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.
The enzyme appears in viruses and cellular organisms
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.
Substrates: 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) Products: -
JMJD5 has divalent cation-dependent protease activities that preferentially cleave the tails of histones 2, 3, or 4 containing methylated arginines, e.g. reaction of EC 1.14.11.27. After the initial specific cleavage, JMJD5 acting as aminopeptidase, progressively digests the C-terminal products. JMJD5-deficient fibroblasts exhibit dramatically increased levels of methylated arginines and histones
JMJD5 and JMJD7, EC 1.14.11.73, function as endopeptidases that cleave histone tails specifically adjacent to methylated arginine residues and continue to degrade N-terminal residues of histones via their aminopeptidase activity. Recognition between the enzymes and histone substrates is specific. JMJD5 and JMJD7 show high structural similarity, share common substrates and high binding affinity. JMJD5 does not bind to arginine methylated histone tails with additional lysine acetylation while JMJD7 does not bind to arginine methylated histone tails with additional lysine methylation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
the complex structures of JMJD5 and arginine derivatives reveals a Tudor domain-like binding pocket to accommodate the methylated sidechain of arginine, but not lysine
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