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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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Escherichia coli K-12 substr. MG1655 Reaction: 2.8.4.4

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 2.8.4.4

Enzymes and Genes:
ribosomal protein S12 D88 methylthiotransferase Inferred from experiment : rimO

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: The left side is missing: H: 1

Enzyme Commission Primary Name: [ribosomal protein S12] (aspartate89-C3)-methylthiotransferase

Enzyme Commission Synonyms: RimO

Enzyme Commission Summary:
This bacterial enzyme binds two [4Fe-4S] clusters [Lee09, Arragain10]. A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters [Forouhar13]. In the first reaction the enzyme transfers a methyl group from SAM to the external sulfur ion of the sulfur bridge. In the second reaction the enzyme catalyses the reductive fragmentation of a second molecule of SAM, yielding a 5'-deoxyadenosyl radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylthiol group to aspartate89 [Landgraf13, Forouhar13]. The enzyme is a member of the superfamily of S-adenosyl-L-methionine-dependent radical (radical AdoMet) enzymes.

Citations: [Anton08, Strader11]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:2.8.4.4 , ENZYME:EC:2.8.4.4 , IUBMB-ExplorEnz:EC:2.8.4.4

Credits:
Created 13-Nov-2009 by Keseler I , SRI International
Revised 07-Jun-2013 by Caspi R , SRI International


References

Anton08: Anton BP, Saleh L, Benner JS, Raleigh EA, Kasif S, Roberts RJ (2008). "RimO, a MiaB-like enzyme, methylthiolates the universally conserved Asp88 residue of ribosomal protein S12 in Escherichia coli." Proc Natl Acad Sci U S A 105(6);1826-31. PMID: 18252828

Arragain10: Arragain S, Garcia-Serres R, Blondin G, Douki T, Clemancey M, Latour JM, Forouhar F, Neely H, Montelione GT, Hunt JF, Mulliez E, Fontecave M, Atta M (2010). "Post-translational modification of ribosomal proteins: structural and functional characterization of RimO from Thermotoga maritima, a radical S-adenosylmethionine methylthiotransferase." J Biol Chem 285(8);5792-801. PMID: 20007320

Forouhar13: Forouhar F, Arragain S, Atta M, Gambarelli S, Mouesca JM, Hussain M, Xiao R, Kieffer-Jaquinod S, Seetharaman J, Acton TB, Montelione GT, Mulliez E, Hunt JF, Fontecave M (2013). "Two Fe-S clusters catalyze sulfur insertion by radical-SAM methylthiotransferases." Nat Chem Biol 9(5);333-8. PMID: 23542644

Landgraf13: Landgraf BJ, Arcinas AJ, Lee KH, Booker SJ (2013). "Identification of an intermediate methyl carrier in the radical S-adenosylmethionine methylthiotransferases RimO and MiaB." J Am Chem Soc 135(41);15404-16. PMID: 23991893

Lee09: Lee KH, Saleh L, Anton BP, Madinger CL, Benner JS, Iwig DF, Roberts RJ, Krebs C, Booker SJ (2009). "Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily." Biochemistry 48(42);10162-74. PMID: 19736993

Strader11: Strader MB, Costantino N, Elkins CA, Chen CY, Patel I, Makusky AJ, Choy JS, Court DL, Markey SP, Kowalak JA (2011). "A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein S12." Mol Cell Proteomics 10(3);M110.005199. PMID: 21169565


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, BIOCYC13A.