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1.14.11.47: [50S ribosomal protein L16]-arginine 3-hydroxylase

This is an abbreviated version!
For detailed information about [50S ribosomal protein L16]-arginine 3-hydroxylase, go to the full flat file.

Reaction

[50S ribosomal protein L16]-L-Arg81
+
2-oxoglutarate
+
O2
=
[50S ribosomal protein L16]-(3R)-3-hydroxy-L-Arg81
+
succinate
+
CO2

Synonyms

50S ribosomal protein L16 arginine hydroxylase, ycfD

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.47 [50S ribosomal protein L16]-arginine 3-hydroxylase

Reference

Reference on EC 1.14.11.47 - [50S ribosomal protein L16]-arginine 3-hydroxylase

Please use the Reference Search for a specific query.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van Staalduinen, L.; Novakowski, S.; Jia, Z.
Structure and functional analysis of YcfD, a novel 2-oxoglutarate/Fe2+-dependent oxygenase involved in translational regulation in Escherichia coli
J. Mol. Biol.
426
1898-1910
2014
Escherichia coli (P27431)
Manually annotated by BRENDA team
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
Nat. Chem. Biol.
8
960-962
2012
Escherichia coli (P27431)
Manually annotated by BRENDA team
Chowdhury, R.; Sekirnik, R.; Brissett, N.; Krojer, T.; Ho, C.; Ng, S.; Clifton, I.; Ge, W.; Kershaw, N.; Fox, G.; Muniz, J.; Vollmar, M.; Phillips, C.; Pilka, E.; Kavanagh, K.; von Delft, F.; Oppermann, U.; McDonough, M.; Doherty, A.; Schofield, C.
Ribosomal oxygenases are structurally conserved from prokaryotes to humans
Nature
510
422-426
2014
Escherichia coli (P27431)
Manually annotated by BRENDA team
van Staalduinen, L.M.; Jia, Z.
Post-translational hydroxylation by 2OG/Fe(II)-dependent oxygenases as a novel regulatory mechanism in bacteria
Front. Microbiol.
5
798
2014
Escherichia coli (P27431)
Manually annotated by BRENDA team
Sekirnik, R.; Wilkins, S.; Bush, J.; Tarhonskaya, H.; Münzel, M.; Hussein, A.; Flashman, E.; Mohammed, S.; McDonough, M.; Loenarz, C.; Schofield, C.
YcfDRM is a thermophilic oxygen-dependent ribosomal protein uL16 oxygenase
Extremophiles
22
553-562
2018
Rhodothermus marinus, Rhodothermus marinus DSM 4252
Manually annotated by BRENDA team