RIOX1:Fe2+ hydroxylates a histidine residue of RPL8

Stable Identifier
R-HSA-9630993
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
2-oxoglutarate + L-histidyl-(protein) + O2 => (3S)-3-hydroxy-L-histidyl-(protein) + CO2 + succinate
ReviewStatus
3/5
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Nuclear RIOX1 (Ribosomal oxygenase NO66) 3-hydroxylates histidine 216 of RPL8 (60S ribosomal protein L8) (Ge et al. 2012). The oligomerization state of RIOX1 in vivo is unknown; it is annotated here as a monomer complexed with one Fe2+ ion (Brauer et al. 2018).
Literature References
PubMed ID Title Journal Year
23103944 Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

Liu-Yi, P, Sekirnik, R, Wolf, A, Robinson, CV, Loenarz, C, Preston, GM, Zhang, Z, Yamamoto, A, Hamed, RB, Mccullagh, JS, Kessler, BM, Thalhammer, A, Mackeen, MM, Ho, CH, Jiang, M, Ratcliffe, PJ, Schofield, CJ, Trudgian, DC, Hardy, AP, Loik, ND, Zayer, A, Coleman, ML, Gong, L, Feng, T, Schmidt-Zachmann, M, Claridge, TDW, Gordiyenko, Y, Ge, W, Yang, M, Chowdhury, R, Cockman, ME, Granatino, N

Nat. Chem. Biol. 2012
29914368 Phylogenetic and genomic analyses of the ribosomal oxygenases Riox1 (No66) and Riox2 (Mina53) provide new insights into their evolution

Lengeling, A, Brockers, K, Wolf, A, Feuchtinger, A, Wollscheid-Lengeling, E, Moneer, J, Bräuer, KE

BMC Evol. Biol. 2018
Participants
Participates
Event Information
Catalyst Activity

peptidyl-histidine dioxygenase activity of RIOX1:Fe2+ [nucleoplasm]

Orthologous Events
Authored
Created
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