-dependent photo-crosslinking of the cap to the methyl acceptor site
Biochemistry
35
6900-6910
1996
Vaccinia virus
brenda
Li, Y.I.; Chen, Y.J.; Hsu, Y.H.; Meng, M.
Characterization of the Adomet-dependent guanylyltransferase activity that is associated with the N terminus of bamboo mosaic virus replicase
J. Virol.
75
782-788
2001
bamboo mosaic virus
brenda
Fabrega, C.; Hausmann, S.; Shen, V.; Shuman, S.; Lima, C.D.
Structure and mechanism of mRNA cap (guanine-N7) methyltransferase
Mol. Cell
13
77-89
2004
Encephalitozoon cuniculi
brenda
Shafer, B.; Chu, C.; Shatkin, A.J.
Human mRNA cap methyltransferase: alternative nuclear localization signal motifs ensure nuclear localization required for viability
Mol. Cell. Biol.
25
2644-2649
2005
Homo sapiens
brenda
Hausmann, S.; Zheng, S.; Fabrega, C.; Schneller, S.W.; Lima, C.D.; Shuman, S.
Encephalitozoon cuniculi mRNA cap (guanine N-7) methyltransferase: methyl acceptor specificity, inhibition BY S-adenosylmethionine analogs, and structure-guided mutational analysis
J. Biol. Chem.
280
20404-20412
2005
Encephalitozoon cuniculi (Q8SR66), Encephalitozoon cuniculi
brenda
Zheng, S.; Hausmann, S.; Liu, Q.; Ghosh, A.; Schwer, B.; Lima, C.D.; Shuman, S.
Mutational analysis of Encephalitozoon cuniculi mRNA cap (guanine-N7) methyltransferase, structure of the enzyme bound to sinefungin, and evidence that cap methyltransferase is the target of sinefungins antifungal activity
J. Biol. Chem.
281
35904-35913
2006
Saccharomyces cerevisiae, Encephalitozoon cuniculi (Q8SR66), Encephalitozoon cuniculi
brenda
Peyrane, F.; Selisko, B.; Decroly, E.; Vasseur, J.J.; Benarroch, D.; Canard, B.; Alvarez, K.
High-yield production of short GpppA- and 7MeGpppA-capped RNAs and HPLC-monitoring of methyltransfer reactions at the guanine-N7 and adenosine-2O positions
Nucleic Acids Res.
35
e26
2007
Homo sapiens
brenda
Hall, M.P.; Ho, C.K.
Characterization of a Trypanosoma brucei RNA cap (guanine N-7) methyltransferase
RNA
12
488-497
2006
Trypanosoma brucei
brenda
Schwer, B.; Shuman, S.
Genetic analysis of poxvirus mRNA cap methyltransferase: suppression of conditional mutations in the stimulatory D12 subunit by second-site mutations in the catalytic D1 subunit
Virology
352
145-156
2006
Vaccinia virus
brenda
Zheng, S.; Shuman, S.
Mutational analysis of vaccinia virus mRNA cap (guanine-N7) methyltransferase reveals essential contributions of the N-terminal peptide that closes over the active site
RNA
14
2297-2304
2008
Vaccinia virus
brenda
Milani, M.; Mastrangelo, E.; Bollati, M.; Selisko, B.; Decroly, E.; Bouvet, M.; Canard, B.; Bolognesi, M.
Flaviviral methyltransferase/RNA interaction: structural basis for enzyme inhibition
Antiviral Res.
83
28-34
2009
Dengue virus, Wesselsbron virus
brenda
Selisko, B.; Peyrane, F.F.; Canard, B.; Alvarez, K.; Decroly, E.
Biochemical characterization of the (nucleoside-2'O)-methyltransferase activity of dengue virus protein NS5 using purified capped RNA oligonucleotides (7Me)GpppAC(n) and GpppAC(n)
J. Gen. Virol.
91
112-121
2010
Dengue virus
brenda
Dong, H.; Ren, S.; Zhang, B.; Zhou, Y.; Puig-Basagoiti, F.; Li, H.; Shi, P.Y.
West Nile virus methyltransferase catalyzes two methylations of the viral RNA cap through a substrate-repositioning mechanism
J. Virol.
82
4295-4307
2008
West Nile virus
brenda
Cowling, V.H.
Enhanced mRNA cap methylation increases cyclin D1 expression and promotes cell transformation
Oncogene
29
930-936
2009
Homo sapiens
brenda
Chen, Y.; Cai, H.; Pan, J.; Xiang, N.; Tien, P.; Ahola, T.; Guo, D.
Functional screen reveals SARS coronavirus nonstructural protein nsp14 as a novel cap N7 methyltransferase
Proc. Natl. Acad. Sci. USA
106
3484-3489
2009
Severe acute respiratory syndrome-related coronavirus
brenda
Zheng, S.; Shuman, S.
Structure-function analysis of vaccinia virus mRNA cap (guanine-N7) methyltransferase
RNA
14
696-705
2008
Vaccinia virus
brenda
Chung, K.Y.; Dong, H.; Chao, A.T.; Shi, P.Y.; Lescar, J.; Lim, S.P.
