Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.1.1.57 - methyltransferase cap1 and Organism(s) Vaccinia virus and UniProt Accession P07617

for references in articles please use BRENDA:EC2.1.1.57
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.57 methyltransferase cap1
IUBMB Comments
This enzyme catalyses the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules. This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses. The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Vaccinia virus
UNIPROT: P07617
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Vaccinia virus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA]
=
+
a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Synonyms
nsp16, 2'-o-methyltransferase, 2'-o-mtase, cmtr1, ns5 mtase, 2'-o mtase, (nucleoside-2'-o-)-methyltransferase, nonstructural protein 16, 2'-o methyltransferase, isg95, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
mRNA cap-specific 2'-O-methyltransferase
-
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
-
i.e. VP39
mRNA cap-specific 2'-O-methyltransferase
-
i.e. VP39
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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]
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:5-(N7-methyl 5-triphosphoguanosine)-(ribonucleotide)-[mRNA] 2-O-methyltransferase
This enzyme catalyses the methylation of the ribose on the first transcribed nucleotide of mRNA or snRNA molecules. This methylation event is known as cap1, and occurs in all mRNAs and snRNAs of higher eukaryotes, including insects, vertebrates and their viruses. The human enzyme can also methylate mRNA molecules that lack methylation on the capping 5'-triphosphoguanosine [6].
CAS REGISTRY NUMBER
COMMENTARY hide
61970-02-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + m7G-(5')pppGpApApA
?
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + ApppGR-RNA
?
show the reaction diagram
S-adenosyl-L-methionine + brome mosaic virus RNA
?
show the reaction diagram
-
-
-
-
r
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
show the reaction diagram
S-adenosyl-L-methionine + m7GpppGp
S-adenosyl-L-homocysteine + m7GpppGmp
show the reaction diagram
-
substrate of minimal chain length for the cap-specific enzyme, m7GpppG is no substrate
-
-
?
S-adenosyl-L-methionine + m7GpppGpN
S-adenosyl-L-homocysteine + m7GpppGmpN
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + m7GpppGpNp
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + m7GpppGpUbiotin-p
?
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + RNA chain length 2-6 nt
?
show the reaction diagram
-
-
-
-
r
S-adenosyl-L-methionine + RNA chain length 20-50 nt
?
show the reaction diagram
-
-
-
-
r
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + m7G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppRm-RNA
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no divalent cations required
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5',N8-Adenosyl-alpha,beta-diaminobutyric acid
-
moderate
7-methylguanosine(5')pppN-dinucleotides
-
weak, competitive
A9145C
NaCl
-
above 0.05 M
S-(2-azaadenosyl)-L-homocysteine
-
-
S-(3'-aminoadenosyl)-L-homocysteine
-
-
S-(3-deazaadenosyl)-L-homocysteine
-
strong
S-(8-azaadenosyl)-L-homocysteine
-
weak
S-(N6-Dimethyl-3-deazaadenosyl)-L-homocysteine
-
weak
S-(N6-Methyladenosyl)-L-homocysteine
-
-
S-Adenosyl-D-homocysteine
-
-
S-adenosyl-L-cysteine
-
moderate
S-adenosyl-L-homocysteine
S-Adenosyl-L-homocysteine sulfone
-
strong
S-adenosyl-L-homocysteine sulfoxide
-
strong
S-Aristeromycinyl-L-homocysteine
-
-
S-Cytidyl-L-homocysteine
-
weak
S-Inosyl-L-homocysteine
-
weak
S-Tubercidinyl-L-homocysteine
-
strong
S-Uridyl-L-homocysteine
-
weak
sinefungin
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000005
brome mosaic virus RNA
-
-
-
0.00016 - 0.00023
RNA chain length 2-6 nt
-
-
-
0.000005 - 0.000015
RNA chain length 20-50 nt
-
-
-
0.002
S-adenosyl-L-methionine
-
-
additional information
additional information
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00000018 - 0.00000134
A9145C
0.0046
S-(3'-aminoadenosyl)-L-homocysteine
-
-
0.0021
S-(3-deazaadenosyl)-L-homocysteine
-
-
0.009
S-(N6-Methyladenosyl)-L-homocysteine
-
-
0.014
S-Adenosyl-D-homocysteine
-
-
0.058
S-adenosyl-L-cysteine
-
-
0.00053 - 0.001
S-adenosyl-L-homocysteine
0.0012
S-Adenosyl-L-homocysteine sulfone
-
-
0.0012
S-adenosyl-L-homocysteine sulfoxide
-
-
0.0026
S-Aristeromycinyl-L-homocysteine
-
-
0.0012
S-Tubercidinyl-L-homocysteine
-
-
0.0000075 - 0.0000194
sinefungin
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000233
-
purified enzyme
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
pI: 8.4
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8
