Cloned (Comment) | Organism |
---|---|
gene CMTR2, recombinant overexpression of wild-type and mutant enzymes in HEK-293 cells | Homo sapiens |
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 | 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 | - |
S-adenosyl-L-homocysteine + a 5'-(N7-methyl 5'-triphosphoguanosine)-(2'-O-methyl-purine-ribonucleotide)-(2'-O-methyl-ribonucleotide)-[mRNA] | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q8IYT2 | gene CMTR2 | - |
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 | 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 | Comment | Organism |
---|---|---|
AFT | - |
Homo sapiens |
cap2-MTase | - |
Homo sapiens |
CMTr2 | - |
Homo sapiens |
FLJ11171 | - |
Homo sapiens |
FTSJD1 | - |
Homo sapiens |
hMTr2 | - |
Homo sapiens |
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 | 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 |