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Literature summary extracted from

  • Moon, H.J.; Redman, K.L.
    Trm4 and Nsun2 RNA:m5C methyltransferases form metabolite-dependent, covalent adducts with previously methylated RNA (2014), Biochemistry, 53, 7132-7144.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.202 additional information Saccharomyces cerevisiae the enzyme Trm4 fabricate 5-methylcytosine (m5C) in RNA molecules utilizing a dual-cysteine catalytic mechanism ?
-
 ?
2.1.1.203 additional information Mammalia the Nsun2 fabricate 5-methylcytosine (m5C) in RNA molecules utilizing a dual-cysteine catalytic mechanism ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.202 Saccharomyces cerevisiae
-
 gene Trm4
-
2.1.1.203 Mammalia
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.202 additional information the enzyme Trm4 fabricate 5-methylcytosine (m5C) in RNA molecules utilizing a dual-cysteine catalytic mechanism Saccharomyces cerevisiae ?
-
 ?
2.1.1.202 additional information the enzyme forms covalent complexes with previously methylated RNA requiring S-adenosyl-L-homocysteine, the removal of this metabolite results in the disassembly of preexisting complexes Saccharomyces cerevisiae ?
-
 ?
2.1.1.203 additional information the Nsun2 fabricate 5-methylcytosine (m5C) in RNA molecules utilizing a dual-cysteine catalytic mechanism Mammalia ?
-
 ?
2.1.1.203 additional information the enzyme forms covalent complexes with previously methylated RNA requiring S-adenosyl-L-homocysteine, the removal of this metabolite results in the disassembly of preexisting complexes Mammalia ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.202 RNA:m5C methyltransferase
-
 Saccharomyces cerevisiae
2.1.1.202 Trm4p
-
 Saccharomyces cerevisiae
2.1.1.203 NSUN2
-
 Mammalia
2.1.1.203 RNA:m5C methyltransferase
-
 Mammalia

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.202 5.5 6.5 maximal formation of Trm4p-RNA complexes observed in the pH range of 5.5-6.5 Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.202 S-adenosyl-L-methionine
-
 Saccharomyces cerevisiae
2.1.1.203 S-adenosyl-L-methionine
-
 Mammalia

General Information

EC Number General Information Comment Organism
2.1.1.202 metabolism formation of a covalent complex between dual-cysteine RNA:m5C methyltransferases and methylated RNA provides a unique means by which metabolic factors can influence RNA. By controlling the degree of formation of the enzyme-RNA covalent complex, S-adenosyl-L-homocysteine and pH are likely to influence the extent of m5C formation and the rate of release of methylated RNA from RNA:m5C methyltransferases. Metabolite-induced covalent complexes could plausibly affect the processing and function of m5C-containing RNAs Saccharomyces cerevisiae
2.1.1.202 additional information four active-site residues critical for Trm4p-mediated tRNA methylation are also required for the formation of the denaturant-resistant complexes with m5C-containing RNA Saccharomyces cerevisiae
2.1.1.203 metabolism formation of a covalent complex between dual-cysteine RNA:m5C methyltransferases and methylated RNA provides a unique means by which metabolic factors can influence RNA. By controlling the degree of formation of the enzyme-RNA covalent complex, S-adenosyl-L-homocysteine and pH are likely to influence the extent of m5C formation and the rate of release of methylated RNA from RNA:m5C methyltransferases. Metabolite-induced covalent complexes could plausibly affect the processing and function of m5C-containing RNAs Mammalia
2.1.1.203 additional information four active-site residues critical for Nsun2-mediated tRNA methylation are also required for the formation of the denaturant-resistant complexes with m5C-containing RNA Mammalia