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Information on EC 1.14.11.27 - [histone H3]-dimethyl-L-lysine36 demethylase and Organism(s) Drosophila melanogaster and UniProt Accession Q9V6L0

for references in articles please use BRENDA:EC1.14.11.27
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IUBMB Comments
Requires iron(II). Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys36. Lysine residues exist in three methylation states (mono-, di- and trimethylated). The enzyme preferentially demethylates the dimethyl form of Lys36 (K36me2), which is its natural substrate, to form the monomethylated and unmethylated forms of Lys36. It can also demethylate monomethylated (but not the trimethylated) Lys36. cf. EC 1.14.11.69, [histone H3]-trimethyl-L-lysine36 demethylase.
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Drosophila melanogaster
UNIPROT: Q9V6L0
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The taxonomic range for the selected organisms is: Drosophila melanogaster
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
jmjd2a, kdm4b, kdm2b, kdm4a, kdm2a, kdm4c, lysine demethylase, jmjd5, kdm4d, gasc1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
[histone-H3]-lysine-36 demethylase 1
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SYSTEMATIC NAME
IUBMB Comments
[histone H3]-N6,N6-dimethyl-L-lysine36,2-oxoglutarate:oxygen oxidoreductase
Requires iron(II). Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys36. Lysine residues exist in three methylation states (mono-, di- and trimethylated). The enzyme preferentially demethylates the dimethyl form of Lys36 (K36me2), which is its natural substrate, to form the monomethylated and unmethylated forms of Lys36. It can also demethylate monomethylated (but not the trimethylated) Lys36. cf. EC 1.14.11.69, [histone H3]-trimethyl-L-lysine36 demethylase.
CAS REGISTRY NUMBER
COMMENTARY hide
55071-98-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
show the reaction diagram
additional information
?
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dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[histone H3]-N6,N6-dimethyl-L-lysine36 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine36 + 2 succinate + 2 formaldehyde + 2 CO2
show the reaction diagram
additional information
?
-
-
dynamic nature of histone methylation regulation on four of the main lysine sites of methylation on histone H3 and H4 tails, i.e. H3K4, H3K9, H3K27 and H3K36, overview. Methylation of non-histone proteins may be a general means to regulate epigenetic information
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?
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
HP1a
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H3K36 demethylation activity of the fly dKDM4A is dramatically stimulated upon HP1a association
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group gene silencing as a mode of histone crosstalk, the enzyme acts as part of the dRING-associated factor, dRAF, a Polycomb group silencing complex harboring also the histone H2A ubiquitin ligase dRING, Posterior sex combs and the F-box protein, overview. dRAF and PCR1 are separtate Polycomb group complexes, dKDM2 and PRC1 control overlapping transcriptomes, mechanisms, overview
physiological function
in vivo, the enzyme cooperates with Polycomb but antagonizes gene activation by particular trxG methyltransferases, gene dkdm2 is an enhancer of Polycomb but a suppressor of histone methyltransferases trx and ash1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lagarou, A.; Mohd-Sarip, A.; Moshkin, Y.; Chalkley, G.; Bezstarosti, K.; Demmers, J.; Verrijzer, C.
dKDM2 couples histone H2A ubiquitylation to histone H3 demethylation during Polycomb group silencing
Genes Dev.
22
2799-2810
2008
Drosophila melanogaster (Q9VHH9)
Manually annotated by BRENDA team
Lan, F.; Shi, Y.
Epigenetic regulation: methylation of histone and non-histone proteins
Sci. China C Life Sci.
52
311-322
2009
Drosophila melanogaster
Manually annotated by BRENDA team