Surf Wiki
Save to docs
general/ec-2-1-1

From Surf Wiki (app.surf) — the open knowledge base

16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase

Class of enzymes

Class of enzymes

FieldValue
Name16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase
EC_number2.1.1.182

16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase (, S-adenosylmethionine-6-N',N'-adenosyl (rRNA) dimethyltransferase, KsgA, ksgA methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase. This enzyme catalyses the following chemical reaction

: 4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA \rightleftharpoons 4 Ribosomal RNA + N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA

KsgA introduces the dimethylation of adenine1518 and adenine1519 in 16S rRNA. Strains lacking the methylase are resistant to kasugamycin [1].

References

References

  1. (September 1971). "Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli". Nature.
  2. (January 1972). "Mechanism of kasugamycin resistance in Escherichia coli". Nature.
  3. (1985). "Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA". Gene.
  4. (1994). "Methylation of the conserved A1518-A1519 in Escherichia coli 16S ribosomal RNA by the ksgA methyltransferase is influenced by methylations around the similarly conserved U1512.G1523 base pair in the 3' terminal hairpin". Biochimie.
  5. (May 2004). "Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli". Journal of Molecular Biology.
  6. (September 1979). "Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3' end of 16 S ribosomal RNA of Escherichia coli. III. Purification and properties of the methylating enzyme and methylase-30 S interactions". The Journal of Biological Chemistry.
  7. (May 2009). "Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine". Journal of Molecular Biology.
  8. (March 2009). "Structural basis for binding of RNA and cofactor by a KsgA methyltransferase". Structure.
Info: Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

ec-2.1.1
Want to explore this topic further?

Ask Mako anything about 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase — get instant answers, deeper analysis, and related topics.

Research with Mako

Free with your Surf account

Content sourced from Wikipedia, available under CC BY-SA 4.0.

This content may have been generated or modified by AI. CloudSurf Software LLC is not responsible for the accuracy, completeness, or reliability of AI-generated content. Always verify important information from primary sources.

Report