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Literature summary for 1.14.11.47 extracted from

  • Ge, W.; Wolf, A.; Feng, T.; Ho, C.; Sekirnik, R.; Zayer, A.; Granatino, N.; Cockman, M.; Loenarz, C.; Loik, N.; Hardy, A.; Claridge, T.; Hamed, R.; Chowdhury, R.; Gong, L.; Robinson, C.; Trudgian, D.; Jiang, M.; MacKeen, M.; McCullagh, J.; Gordiyenko, Y.;
    Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans (2012), Nat. Chem. Biol., 8, 960-962.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.47

Organism

Organism UniProt Comment Textmining
Escherichia coli P27431
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AVSEATIR + 2-oxoglutarate + O2
-
 Escherichia coli [AVSEATIR]-(3R)-3-hydroxy-L-Arg8 + succinate + CO2
-
 ?
KPITEKPLAVRMGKGKGNVE + 2-oxoglutarate + O2 peptide derived from 50S ribosomal protein L16 Escherichia coli [KPITEKPLAVRMGKGKGNVE]-(3R)-3-hydroxy-L-Arg11 + succinate + CO2
-
 ?
additional information of the tested peptides, six or more residues are required for efficient hydroxylation. Hydroxylation is ablated when the C-terminus is extended to more closely resemble a protein. Hydroxylation occurs with incorporation of more than 90% 18O from 18O2 and occurs at C-3 of arginine leaing to a stereochemistry of the hydroxylated arginine of 2S,3R Escherichia coli ?
-
 ?
RLLPAVSEATIRRL + 2-oxoglutarate + O2
-
 Escherichia coli [RLLPAVSEATIRRL]-(3R)-3-hydroxy-L-Arg12 + succinate + CO2 modification occurs at the arginine at the -3 position relative to the C-terminus ?
[50S ribosomal protein L16]-L-Arg81 + 2-oxoglutarate + O2
-
 Escherichia coli [50S ribosomal protein L16]-(3R)-3-hydroxy-L-Arg81 + succinate + CO2 more than 95% hydoxylation, residue Arg81 is the only residue observed to be hydroxylated ?

Synonyms

Synonyms Comment Organism
ycfD
-
 Escherichia coli