1.14.11.73: [protein]-arginine 3-hydroxylase
This is an abbreviated version!
For detailed information about [protein]-arginine 3-hydroxylase, go to the full flat file.
Reaction
Synonyms
JMJD5, KDM8
ECTree
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General Information
General Information on EC 1.14.11.73 - [protein]-arginine 3-hydroxylase
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physiological function
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
physiological function
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