Higher catalytic efficiency of N-7-methylation is responsible for processive N-7 and 2-O methyltransferase activity in dengue virus
Virology
402
52-60
2010
Dengue virus
brenda
Dong, H.; Chang, D.C.; Xie, X.; Toh, Y.X.; Chung, K.Y.; Zou, G.; Lescar, J.; Lim, S.P.; Shi, P.Y.
Biochemical and genetic characterization of dengue virus methyltransferase
Virology
405
568-578
2010
Dengue virus
brenda
Zhang, X.; Wei, Y.; Ma, Y.; Hu, S.; Li, J.
Identification of aromatic amino acid residues in conserved region VI of the large polymerase of vesicular stomatitis virus is essential for both guanine-N-7 and ribose 2-O methyltransferases
Virology
408
241-252
2010
vesicular stomatitis virus
brenda
Sun, Y.; Wang, Z.; Tao, J.; Wang, Y; Wu, A; Yang, Z.; Wang, K.; Shi, L.; Chen, Y.; Guo, D.
Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase
Antiviral Res.
104
156-164
2014
Severe acute respiratory syndrome-related coronavirus (P0C6X7), Severe acute respiratory syndrome-related coronavirus
brenda
Chen, Y.; Tao, J.; Sun, Y.; Wu, A.; Su, C.; Gao, G.; Cai, H.; Qiu, S., Wu, Y.; Ahola, T., Guo, D.
Structure-function analysis of severe acute respiratory syndrome coronavirus RNA cap guanine-N7-methyltransferase
J. Virol.
87
6296-6305
2013
Severe acute respiratory syndrome-related coronavirus (P0C6X7), Severe acute respiratory syndrome-related coronavirus
brenda
Thillier, Y.; Decroly, E.; Morvan, F.; Canard, B.; Vasseur, J.J.; Debart, F.
Synthesis of 5' cap-0 and cap-1 RNAs using solid-phase chemistry coupled with enzymatic methylation by human (guanine-N7)-methyl transferase
RNA
18
856-868
2012
Homo sapiens (O43148)
brenda
Jin, X.; Chen, Y.; Sun, Y.; Zeng, C.; Wang, Y.; Tao, J.; Wu, A.; Yu, X.; Zhang, Z.; Tian, J.; Guo, D.
Characterization of the guanine-N7 methyltransferase activity of coronavirus nsp14 on nucleotide GTP
Virus Res.
176
45-52
2013
Severe acute respiratory syndrome-related coronavirus (P0C6X7), Severe acute respiratory syndrome-related coronavirus
brenda
Aouadi, W.; Eydoux, C.; Coutard, B.; Martin, B.; Debart, F.; Vasseur, J.J.; Contreras, J.M.; Morice, C.; Querat, G.; Jung, M.L.; Canard, B.; Guillemot, J.C.; Decroly, E.
Toward the identification of viral cap-methyltransferase inhibitors by fluorescence screening assay
Antiviral Res.
144
330-339
2017
Homo sapiens, Severe acute respiratory syndrome-related coronavirus
brenda
Varshney, D.; Lombardi, O.; Schweikert, G.; Dunn, S.; Suska, O.; Cowling, V.H.
mRNA cap methyltransferase, RNMT-RAM, promotes RNA Pol II-dependent transcription
Cell Rep.
23
1530-1542
2018
Homo sapiens
brenda
Case, J.B.; Ashbrook, A.W.; Dermody, T.S.; Denison, M.R.
Mutagenesis of S-adenosyl-L-methionine-binding residues in coronavirus nsp14 N7-methyltransferase demonstrates differing requirements for genome translation and resistance to innate immunity
J. Virol.
90
7248-7256
2016
Murine hepatitis virus
brenda
Trotman, J.B.; Giltmier, A.J.; Mukherjee, C.; Schoenberg, D.R.
RNA guanine-7 methyltransferase catalyzes the methylation of cytoplasmically recapped RNAs
Nucleic Acids Res.
45
10726-10739
2017
Homo sapiens
brenda
Martin, B.; Coutard, B.; Guez, T.; Paesen, G.C.; Canard, B.; Debart, F.; Vasseur, J.J.; Grimes, J.M.; Decroly, E.
The methyltransferase domain of the Sudan ebolavirus L protein specifically targets internal adenosines of RNA substrates, in addition to the cap structure
Nucleic Acids Res.
46
7902-7912
2018
Sudan ebolavirus
brenda
Bueren-Calabuig, J.A.; G Bage, M.; Cowling, V.H.; Pisliakov, A.V.
Mechanism of allosteric activation of human mRNA cap methyltransferase (RNMT) by RAM insights from accelerated molecular dynamics simulations
Nucleic Acids Res.
47
8675-8692
2019
Homo sapiens (O43148), Homo sapiens
brenda
Dunn, S.; Lombardi, O.; Lukoszek, R.; Cowling, V.H.
Oncogenic PIK3CA mutations increase dependency on the mRNA cap methyltransferase, RNMT, in breast cancer cells
Open Biology
9
190052
2019
Homo sapiens
brenda
Kaur, R.; Mudgal, R.; Narwal, M.; Tomar, S.
Development of an ELISA assay for screening inhibitors against divalent metal ion dependent alphavirus capping enzyme
Virus Res.
256
209-218
2018
Chikungunya virus (A0A1I9WLN6), Chikungunya virus
brenda