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Literature summary for 2.1.1.296 extracted from

  • Smietanski, M.; Werner, M.; Purta, E.; Kaminska, K.; Stepinski, J.; Darzynkiewicz, E.; Nowotny, M.; Bujnicki, J.
    Structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation (2014), Nat. Commun., 5, 3004.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene CMTR2, recombinant overexpression of wild-type and mutant enzymes in HEK-293 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
E145A site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity Homo sapiens
H142A site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity Homo sapiens
K307A site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity Homo sapiens
K74A site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity Homo sapiens
L77A site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity Homo sapiens
additional information the substitutions of residues S78, H86 and Q113 only mildly affect RNA binding and catalysis, so they are not essential for CMTr2 MTase activity Homo sapiens
T89A site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity Homo sapiens
W85A site-directed mutagenesis, the mutant shows strongly affected RNA binding and catalytic activity Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA] Homo sapiens
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S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8IYT2 gene CMTR2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(ribonucleotide)-[mRNA]
-
Homo sapiens S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA]
-
?

Subunits

Subunits Comment Organism
More 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 Homo sapiens

Synonyms

Synonyms Comment Organism
AFT
-
Homo sapiens
cap2-MTase
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Homo sapiens
CMTr2
-
Homo sapiens
FLJ11171
-
Homo sapiens
FTSJD1
-
Homo sapiens
hMTr2
-
Homo sapiens

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine cofactor binding by CMTr2 is essential for the binding of RNA, residues K74, L77, W85, T89, K307, H142, and E145 are involved Homo sapiens

General Information

General Information Comment Organism
malfunction the substitutions of residues S78, H86 and Q113 only mildly affect RNA binding and catalysis, so they are not essential for CMTr2 MTase activity Homo sapiens
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 Homo sapiens
additional information structural analysis of human 2'-O-ribose methyltransferases involved in mRNA cap structure formation, homology modeling of the CMTr2 catalytic domain bound to its target using the crystal structure of CMTr1 catalytic domain, overview. 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. Residues K74, L77, W85, T89, K307, H142, and E145 are involved in RNA binding and catalysis, while residues residues S78, H86 and Q113 are not important Homo sapiens