Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 2.1.1.224

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Macromolecule Reactions Polynucleotide-Reactions RNA-Reactions

EC Number: 2.1.1.224

Enzymes and Genes:
23S rRNA (adenine2503-C8)-methyltransferase Inferred from experiment : cfr ( Staphylococcus sciuri )

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 Inferred by computational analysis [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 2.1.1.192 (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.

Citations: [Kaminska10, Yan10, Yan11a, Grove11, Boal11]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.1.1.224 , ENZYME:EC:2.1.1.224 , IUBMB-ExplorEnz:EC:2.1.1.224

Credits:
Created 20-Jun-2011 by Kothari A , SRI International


References

Boal11: Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC (2011). "Structural basis for methyl transfer by a radical SAM enzyme." Science 332(6033);1089-92. PMID: 21527678

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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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

Yan11a: Yan F, Fujimori DG (2011). "RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift." Proc Natl Acad Sci U S A 108(10);3930-4. PMID: 21368151


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, BIOCYC13A.