-
m7G- and A-capped RNA substrates
6.6 - 8.1
-
about half-maximal activity at pH 6.6 and 8.1
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
gel filtration
36000
-
sucrose density gradient centrifugation
38000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 38000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
C178S
-
point mutations, glutathione-S-transferase-tagged, exchange shows no effect
C272S
-
point mutations, glutathione-S-transferase-tagged, exchange shows no effect
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
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
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
binding site of the enzyme for RNA, immediately downstream, is pH-sensitive, above pH 7.5: dramatic increase of Km
639484
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
and below, stable in the presence of 10% v/v glycerol and 250 mg/l bovine serum albumin
59
-
rapid inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
bovine serum albumin stabilizes
-
glycerol, 10% v/v stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several months
-
4°C, several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on ADP-Sepharose
-
fragment mutant and exchange mutants from recombinant E. coli
-
mutants recombinant from E. coli
-
solubilized from viral core
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant C272S/K175C/R209K
expression of wild-type, exchange mutants and open-reading-frame mutant in Escherichia coli, all glutathione-S-transferase-tagged
-
mutant enzymes are expressed in Escherichia coli and the tag is cleaved off
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
characterization of the side chain pKa for a single lysine analogue within a 316-residue protein containing 21 lysines and 1678 carbon atoms at natural isotope abundance, achieved by the single reactive cysteine of a K175C mutant of VP39 modified to S-(beta-aminoethyl)cysteine (gamma-thialysine) using freshly prepared (13C)aziridine at room temperature
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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, Vaccinia virus WR
Manually annotated by BRENDA team
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, Vaccinia virus WR
Manually annotated by BRENDA team
Barbosa, E.; Moss, B.
mRNA(nucleoside-2-)-methyltransferase from vaccinia virus. Purification and physical properties
J. Biol. Chem.
253
7692-7697
1978
Vaccinia virus, Vaccinia virus WR
Manually annotated by BRENDA team
Barbosa, E.; Moss, B.
mRNA(nucleoside-2-)-methyltransferase from vaccinia virus. Characteristics and substrate specificity
J. Biol. Chem.
253
7698-7702
1978
Vaccinia virus, Vaccinia virus WR
Manually annotated by BRENDA team
Pugh, C.S.G.; Borchardt, R.T.; Stone, H.O.
Sinefungin, a potent inhibitor of virion mRNA(guanine-7-)-methyltransferase, mRNA(nucleoside-2-)-methyltransferase, and viral multiplication
J. Biol. Chem.
253
4075-4077
1978
Vaccinia virus, Vaccinia virus WR
Manually annotated by BRENDA team
Schnierle, B.S.; Gershon, P.; Moss, B.
Cap-specific mRNA (nucleoside-O2-)-methyltransferase and poly(A) polymerase stimulatory activities of vaccinia virus are mediated by a single protein
Proc. Natl. Acad. Sci. USA
89
2897-2901
1992
Vaccinia virus, Vaccinia virus WR
Manually annotated by BRENDA team
Lockless, S.W.; Cheng, H.T.; Hodel, A.E.; Quiocho, F.A.; Gershon, P.D.
Recognition of capped RNA substrates by VP39, the vaccinia virus-encoded mRNA cap-specific 2'-O-methyltransferase
Biochemistry
37
8564-8574
1998
Vaccinia virus
Manually annotated by BRENDA team
Schnierle, B.S.; Gershon, P.D.; Moss, B.
Mutational analysis of a multifunctional protein, with mRNA 5' cap-specific (nucleoside-2'-O-)-methyltransferase and 3'-adenylyltransferase stimulatory activities, encoded by vaccinia virus
J. Biol. Chem.
269
20700-20706
1994
Vaccinia virus
Manually annotated by BRENDA team
Latner, D.R.; Xiang, Y.; Lewis, J.I.; Condit, J.; Condit, R.C.
The vaccinia virus bifunctional gene J3 (nucleoside-2'-O-)-methyltransferase and poly(A) polymerase stimulatory factor is implicated as a positive transcription elongation factor by two genetic approaches
Virology
269
345-355
2000
Vaccinia virus
Manually annotated by BRENDA team
Hu, G.; Tsai, A.L.; Quiocho, F.A.
Insertion of an N7-methylguanine mRNA cap between two coplanar aromatic residues of a cap-binding protein is fast and selective for a positively charged cap
J. Biol. Chem.
278
51515-51520
2003
Vaccinia virus
Manually annotated by BRENDA team
Li, C.; Gershon, P.D.
pKa of the mRNA cap-specific 2-O-methyltransferase catalytic lysine by HSQC NMR detection of a two-carbon probe
Biochemistry
45
907-917
2006
Vaccinia virus (P07617)
Manually annotated by BRENDA team