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2.1.1.57: methyltransferase cap1

This is an abbreviated version!
For detailed information about methyltransferase cap1, go to the full flat file.

Word Map on EC 2.1.1.57

Reaction

S-adenosyl-L-methionine
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA]
=
S-adenosyl-L-homocysteine
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]

Synonyms

(nucleoside-2'-O-)-methyltransferase, (nucleoside-2'O)-methyltransferase, 2'-O methyltransferase, 2'-O MTase, 2'-O-methyltransferase, 2'-O-MTase, 2'O methyltransferase, 2'O-MTase, 2'OMTases, cap-specific 2'-O-methyltransferase, cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1, cap1 2-O'-ribose methyltransferase, CMTr1, EC 2.1.1.58, FtsJ methyltransferase domain-containing 2, FTSJD2, ISG95, KIAA0082, L protein domain VI, large polymerase protein domain VI, messenger ribonucleate nucleoside 2'-methyltransferase, messenger RNA (nucleoside-2'-)-methyltransferase, methyltransferase, messenger ribonucleate nucleoside 2'-, mRNA (nucleoside-2'-O)-methyltransferase, mRNA 5' cap-specific (nucleoside-2'-O)-methyltransferase, mRNA cap (nucleoside-2'-O)-methyltransferase, mRNA cap methyltransferase, mRNA cap-specific 2'-O-methyltransferase, MT57, Mtr1, nonstructural protein 16, nonstructural protein 16 methyltransferase, nonstructural protein 5 methyltransferase, NS5, NS5 MTase, NS5MTase, nsp10/16 complex, nsp10/nsp16 complex, nsp16, nsp16 protein, nsp16/nsp10 protein complex, ribose 2'-O methyltransferase, RNA (nucleoside-2'O)-methyltransferase, RNA cap 2'-O-methyltransferase, RNA cap 2'-O-MTase, RNA cap 2'O-MTase, RNA cap1 methyltransferase, RNA capping enzyme domain in protein A, S-adenosyl-L-methionine-dependent mRNA cap MTase, TbMT48, TbMT57, VP39, VP4

