Information on EC 2.1.1.296 - methyltransferase cap2

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.296
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RECOMMENDED NAME
GeneOntology No.
methyltransferase cap2
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
mRNA capping II
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-ribonucleotide-[mRNA] 2'-O-methyltransferase
The enzyme, found in higher eukaryotes including insects and vertebrates, and their viruses, methylates the ribose of the ribonucleotide at the second transcribed position of mRNAs and snRNAs. This methylation event is known as cap2. The human enzyme can also methylate mRNA molecules where the upstream purine ribonucleotide is not methylated (see EC 2.1.1.57, methyltransferase cap1), but with lower efficiency [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
the 5' cap of human messenger RNA contains 2'-O-methylation of the first and often second transcribed nucleotide that is important for its processing, translation and stability. Enzyme responsible for the methylations are CMTr1 and CMTr2, respectively
physiological function
additional information
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 + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
show the reaction diagram
Q8IYT2
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additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CapG
the hMTr2 MTase activity is dependent on the presence of capG
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additional information
neither N7 methylation of the guanosine cap nor 2'-O-ribose methylation of the first transcribed nucleotide are required for hMTr2, but the presence of cap1 methylation increases hMTr2 activity
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
localization of hMTr2 assayed in situ by immunostaining of epitope-tagged protein
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Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CMTr2 is divided into two parts: the amino-terminal part with the catalytic RFM domain (CMTr21-430) and the C-terminal part with the non-catalytic RFM domain (CMTr2430-770). The single domains of CMTr2 do not bind the substrate and do not exhibit any cap MTase activity alone or when mixed together as separately purified chains. Thus, CMTr2 requires both RFM domains in a single polypeptide chain for substrate binding and methylation
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene CMTR2, recombinant overexpression of wild-type and mutant enzymes in HEK-293 cells
gene HMTR2 or FTSJD1, phylogenetic tree, functional overexpression of the cap2 MTase hMTr2 and of c-myc-tagged enzyme in MCF7 cells
primer extension analysis, functional expression observed of the MT48 gene tagged at the C-terminus with an HA epitope in mt48-/- cells
the mt57-/- mutant cells are complemented with the triple MT57 mutant W62D/G63D/Q64D and with MT57 containing the K266A mutation, both mutants do not reestablish the +5 primer extension stop to wild-type levels
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E145A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
H142A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
K307A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
K74A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
L77A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
T89A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
W85A
site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity
K266A
site-directed mutagenesis, partly complements the enzyme defective mtant MT57-/- cells
W62D/G63D/Q64D
site-directed mutagenesis, partly complements the enzyme defective mtant MT57-/- cells
additional information