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1.14.11.66: [histone H3]-trimethyl-L-lysine9 demethylase

This is an abbreviated version!
For detailed information about [histone H3]-trimethyl-L-lysine9 demethylase, go to the full flat file.

Word Map on EC 1.14.11.66

Reaction

a [histone H3]-N6,N6,N6-trimethyl-L-lysine9
+ 2 2-oxoglutarate + 2 O2 =
a [histone H3]-N6-methyl-L-lysine9
+ 2 succinate + 2 formaldehyde + 2 CO2

Synonyms

5qNCA, AN1060, BHC110, CG15835, CG33182, Dmel\Kdm4A, GASC1, H3K9 demethylase, H3K9 trimethyl demethylase, H3K9-specific demethylase, H3K9/36me3 lysine demethylase, H3K9me2/3 demethylase, H3K9Me3 demethylase, H3K9me3 histone demethylase, H3K9me3-specific demethylase, histone demethylase, histone demethylase JmjD2A, histone demethylase JMJD2A/KDM4A, histone demethylase JMJD2B, histone H3 demethylase, histone H3 Lys 9 demethylase, histone H3K9 demethylase, histone H3K9/H3K36 trimethyldemethylase, histone lysine demethylase, histone-3 lysine-9 di-/tri-methyl demethylase, JDHM3A, JHDM2A, JHDM2B, JHDM3A, JmjC histone lysine demethylase, JmjC-domain-containing histone demethylase 3A, JMJD1A, JMJD1B, JMJD2, JMJD2(1), JMJD2(2), JMJD2A, JMJD2A demethylase, JMJD2A/KDM4A, JMJD2B, JMJD2b histone demethylase, JMJD2C, JMJD2D, jumonji C-domaincontaining histone demethylase 3A, jumonji domain containing 2A, Jumonji domaincontaining demethylase, JumonjiC-domain-containing histone demethylase, JumonjiD2A, KDM1, KDM2B, Kdm3a, Kdm3b, KDM4, KDM4A, KDM4A lysine demethylase, KDM4A/JMJD2A, KDM4B, KDM4B/JMJD2B histone demethylase, Kdm4c, KDM4D, KDM4E, KdmA, KIAA0601, LD33386, LSD1, LSD1 demethylase, LSD1 H3 demethylase, lysine-specific demethylase 1, lysine-specific demethylase 4A, lysine-specific demethylase 4B, lysine-specific demethylase 4C, lysine-specific demethylase 4D, More, testis-enriched histone demethylase, tridemethylase of H3K9, trimethylated histone H3-lysine 9-specific demethylase, trimethyllysine-specific histone demethylase, trimethyllysine-specific JmjC HDM, [histone H3]-lysine-9 demethylase

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
                1.14.11.66 [histone H3]-trimethyl-L-lysine9 demethylase

Engineering

Engineering on EC 1.14.11.66 - [histone H3]-trimethyl-L-lysine9 demethylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H195A
site-directed mutagenesis, mutation of an Fe2+ binding residue, abolishes demethylase activity of dJMJD2(1)/CG15835
G133A
site-directed mutagenesis, the mutation in the catalytic domain abrogates enzyme activity
G138A
site-directed mutagenesis, the mutation in the catalytic domain abrogates enzyme activity
G165A
site-directed mutagenesis, the mutation in the catalytic domain abrogates enzyme activity
G170A
site-directed mutagenesis, the mutation in the catalytic domain abrogates enzyme activity
S288N
site-directed mutagenesis, the mutation in the catalytic domain abrogates enzyme activity
T289B
site-directed mutagenesis, the mutation in the catalytic domain abrogates enzyme activity
D191A
site-directed mutagenesis, the mutant shows about 95%reduced activity with H3K9me3 compared to wild-type, and no activity with H3K36me3
H188A
-
inactive
H188A/E190A
site-directed mutagenesis, inactive mutant
I71L
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
I87K
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
N202M
site-directed mutagenesis, a KDM4D demethylase-dead mutant, that binds RNA like the wild-type enzyme
N290A
site-directed mutagenesis, the mutant shows no activity with H3K36me3 and almost no activity with H3K9me3
N290D
site-directed mutagenesis, the mutant shows about 98%reduced activity with H3K9me3 compared to wild-type, and no activity with H3K36me3
N86H
KDM4E mutant, no demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
Q88K
KDM4E mutant, the mutant shows demethylation of H3K9me2, and the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
R309G
KDM4E mutant, poor demethylation of H3K9me2, but the mutant demethylates H3K9me3 to H3K9me2 and H3K9me1 in a similar manner to wild-type KDM4A
R919D
site-directed mutagenesis, the mutant is not associated with mitotic chromatin in contrast to the wild-type enzyme
S198M
site-directed mutagenesis, a KDM4C demethylase dead mutant
S288A
Y175F
site-directed mutagenesis, the mutant shows about 90%reduced activity with H3K9me3 compared to wild-type, and no activity with H3K36me3
Y177F
site-directed mutagenesis, the mutant shows about 90%reduced activity with H3K9me3 compared to wild-type, and no activity with H3K36me3
additional information