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Literature summary extracted from

  • Brasacchio, D.; Okabe, J.; Tikellis, C.; Balcerczyk, A.; George, P.; Baker, E.K.; Calkin, A.C.; Brownlee, M.; Cooper, M.E.; El-Osta, A.
    Hyperglycemia induces a dynamic cooperativity of histone methylase and demethylase enzymes associated with gene-activating epigenetic marks that coexist on the lysine tail (2009), Diabetes, 58, 1229-1236 .
    View publication on PubMedView publication on EuropePMC

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.11.65 nucleus
-
Homo sapiens 5634
-
1.14.11.65 nucleus
-
Mus musculus 5634
-
1.14.99.66 nucleus
-
Homo sapiens 5634
-
1.14.99.66 nucleus
-
Mus musculus 5634
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.11.65 [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 Homo sapiens
-
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 Mus musculus
-
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2 Mus musculus C57BL/6
-
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2 Homo sapiens
-
[histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2 Mus musculus
-
[histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2 Mus musculus C57BL/6
-
[histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.99.66 [histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2 Homo sapiens
-
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
?
1.14.99.66 [histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2 Mus musculus
-
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
?
1.14.99.66 [histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2 Mus musculus C57BL/6
-
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
?
1.14.99.66 [histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2 Homo sapiens
-
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
?
1.14.99.66 [histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2 Mus musculus
-
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.11.65 Homo sapiens O60341
-
-
1.14.11.65 Mus musculus Q6ZQ88 male apolipoprotein knockout (apoE KO) mice
-
1.14.11.65 Mus musculus C57BL/6 Q6ZQ88 male apolipoprotein knockout (apoE KO) mice
-
1.14.99.66 Homo sapiens O60341
-
-
1.14.99.66 Mus musculus Q6ZQ88 male apolipoprotein knockout (apoE KO) mice
-
1.14.99.66 Mus musculus C57BL/6 Q6ZQ88 male apolipoprotein knockout (apoE KO) mice
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.11.65 additional information the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 and H3K4me2/me1 (EC 1.14.99.66) Homo sapiens ?
-
?
1.14.11.65 additional information the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 and H3K4me2/me1 (EC 1.14.99.66) Mus musculus ?
-
?
1.14.11.65 additional information the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 and H3K4me2/me1 (EC 1.14.99.66) Mus musculus C57BL/6 ?
-
?
1.14.11.65 [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
-
Homo sapiens [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
-
Mus musculus [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
-
Mus musculus C57BL/6 [histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2
-
Homo sapiens [histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2
-
Mus musculus [histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.11.65 [histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2
-
Mus musculus C57BL/6 [histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
-
?
1.14.99.66 additional information the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1 Homo sapiens ?
-
?
1.14.99.66 additional information the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1 Mus musculus ?
-
?
1.14.99.66 additional information the bifunctional enzyme catalyzes the demethylation of H3K9me2/me1 (EC 1.14.11.65) and H3K4me2/me1 Mus musculus C57BL/6 ?
-
?
1.14.99.66 [histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
-
Homo sapiens [histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
?
1.14.99.66 [histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
-
Mus musculus [histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
?
1.14.99.66 [histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
-
Mus musculus C57BL/6 [histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
-
?
1.14.99.66 [histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
-
Homo sapiens [histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
?
1.14.99.66 [histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
-
Mus musculus [histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
1.14.11.65 LSD1
-
Homo sapiens
1.14.11.65 LSD1
-
Mus musculus
1.14.11.65 More see also for EC 1.14.99.66 Homo sapiens
1.14.11.65 More see also for EC 1.14.99.66 Mus musculus
1.14.99.66 LSD1
-
Homo sapiens
1.14.99.66 LSD1
-
Mus musculus
1.14.99.66 More see also for EC 1.14.11.65 Homo sapiens
1.14.99.66 More see also for EC 1.14.11.65 Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.99.66 FAD
-
Homo sapiens
1.14.99.66 FAD
-
Mus musculus

General Information

EC Number General Information Comment Organism
1.14.11.65 additional information transient hyperglycemia induces recruitment of LSD1 to gene regulation sites/promoters. Transient hyperglycemia causes a sustained reduction in both H3K9m2 and H3K9m3 on the NFkappaB-p65 promoter Homo sapiens
1.14.11.65 additional information transient hyperglycemia induces recruitment of LSD1 to gene regulation sites/promoters. Transient hyperglycemia causes a sustained reduction in both H3K9m2 and H3K9m3 on the NFkappaB-p65 promoter Mus musculus
1.14.11.65 physiological function LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active methylation mark. LSD1 is associated with co-repressor complexes and promotes suppression or activation of gene expression, e.g. LSD1 might be associated to cooperative recruitment to the NFkappaB p65 site for activation in hyperglycemia Homo sapiens
1.14.11.65 physiological function LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active methylation mark. LSD1 is associated with co-repressor complexes and promotes suppression or activation of gene expression, e.g. LSD1 might be associated to cooperative recruitment to the NFkappaB p65 site for activation in hyperglycemia Mus musculus
1.14.99.66 additional information transient hyperglycemia induces recruitment of LSD1 to gene regulation sites/promoters Homo sapiens
1.14.99.66 additional information transient hyperglycemia induces recruitment of LSD1 to gene regulation sites/promoters Mus musculus
1.14.99.66 physiological function LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active methylation mark. LSD1 is associated with co-repressor complexes and promotes suppression or activation of gene expression, e.g. LSD1 might be associated to cooperative recruitment to the NFkappaB p65 site for activation in hyperglycemia Homo sapiens
1.14.99.66 physiological function LSD1 is a nuclear amine oxidase that utilizes oxygen as an electron acceptor to reduce methylated lysine to form lysine. It demethylates H3K4m1 and H3K4m2, as well as H3K9m1 and H3K9m2 as a removal of the active methylation mark. LSD1 is associated with co-repressor complexes and promotes suppression or activation of gene expression, e.g. LSD1 might be associated to cooperative recruitment to the NFkappaB p65 site for activation in hyperglycemia Mus musculus