EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.14.11.63 | a [protein]-L-lysine + 2-oxoglutarate + O2 |
- |
Drosophila melanogaster |
a [protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2 |
- |
? |
1.14.11.63 | more |
enzyme additionally displays slow Fe(II)-stimulated conversion of 2-oxoglutarate to succinate in the absence of a substrate |
Drosophila melanogaster |
? |
- |
? |
1.14.11.63 | more |
enzyme additionally displays slow Fe(II)-stimulated conversion of 2-oxoglutarate to succinate in the absence of a substrate |
Homo sapiens |
? |
- |
? |
1.14.11.63 | more |
JMJD7 has divalent cation-dependent protease activities that preferentially cleave the tails of histones 2, 3, or 4 containing methylated arginines. After the initial specific cleavage, JMJD7, acting as aminopeptidase, progressively digests the C-terminal products |
Mus musculus |
? |
- |
? |
1.14.11.63 | [protein]-L-lysine + 2-oxoglutarate + O2 |
substrate is Developmentally Regulated GTP Binding Protein 1 |
Homo sapiens |
[protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2 |
- |
? |
1.14.11.63 | [protein]-L-lysine + 2-oxoglutarate + O2 |
substrate is Developmentally Regulated GTP Binding Protein 2 |
Homo sapiens |
[protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2 |
- |
? |