| 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, PDB |
| 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] |
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| [EC 1.14.11.73 created 2020] |
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