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Escherichia coli K-12 substr. MG1655 Reaction: 2.1.1.182

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

EC Number: 2.1.1.182

Enzymes and Genes:
16S rRNA m62A1518,m62A1519 dimethyltransferase Inferred from experiment : rsmA

Supersedes EC number: 2.1.1.48

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

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: 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase

Enzyme Commission Synonyms: S-adenosylmethionine-6-N',N'-adenosyl (rRNA) dimethyltransferase, KsgA, ksgA methyltransferase

Enzyme Commission Summary:
KsgA introduces the most highly conserved ribosomal RNA modification, the dimethylation of adenine1518 and adenine1519 in 16S rRNA. Strains lacking the methylase are resistant to kasugamycin [Helser71].

Citations: [Helser72, vanBuul85, Formenoy94, OFarrell04, Poldermans79, Demirci09, Tu09]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:2.1.1.182 , ENZYME:EC:2.1.1.182 , IUBMB-ExplorEnz:EC:2.1.1.182

Credits:
Created 23-Aug-2010 by Kothari A , SRI International


References

Demirci09: Demirci H, Belardinelli R, Seri E, Gregory ST, Gualerzi C, Dahlberg AE, Jogl G (2009). "Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine." J Mol Biol 388(2);271-82. PMID: 19285505

Formenoy94: Formenoy LJ, Cunningham PR, Nurse K, Pleij CW, Ofengand J (1994). "Methylation of the conserved A1518-A1519 in Escherichia coli 16S ribosomal RNA by the ksgA methyltransferase is influenced by methylations around the similarly conserved U1512.G1523 base pair in the 3' terminal hairpin." Biochimie 76(12);1123-8. PMID: 7538324

Helser71: Helser TL, Davies JE, Dahlberg JE (1971). "Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli." Nat New Biol 233(35);12-4. PMID: 4329247

Helser72: Helser TL, Davies JE, Dahlberg JE (1972). "Mechanism of kasugamycin resistance in Escherichia coli." Nat New Biol 235(53);6-9. PMID: 4336392

OFarrell04: O'Farrell HC, Scarsdale JN, Rife JP (2004). "Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli." J Mol Biol 339(2);337-53. PMID: 15136037

Poldermans79: Poldermans B, Roza L, Van Knippenberg PH (1979). "Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3' end of 16 S ribosomal RNA of Escherichia coli. III. Purification and properties of the methylating enzyme and methylase-30 S interactions." J Biol Chem 254(18);9094-100. PMID: 383712

Tu09: Tu C, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X (2009). "Structural basis for binding of RNA and cofactor by a KsgA methyltransferase." Structure 17(3);374-85. PMID: 19278652

vanBuul85: van Buul CP, van Knippenberg PH (1985). "Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA." Gene 38(1-3);65-72. PMID: 3905517


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 19.0 on Thu Sep 3, 2015, biocyc12.