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Literature summary for 1.14.11.73 extracted from

  • Wilkins, S.E.; Islam, M.S.; Gannon, J.M.; Markolovic, S.; Hopkinson, R.J.; Ge, W.; Schofield, C.J.; Chowdhury, R.
    JMJD5 is a human arginyl C-3 hydroxylase (2018), Nat. Commun., 9, 1180 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.73

Crystallization (Commentary)

Crystallization (Comment) Organism
structures of N-terminally truncated (aa 153-416 and aa 183-416) constructs and in complex with substrate RPS6. The JMJD5 active site contains a metal centre, which is octahedrally coordinated by an HXD..H motif, the 2-oxoglutarate oxalyl group and a water molecule, which is likely replaced by a dioxygen during catalysis Homo sapiens

Protein Variants

Protein Variants Comment Organism
H321A substitution of Fe2+-binding residue, significantly reduces 2-oxoglutarate turnover Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
N-oxalylglycine
-
 Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q8N371
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information JMJD5 catalyses stereoselective C-3 hydroxylation of arginine residues in sequences from human regulator of chromosome condensation domain-containing protein 1 (RCCD1) and ribosomal protein S6 (RPS6) Homo sapiens ?
-
-
[RCCD1]-L-arginine + 2-oxoglutarate + O2 substrate i.e. regulator of chromosome condensation domain-containing protein 1 Homo sapiens [RCCD1]-(3R)-3-hydroxy-L-arginine + succinate + CO2
-
 ?
[RPS6]-L-arginine + 2-oxoglutarate + O2 substrate i.e. ribosomal protein S6 Homo sapiens [RPS6]-(3R)-3-hydroxy-L-arginine + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
JMJD5
-
 Homo sapiens
KDM8
-
 Homo sapiens