Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.187 extracted from

  • Bujnicki, J.M.; Blumenthal, R.M.; Rychlewski, L.
    Sequence analysis and structure prediction of 23S rRNA:m1G methyltransferases reveals a conserved core augmented with a putative Zn-binding domain in the N-terminus and family-specific elaborations in the C-terminus (2002), J. Mol. Microbiol. Biotechnol., 4, 93-99.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli P36999
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + guanine745 in 23S rRNA methylated guanines are located in hairpin 35, in domain II of prokaryotic 23S rRNA. RrmA possesses two regions that may be responsible for specific interactions with their target nucleic acid sequences: a putative Zn-finger domain in the N-terminus and the variable domain close to the C-terminus, which indicates that the enzyme exhibits the primary structural organization distinct from other nucleic acid MTases, despite sharing the common catalytic domain Escherichia coli S-adenosyl-L-homocysteine + N1-methylguanine745 in 23S rRNA
-
?

Synonyms

Synonyms Comment Organism
23S rRNA:m1G745 methyltransferase
-
Escherichia coli

General Information

General Information Comment Organism
malfunction mutant lacking N1-methylation of G745 exhibits increased resistance to viomycin in addition to severe defects of growth characteristics Escherichia coli