The Enzyme Database

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EC 2.1.1.296     
Accepted name: methyltransferase cap2
Reaction: 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]
Other name(s): MTR2; cap2-MTase; mRNA (nucleoside-2′-O)-methyltransferase (ambiguous)
Systematic name: S-adenosyl-L-methionine:5′-(N7-methyl 5′-triphosphoguanosine)-(2′-O-methyl-purine-ribonucleotide)-ribonucleotide-[mRNA] 2′-O-methyltransferase
Comments: 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].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Arhin, G.K., Ullu, E. and Tschudi, C. 2′-O-methylation of position 2 of the trypanosome spliced leader cap 4 is mediated by a 48 kDa protein related to vaccinia virus VP39. Mol. Biochem. Parasitol. 147 (2006) 137–139. [PMID: 16516986]
2.  Werner, M., Purta, E., Kaminska, K.H., Cymerman, I.A., Campbell, D.A., Mittra, B., Zamudio, J.R., Sturm, N.R., Jaworski, J. and Bujnicki, J.M. 2′-O-ribose methylation of cap2 in human: function and evolution in a horizontally mobile family. Nucleic Acids Res. 39 (2011) 4756–4768. [PMID: 21310715]
[EC 2.1.1.296 created 2014]
 
 


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