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Information on EC 2.1.1.56 - mRNA (guanine-N7)-methyltransferase and Organism(s) Xenopus laevis and UniProt Accession Q9I8S2

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.56 mRNA (guanine-N7)-methyltransferase
IUBMB Comments
The terminal N7-methylguanosine facilitates gene expression in eukaryotic cells and is recognized by cap-binding proteins.
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This record set is specific for:
Xenopus laevis
UNIPROT: Q9I8S2
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Word Map
The taxonomic range for the selected organisms is: Xenopus laevis
The enzyme appears in selected viruses and cellular organisms
Synonyms
non-structural protein 1, nsp14, cap methyltransferase, n7-mtase, mrna cap methyltransferase, nonstructural protein 14, tbcmt1, n7-methyltransferase, tbcgm1, guanine-n7 methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
guanine-7-methyltransferase
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messenger ribonucleate guanine 7-methyltransferase
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messenger RNA guanine 7-methyltransferase
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methyltransferase, messenger ribonucleate guanine 7-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
show the reaction diagram
RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-N7-)methyltransferase form the mRNA capping enzyme complex consiting of a small and a large subunit
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA]
show the reaction diagram
RNA triphosphatase, RNA guanylyltransferase, and RNA (guanine-N7-)methyltransferase form the mRNA capping enzyme complex consiting of a small and a large subunit
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:mRNA (guanine-N7)-methyltransferase
The terminal N7-methylguanosine facilitates gene expression in eukaryotic cells and is recognized by cap-binding proteins.
CAS REGISTRY NUMBER
COMMENTARY hide
56941-25-4
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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 + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
show the reaction diagram
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?
S-adenosyl-L-methionine + G(5')pppR-RNA
S-adenosyl-L-homocysteine + m7G(5')pppR-RNA
show the reaction diagram
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?
additional information
?
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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
additional information
?
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
fragment of 402 amino acids
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MCES_XENLA
402
0
46003
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
Western blot
58660 - 60000
DNA sequence determination, western blot
68820 - 70000
DNA sequence determination, western blot
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli, His-tagged
expression in Escherichia coli, His-tagged, amino acid sequence analysis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team