Biology:23S rRNA (guanine2535-N1)-methyltransferase

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Short description: Class of enzymes
23S rRNA (guanine2535-N1)-methyltransferase
Identifiers
EC number2.1.1.209
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

23S rRNA (guanine2535-N1)-methyltransferase (EC 2.1.1.209, AviRa) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine2535-N1)-methyltransferase.[1][2][3] This enzyme catalyses the following chemical reaction

S-adenosyl-L-methionine + guanine2535 in 23S rRNA [math]\displaystyle{ \rightleftharpoons }[/math] S-adenosyl-L-homocysteine + N1-methylguanine2535 in 23S rRNA

This is one of the methyltransferases from Streptomyces viridochromogenes . Streptomyces viridochromogenes produces the antibiotic avilamycin A which binds to the 50S ribosomal subunit to inhibit protein synthesis.[4]

References

  1. "The avilamycin resistance determinants AviRa and AviRb methylate 23S rRNA at the guanosine 2535 base and the uridine 2479 ribose". Molecular Microbiology 49 (2): 309–18. July 2003. doi:10.1046/j.1365-2958.2003.03558.x. PMID 12828631. 
  2. "An ATP-binding cassette transporter and two rRNA methyltransferases are involved in resistance to avilamycin in the producer organism Streptomyces viridochromogenes Tü57". Antimicrobial Agents and Chemotherapy 45 (3): 690–5. March 2001. doi:10.1128/aac.45.3.690-695.2001. PMID 11181344. 
  3. "Crystal structure of the avilamycin resistance-conferring methyltransferase AviRa from Streptomyces viridochromogenes". Journal of Molecular Biology 329 (1): 147–57. May 2003. doi:10.1016/s0022-2836(03)00407-8. PMID 12742024. 
  4. "Avilamycin and evernimicin induce structural changes in rProteins uL16 and CTC that enhance the inhibition of A-site tRNA binding". Proceedings of the National Academy of Sciences of the United States of America 113 (44): E6796–E6805. November 2016. doi:10.1073/pnas.1614297113. PMID 27791159. 

External links