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Information on EC 1.14.11.27 - [histone H3]-dimethyl-L-lysine36 demethylase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P40034

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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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Saccharomyces cerevisiae
UNIPROT: P40034
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
JmjC domain-containing histone demethylase 1
-
JmjC domain-containing histone demethylation protein 1
-
H3-K36 demethylase
-
-
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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethyl-histone 3 L-lysine 36 + 2-oxoglutarate + O2
methyl-histone 3 L-lysine 36 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
protein 6-N,6-N-dimethyl-L-lysine + 2-oxoglutarate + O2
protein 6-N-methyl-L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
-
specifically demethylates Lys36 of histone H3
-
-
?
protein 6-N-methyl-L-lysine + 2-oxoglutarate + O2
protein L-lysine + succinate + formaldehyde + CO2
show the reaction diagram
-
specifically demethylates Lys36 of histone H3
-
-
?
additional information
?
-
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,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
show the reaction diagram
-
-
-
?
additional information
?
-
enzyme Jhd1 is also active on H3K9 methyl groups
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
required for catalysis
Iron
Fe2+ is required
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbate
stimulation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
changes in RENT component recruitment at NTS regions due to loss of H3 methylases or demethylases
metabolism
different roles of histone H3 methylases in regulating Net1/Sir2 recruitment to rDNA regions and the resultant rDNA silencing. In particular, both H3K4 and H3K79 methylation by Set1 and Dot1 positively regulate rDNA silencing, whereas H3K36 methylation by Set2 has the opposite effect
physiological function
changes in histone H3 lysine methylation levels distinctly regulate rDNA silencing by recruiting different silencing proteins to rDNA, thereby contributing to rDNA silencing and nucleolar organization in yeast. Jhd1 positively affects transcription
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
250000
gel filtration
56500
x * 56500, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
x * 56500, calculated
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
phosphorylation at Ser44 is required for cold stress response
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H305A
more than 90% loss of activity
T302A
more than 90% loss of activity
Y315A
more than 90% loss of activity
H305A
-
mutation completely abolishes the enzymatic activity
additional information
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of Flag-tagged protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsukada, Y.; Fang, J.; Erdjument-Bromage, H.; Warren, M.E.; Borchers, C.H.; Tempst, P.; Zhang, Y.
Histone demethylation by a family of JmjC domain-containing proteins
Nature
439
811-816
2006
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Fang, J.; Hogan, G.J.; Liang, G.; Lieb, J.D.; Zhang, Y.
The Saccharomyces cerevisiae histone demethylase Jhd1 fine-tunes the distribution of H3K36me2
Mol. Cell. Biol.
27
5055-5065
2007
Saccharomyces cerevisiae (P40034)
Manually annotated by BRENDA team
Ryu, H.; Ahn, S.
Yeast histone H3 lysine 4 demethylase Jhd2 regulates mitotic ribosomal DNA condensation
BMC Biol.
12
75
2014
Saccharomyces cerevisiae (P40034)
Manually annotated by BRENDA team
Separovich, R.J.; Wong, M.W.M.; Bartolec, T.K.; Hamey, J.J.; Wilkins, M.R.
Site-specific phosphorylation of histone H3K36 methyltransferase Set2p and demethylase Jhd1p is required for stress responses in Saccharomyces cerevisiae
J. Mol. Biol.
434
167500
2022
Saccharomyces cerevisiae (P40034)
Manually annotated by BRENDA team