| 23S rRNA (adenine2503-C8)-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.224 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
23S rRNA (adenine2503-C8)-methyltransferase ( EC 2.1.1.224, Cfr (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C8)-methyltransferase. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction
- 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA S-adenosyl-L-homocysteine + L- methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
This enzyme is a member of the 'AdoMet radical' (radical SAM) family.
References
- ^ Giessing AM, Jensen SS, Rasmussen A, Hansen LH, Gondela A, Long K, Vester B, Kirpekar F (February 2009). "Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria". RNA. 15 (2): 327–36. doi: 10.1261/rna.1371409. PMC 2648713. PMID 19144912.
- ^ Kaminska KH, Purta E, Hansen LH, Bujnicki JM, Vester B, Long KS (March 2010). "Insights into the structure, function and evolution of the radical-SAM 23S rRNA methyltransferase Cfr that confers antibiotic resistance in bacteria". Nucleic Acids Research. 38 (5): 1652–63. doi: 10.1093/nar/gkp1142. PMC 2836569. PMID 20007606.
- ^ Yan F, LaMarre JM, Röhrich R, Wiesner J, Jomaa H, Mankin AS, Fujimori DG (March 2010). "RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA". Journal of the American Chemical Society. 132 (11): 3953–64. doi: 10.1021/ja910850y. PMC 2859901. PMID 20184321.
- ^ Yan F, Fujimori DG (March 2011). "RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift". Proceedings of the National Academy of Sciences of the United States of America. 108 (10): 3930–4. Bibcode: 2011PNAS..108.3930Y. doi: 10.1073/pnas.1017781108. PMC 3054002. PMID 21368151.
- ^ Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ (April 2011). "A radically different mechanism for S-adenosylmethionine-dependent methyltransferases". Science. 332 (6029): 604–7. Bibcode: 2011Sci...332..604G. doi: 10.1126/science.1200877. PMID 21415317. S2CID 2214309.
- ^ Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC (May 2011). "Structural basis for methyl transfer by a radical SAM enzyme". Science. 332 (6033): 1089–92. Bibcode: 2011Sci...332.1089B. doi: 10.1126/science.1205358. PMC 3506250. PMID 21527678.
External links
- 23S+rRNA+(adenine2503-C8)-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| 23S rRNA (adenine2503-C8)-methyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.1.1.224 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
23S rRNA (adenine2503-C8)-methyltransferase ( EC 2.1.1.224, Cfr (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C8)-methyltransferase. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction
- 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA S-adenosyl-L-homocysteine + L- methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA
This enzyme is a member of the 'AdoMet radical' (radical SAM) family.
References
- ^ Giessing AM, Jensen SS, Rasmussen A, Hansen LH, Gondela A, Long K, Vester B, Kirpekar F (February 2009). "Identification of 8-methyladenosine as the modification catalyzed by the radical SAM methyltransferase Cfr that confers antibiotic resistance in bacteria". RNA. 15 (2): 327–36. doi: 10.1261/rna.1371409. PMC 2648713. PMID 19144912.
- ^ Kaminska KH, Purta E, Hansen LH, Bujnicki JM, Vester B, Long KS (March 2010). "Insights into the structure, function and evolution of the radical-SAM 23S rRNA methyltransferase Cfr that confers antibiotic resistance in bacteria". Nucleic Acids Research. 38 (5): 1652–63. doi: 10.1093/nar/gkp1142. PMC 2836569. PMID 20007606.
- ^ Yan F, LaMarre JM, Röhrich R, Wiesner J, Jomaa H, Mankin AS, Fujimori DG (March 2010). "RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA". Journal of the American Chemical Society. 132 (11): 3953–64. doi: 10.1021/ja910850y. PMC 2859901. PMID 20184321.
- ^ Yan F, Fujimori DG (March 2011). "RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift". Proceedings of the National Academy of Sciences of the United States of America. 108 (10): 3930–4. Bibcode: 2011PNAS..108.3930Y. doi: 10.1073/pnas.1017781108. PMC 3054002. PMID 21368151.
- ^ Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ (April 2011). "A radically different mechanism for S-adenosylmethionine-dependent methyltransferases". Science. 332 (6029): 604–7. Bibcode: 2011Sci...332..604G. doi: 10.1126/science.1200877. PMID 21415317. S2CID 2214309.
- ^ Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC (May 2011). "Structural basis for methyl transfer by a radical SAM enzyme". Science. 332 (6033): 1089–92. Bibcode: 2011Sci...332.1089B. doi: 10.1126/science.1205358. PMC 3506250. PMID 21527678.
External links
- 23S+rRNA+(adenine2503-C8)-methyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)