RIOX2Fe2+ hydroxylates a histidine residue of RPL27A

Stable Identifier
R-HSA-9630967
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
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Nuclear RIOX2 (Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA) 3-hydroxylates histidine 39 of RPL27A (60S ribosomal protein L27a) (Ge et al. 2012). The oligomerization state of RIOX2 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

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

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

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

BMC Evol. Biol. 2018
Participants
Participates
Catalyst Activity

peptidyl-histidine dioxygenase activity of RIOX2:Fe2+ [nucleoplasm]

Orthologous Events
Authored
Created
Cite Us!