The Enzyme Database

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Accepted name: [50S ribosomal protein L16]-arginine 3-hydroxylase
Reaction: [50S ribosomal protein L16]-L-Arg81 + 2-oxoglutarate + O2 = [50S ribosomal protein L16]-(3R)-3-hydroxy-L-Arg81 + succinate + CO2
Other name(s): ycfD (gene name)
Systematic name: [50S ribosomal protein L16]-L-Arg81,2-oxoglutarate:oxygen oxidoreductase (3R-hydroxylating)
Comments: The enzyme, characterized from the bacterium Escherichia coli, hydroxylates an arginine residue on the 50S ribosomal protein L16, and is involved in regulation of bacterial ribosome assembly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Ge, W., Wolf, A., Feng, T., Ho, C.H., Sekirnik, R., Zayer, A., Granatino, N., Cockman, M.E., Loenarz, C., Loik, N.D., Hardy, A.P., Claridge, T.DW., Hamed, R.B., Chowdhury, R., Gong, L., Robinson, C.V., Trudgian, D.C., Jiang, M., Mackeen, M.M., Mccullagh, J.S., Gordiyenko, Y., Thalhammer, A., Yamamoto, A., Yang, M., Liu-Yi, P., Zhang, Z., Schmidt-Zachmann, M., Kessler, B.M., Ratcliffe, P.J., Preston, G.M., Coleman, M.L. and Schofield, C.J. Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans. Nat. Chem. Biol. 8 (2012) 960–962. [DOI] [PMID: 23103944]
2.  van Staalduinen, L.M., Novakowski, S.K. and 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 (2014) 1898–1910. [DOI] [PMID: 24530688]
[EC created 2014]

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