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Literature summary for 2.1.1.172 extracted from

  • Bujnicki, J.M.
    Rychlewski. L.: RNA:(guanine-N2) methyltransferases RsmC/RsmD and their homologs revisited--bioinformatic analysis and prediction of the active site based on the uncharacterized Mj0882 protein structure (2002), BMC Bioinformatics, 3, 10.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli P39406
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + guanine1207 in 16S rRNA
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Escherichia coli S-adenosyl-L-homocysteine + N2-methylguanine1207 in 16S rRNA
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?

Subunits

Subunits Comment Organism
dimer based on a comprehensive bioinformatic analysis of m2G methyltransferases it is inferred that the prokaryotic RsmC and RsmD methyltransferases are pseudodimers. The C-terminal catalytic domain is closely related to the structurally characterized Mj0882 protein, while the N-terminal domain lacks the cofactor-binding and catalytic side-chains Escherichia coli

Synonyms

Synonyms Comment Organism
RNA:(guanine-N2) methyltransferase RsmC
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Escherichia coli