|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Polynucleotide-Reactions → RNA-Reactions|
EC Number: 22.214.171.124
In Pathway: linezolid resistance
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: 23S rRNA (adenine2503-C8)-methyltransferase
Enzyme Commission Synonyms: Cfr (gene name)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -50.38626 [Latendresse13]
Enzyme Commission Summary:
Contains an [4Fe-4S] cluster [Giessing09]. Cfr is an plasmid-acquired methyltransferase that protects cells from the action of antibiotics [Giessing09]. The enzyme methylates adenosine by a radical mechanism with CH2 from S-adenosyl-L-methionine and retention of the hydrogen at C-8 of adenine2503 of 23S rRNA. It will also methylate 2-methyladenine2503 of 23S rRNA. cf. EC 126.96.36.199 (23S rRNA (adenine2503-C2)-methyltransferase). This enzyme is a member of the 'AdoMet radical ' (radical SAM) family. S-Adenosyl-L-methionine acts as both a radical generator and as the source of the appended methyl group.
Giessing09: Giessing AM, Jensen SS, Rasmussen A, Hansen LH, Gondela A, Long K, Vester B, Kirpekar F (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. PMID: 19144912
Grove11: Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ (2011). "A radically different mechanism for S-adenosylmethionine-dependent methyltransferases." Science 332(6029);604-7. PMID: 21415317
Kaminska10: Kaminska KH, Purta E, Hansen LH, Bujnicki JM, Vester B, Long KS (2010). "Insights into the structure, function and evolution of the radical-SAM 23S rRNA methyltransferase Cfr that confers antibiotic resistance in bacteria." Nucleic Acids Res 38(5);1652-63. PMID: 20007606
Yan10: Yan F, LaMarre JM, Rohrich R, Wiesner J, Jomaa H, Mankin AS, Fujimori DG (2010). "RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA." J Am Chem Soc 132(11);3953-64. PMID: 20184321
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493