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.57 methyltransferase cap1

Engineering

Engineering on EC 2.1.1.57 - methyltransferase cap1

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D265E
complete loss of 2'-O-methylation activity, Bluetongue virus replication in cells is abrogated
D265V
complete loss of 2'-O-methylation activity, Bluetongue virus replication in cells is abrogated
N311A
2fold reduction of 2'-O-methylation activity, Bluetongue virus replication in cells is abrogated
N311A/Y334/R367A
2fold reduction of 2'-O-methylation activity, Bluetongue virus replication in cells is abrogated
R367A
mutation does not affect methyl group transfer
Y334A
mutation does not affect methyl group transfer
D113A
-
about 110% substrate binding and activity compared to the wild type enzyme
D129A
-
about 40% substrate binding and activity compared to the wild type enzyme
D221A
-
about 115% substrate binding and activity compared to the wild type enzyme
D247A
-
about 75% substrate binding and activity compared to the wild type enzyme
E202A
-
about 30% substrate binding and activity compared to the wild type enzyme
F173A
-
about 20% substrate binding and activity compared to the wild type enzyme
K169A
-
about 20% substrate binding and activity compared to the wild type enzyme
K45A
-
about 1% substrate binding and activity compared to the wild type enzyme
W4A
-
about 90% substrate binding and activity compared to the wild type enzyme
Y14A
-
about 10% substrate binding and activity compared to the wild type enzyme
Y29A
-
about 15% substrate binding and activity compared to the wild type enzyme
D141A
-
RNA synthesis is severely impaired in this mutant
DELTA2-35
-
RNA synthesis is severely impaired in this mutant
H93A
-
RNA synthesis is severely impaired in this mutant
R100A
-
RNA synthesis is severely impaired in this mutant
W215A
-
the mutant shows reduced RNA synthesis activity compared to the wild type
K239A
-
the mutant shows no activity
D106A
-
the mutant shows 38% of wild type activity
D130A
-
the mutant shows 2% of wild type activity
G73A
-
the mutant shows 18% of wild type activity
G94A
-
the nsp10 mutation binds nsp16 with a slightly reduced affinity (60%) but is still able to stimulate nsp16 2'O-MTase activity
G94D
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
I40A
-
the mutant shows 8% of wild type activity
K46A
-
the mutant shows 1% of wild type activity
K93E
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
K95A
-
the nsp10 mutation binds nsp16 with a slightly reduced affinity (80%) but is still able to stimulate nsp16 2'O-MTase activity
M41A
-
the mutant shows 4% of wild type activity
M44A
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
N43A
-
the mutant shows 11% of wild type activity
Q87A
-
the mutant shows 62% of wild type activity
R78A
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
R78G
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
S188A
-
the substitution shows 72% loss of activity with no significant effect on the stability of the nsp10/nsp16 complex
S72A
-
the mutant protein binds nsp16 but weakly activates 2'O-MTase activity
T48A
-
the mutant shows 20% of wild type activity
T54E
-
the substitution shows 72% loss of activity with no significant effect on the stability of the nsp10/nsp16 complex
T58A
-
the substitution shows 43% loss of activity with no significant effect on the stability of the nsp10/nsp16 complex
T58E
-
the substitution shows 99% loss of activity with 54% association of the Nsp10/nsp16 complex compared to the wild type
T58N
-
the substitution shows 70% loss of activity with no significant effect on the stability of the nsp10/nsp16 complex
V104G
-
the mutant shows 4% of wild type activity
V42A
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
V44A
-
the mutant shows 1% of wild type activity
Y132A
-
the mutant shows 5% of wild type activity
Y132F
-
the mutant shows 9% of wild type activity
Y132T
-
the mutant shows 5% of wild type activity
Y30A
-
the mutant shows 1% of wild type activity
Y30F
-
the mutant shows 6% of wild type activity
Y96I
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
Y96V
-
the nsp10 mutation abrogates stimulation of nsp16 enzyme activity
G70A
-
the mutant shows reduced activity compared to the wild type
-
K93A
-
the mutant shows reduced activity compared to the wild type
-
K266A
proteins similar to that of the wild-type TbMT57-HA protein, defective in the biogenesis of the SL cap 4 structure
C178S
-
point mutations, glutathione-S-transferase-tagged, exchange shows no effect
C272S
-
point mutations, glutathione-S-transferase-tagged, exchange shows no effect
C272S/K175C/R209K
2-bromoethylamine reveals 64% target site modification in a overnight reaction at 37°C, unmodified mutant has no detectable methyltransferase activity, whereas the modified protein is active, exhibiting 20-30% of the specific catalytic rate of wild-type
D182A
-
m7G binding pocket mutant, mutagenesis, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
D182A/E233A
-
m7G binding pocket double mutant, mutagenesis, N-terminal glutathione-S-transferase-tagged, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
E233A
-
m7G binding pocket mutant, mutagenesis, N-terminal glutathione-S-transferase-tagged, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
F180A
-
m7G binding pocket mutant, mutagenesis, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
F180W
-
no apparent defects in catalytic activity
K175C
aziridine reveals 66.7% target site modification in a 4 h, room temperature reaction, equivalent modification level achieved in an overnight incubation using 2-bromoethylamine at 37°C, but protein losses due to aggregation during the modification reaction are, notably, negligible in the lower temperature/shorter duration reactions employed for aziridine
Y22A
-
m7G binding pocket mutant, mutagenesis, N-terminal glutathione-S-transferase-tagged, C-terminal truncated by 26 amino acids, lacks specific m7G-contact side chains and shows reduced activity, but remains cap-dependent
D1762A
-
with pinpoint plaque morphologies and replication defects in single-step growth assays, viral RNA and protein synthesis is diminished
E1674A
-
the mutation in the V1 region of L protein abolishes 2'-O methylation activity
E1674D
-
the mutation in the V1 region of L protein shows severely reduced 2'-O methylation activity (about 20%) compared to the wild type
E1674K
-
the mutation in the V1 region of L protein shows severely reduced 2'-O methylation activity (about 15%) compared to the wild type
E1674Q
-
the mutation in the V1 region of L protein shows severely reduced 2'-O methylation activity (about 15%) compared to the wild type
E1833A
-
with pinpoint plaque morphologies and most significant replication defects in single-step growth assays, viral RNA and protein synthesis is diminished
E1833Q
-
delay in replication
F1691A
-
the mutation in the V1 region of L protein abolishes 2'-O methylation activity
F1691W
-
the mutation in the V1 region of L protein shows slightly reduced 2'-O methylation activity (about 78%) compared to the wild type
F1691Y
-
the mutation in the V1 region of L protein shows slightly reduced 2'-O methylation activity (about 80%) compared to the wild type
G1674A
-
does not significantly perturb viral growth and gene expression, replicates with almost indistinguishable kinetics to recombinant vesicular stomatitis virus
K1651A
-
with pinpoint plaque morphologies and most significant replication defects in single-step growth assays, viral RNA and protein synthesis is diminished
K1795A
Y1650A
-
the mutation in the V1 region of L protein abolishes 2'-O methylation activity
Y1650F
-
the mutation in the V1 region of L protein shows slightly reduced 2'-O methylation activity (about 85%) compared to the wild type
Y1650W
-
the mutation in the V1 region of L protein shows slightly reduced 2'-O methylation activity (about 90%) compared to the wild type
E218A
-
the mutation abolishes 2'-O-methyltransferase activity and enhances replication but not virulence in Ifit1-deficient mice after peripheral infection
additional information