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IUBMB Comments Requires iron(II). The enzyme acts on specific lysine residues in its substrates, and is stereo-specific. The enzyme encoded by the human JMJD7 gene acts specifically on two related members of the translation factor family of GTPases, DRG1 and DRG2.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
a [protein]-L-lysine
+
+
=
a [protein]-(3S)-3-hydroxy-L-lysine
+
+
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JmjC domain-containing protein 7
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-
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Jumonji domain-containing protein 7
JMJD7
-
-
-
Jumonji domain-containing protein 7
-
-
-
Jumonji domain-containing protein 7
-
Jumonji domain-containing protein 7
-
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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:oxygen oxidoreductase (3S-hydroxylating)
Requires iron(II). The enzyme acts on specific lysine residues in its substrates, and is stereo-specific. The enzyme encoded by the human JMJD7 gene acts specifically on two related members of the translation factor family of GTPases, DRG1 and DRG2.
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a [protein]-L-lysine + 2-oxoglutarate + O2
a [protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
-
-
?
[protein]-L-lysine + 2-oxoglutarate + O2
[protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
additional information
?
-
[protein]-L-lysine + 2-oxoglutarate + O2
[protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
substrate is Developmentally Regulated GTP Binding Protein 1
-
?
[protein]-L-lysine + 2-oxoglutarate + O2
[protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
substrate is Developmentally Regulated GTP Binding Protein 2
-
?
additional information
?
-
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
?
-
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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a [protein]-L-lysine + 2-oxoglutarate + O2
a [protein]-(3S)-3-hydroxy-L-lysine + succinate + CO2
-
-
-
?
additional information
?
-
enzyme additionally displays slow Fe(II)-stimulated conversion of 2-oxoglutarate to succinate in the absence of a substrate
-
-
?
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Breast Neoplasms
Clipping of arginine-methylated histone tails by JMJD5 and JMJD7.
Neoplasms
The potential underlying mechanism of the leukemia caused by MLL-fusion and potential treatments.
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UniProt
brenda
bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7
UniProt
brenda
bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7
UniProt
brenda
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-
brenda
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brenda
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physiological function
enzyme interacts with Developmentally Regulated GTP Binding Proteins 1 and 2, DRG1/2
physiological function
knockdown of JMJD7 correlates with increased posterior wing compartment size, likely through an increase in cell size
physiological function
the content of arginine methylation of both histones H3R2/H4R3 and overall H3/H4 is increased with the knockout of JMJD7, and the colony-forming abilities of JMJD7-deficient MDA-MB-231 cells are greatly decreased
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JMJD7_HUMAN
316
0
35932
Swiss-Prot
other Location (Reliability: 2 )
JMJD7_MOUSE
316
0
35917
Swiss-Prot
other Location (Reliability: 2 )
Q9VU77_DROME
316
0
36088
TrEMBL
-
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in presence of Mn2+ and 2-oxoglutarate, to 2.2 A resolution. JMJD7 crystallizes as an oligomer with two or four molecules in each asymmetric unit
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H178A
almost complete loss of activity
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Markolovic, S.; Zhuang, Q.; Wilkins, S.E.; Eaton, C.D.; Abboud, M.I.; Katz, M.J.; McNeil, H.E.; Lesniak, R.K.; Hall, C.; Struwe, W.B.; Konietzny, R.; Davis, S.; Yang, M.; Ge, W.; Benesch, J.L.P.; Kessler, B.M.; Ratcliffe, P.J.; Cockman, M.E.; Fischer, R.; Wappner, P.; Chowdhury, R.; Coleman, M.L.; Schofield, C.J.
The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases
Nat. Chem. Biol.
14
688-695
2018
Homo sapiens (P0C870), Drosophila melanogaster (Q9VU77)
brenda
Liu, H.; Wang, C.; Lee, S.; Deng, Y.; Wither, M.; Oh, S.; Ning, F.; Dege, C.; Zhang, Q.; Liu, X.; Johnson, A.M.; Zang, J.; Chen, Z.; Janknecht, R.; Hansen, K.; Marrack, P.; Li, C.Y.; Kappler, J.W.; Hagman, J.; Zhang, G.
Clipping of arginine-methylated histone tails by JMJD5 and JMJD7
Proc. Natl. Acad. Sci. USA
114
E7717-E7726
2017
Mus musculus (P0C872)
brenda
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1.14.11.63 peptidyl-lysine (3S)-dioxygenase
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