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Literature summary for 2.1.1.226 extracted from

  • Monshupanee, T.
    Increased bacterial hemolytic activity is conferred by expression of TlyA methyltransferase but not by its 2'-O-methylation of the ribosome (2013), Curr. Microbiol., 67, 61-68.
    View publication on PubMed
Search for more literature for 2.1.1.226

Cloned(Commentary)

Cloned (Comment) Organism
gene tlyA, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mycobacterium tuberculosis the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA ?
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 ?
additional information Mycobacterium tuberculosis H37Rv the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA ?
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 ?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA Mycobacterium tuberculosis
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 S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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 ?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA Mycobacterium tuberculosis H37Rv
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 S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
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 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WJ63 gene tlyA
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Mycobacterium tuberculosis H37Rv P9WJ63 gene tlyA
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Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminally His-tagged enzyme from Escherichia coli Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA Mycobacterium tuberculosis ?
-
 ?
additional information the purified recombinant enzyme TlyA efficiently 2'-O-methylates C1920 in vitro at a molar enzyme to substrate ratio of 1:10 Mycobacterium tuberculosis ?
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 ?
additional information the 2'-O-methyltransferase TlyA from Mycobacterium tuberculosis methylates both nucleotide C1409 of 16S rRNA, EC 2.1.1.227, and C1920 of 23S rRNA Mycobacterium tuberculosis H37Rv ?
-
 ?
additional information the purified recombinant enzyme TlyA efficiently 2'-O-methylates C1920 in vitro at a molar enzyme to substrate ratio of 1:10 Mycobacterium tuberculosis H37Rv ?
-
 ?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
-
 Mycobacterium tuberculosis S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
 ?
S-adenosyl-L-methionine + cytidine1920 in 23S rRNA
-
 Mycobacterium tuberculosis H37Rv S-adenosyl-L-homocysteine + 2'-O-methylcytidine1920 in 23S rRNA
-
 ?

Synonyms

Synonyms Comment Organism
2'-O-methyltransferase
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 Mycobacterium tuberculosis
TlyA
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 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
additional information the S4-type RNA recognition domain (residues 5-64), S-adenosyl-methionine binding domain (residues 84-153), SAM-interacting residues (residues 90-94), and four catalytic residues (K69-D154-K182-E238) are conserved in 2'-O-methyltrasferases TlyA Mycobacterium tuberculosis
physiological function bacterial 2'-O-methyltransferase TlyA methylates either both nucleotide C1409 of 16S rRNA and C1920 of 23S rRNA. Both ribosomal methylations increase bacterial susceptibility to ribosome targeting antibiotics capreomycin and viomycin. The enzyme also function as a hemolysin, but increased bacterial hemolytic function is not likely a consequence of TlyA-mediated methylations of the ribosome Mycobacterium tuberculosis