The Enzyme Database

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EC 1.14.11.73     
Accepted name: [protein]-arginine 3-hydroxylase
Reaction: [protein]-L-arginine + 2-oxoglutarate + O2 = [protein]-(3R)-3-hydroxy-L-arginine + succinate + CO2
Other name(s): JMJD5 (gene name)
Systematic name: [protein]-L-arginine,2-oxoglutarate:oxygen oxidoreductase (3R-hydroxylating)
Comments: The enzyme, characterized from humans, catalyses the stereoselective formation of the (2S,3R)-hydroxy-L-arginine stereoisomer. So far the enzyme has been shown to act on two substrates - the 40S ribosomal protein S6 (RPS6), which is hydroxylated at R137, and, at a lower activity, RCCD1, a protein involved in chromatin stability, which is hydroxylated at R141. Even though the same stereoisomer is produced by the bacterial EC 1.14.11.47, [50S ribosomal protein L16]-arginine 3-hydroxylase, the two enzymes do not exhibit any cross-reactivity on their respective ribosomal protein substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Wilkins, S.E., Islam, M.S., Gannon, J.M., Markolovic, S., Hopkinson, R.J., Ge, W., Schofield, C.J. and Chowdhury, R. JMJD5 is a human arginyl C-3 hydroxylase. Nat. Commun. 9:1180 (2018). [PMID: 29563586]
[EC 1.14.11.73 created 2020]
 
 


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