1.14.11.63: peptidyl-lysine (3S)-dioxygenase
This is an abbreviated version!
For detailed information about peptidyl-lysine (3S)-dioxygenase, go to the full flat file.
Word Map on EC 1.14.11.63
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1.14.11.63
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histone
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demethylases
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trafac
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jumonji-c
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jarid2
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prdm10
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hif1an
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clipping
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gametogenesis
- 1.14.11.63
- histone
- demethylases
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trafac
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jumonji-c
- jarid2
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prdm10
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hif1an
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clipping
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gametogenesis
Reaction
Synonyms
JmjC domain-containing protein 7, JMJD7, Jumonji domain-containing protein 7
ECTree
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Substrates Products
Substrates Products on EC 1.14.11.63 - peptidyl-lysine (3S)-dioxygenase
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REACTION DIAGRAM
a [protein]-L-lysine + 2-oxoglutarate + O2
a [protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
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[protein]-L-lysine + 2-oxoglutarate + O2
[protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
[protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
substrate is Developmentally Regulated GTP Binding Protein 1
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[protein]-L-lysine + 2-oxoglutarate + O2
[protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
substrate is Developmentally Regulated GTP Binding Protein 2
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enzyme additionally displays slow Fe(II)-stimulated conversion of 2-oxoglutarate to succinate in the absence of a substrate
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additional information
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enzyme additionally displays slow Fe(II)-stimulated conversion of 2-oxoglutarate to succinate in the absence of a substrate
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additional information
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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
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