Any feedback?
Literature summary for 1.14.99.66 extracted from
- New roles of flavoproteins in molecular cell biology: histone demethylase LSD1 and chromatin (2009), FEBS J., 276, 4304-4312.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| CoREST | the co-repressor CoREST stabilizes LSD1 and increases in vitro LSD1 activity by approximately twofold and is essential for LSD1-mediated demethylation in intact nucleosomes in vivo and for the in vitro demethylation of nucleosomal particles, binding structure, overview | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| enzyme complex LSD1-CoREST crystal structure in complex with a histone H3 peptide, overview | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K661A | site-directed mutagenesis, inactive mutant | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| nucleosome | - |
Homo sapiens | 786 | - |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Homo sapiens | LSD1 interacts with CoREST, a co-repressor protein that binds REST and recruits other histone-modifying enzymes such as histone deacetylases 1 ? 2. The function of the LSD1CoRESThistone deacetylase subcomplex in transcriptional repression events is not limited to REST-regulated neuronal genes, but can be extended to other contexts such as hematopoietic differentiation and the telomerase reverse transcriptase genes | ? | - |
? |  |
| [histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 | Drosophila melanogaster | - |
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2 | - |
? | |
| [histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 | Homo sapiens | - |
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2 | - |
? | |
| [histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 | Arabidopsis thaliana | - |
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2 | - |
? | |
| [histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 | Caenorhabditis elegans | - |
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2 | - |
? | |
| [histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2 | Drosophila melanogaster | - |
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2 | - |
? | |
| [histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2 | Homo sapiens | - |
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2 | - |
? | |
| [histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2 | Arabidopsis thaliana | - |
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2 | - |
? | |
| [histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2 | Caenorhabditis elegans | - |
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | - |
- |
- |
| Caenorhabditis elegans | - |
- |
- |
| Drosophila melanogaster | - |
- |
- |
| Homo sapiens | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | LSD1 interacts with CoREST, a co-repressor protein that binds REST and recruits other histone-modifying enzymes such as histone deacetylases 1 ? 2. The function of the LSD1CoRESThistone deacetylase subcomplex in transcriptional repression events is not limited to REST-regulated neuronal genes, but can be extended to other contexts such as hematopoietic differentiation and the telomerase reverse transcriptase genes | Homo sapiens | ? | - |
? | |
| additional information | LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview | Drosophila melanogaster | ? | - |
? | |
| additional information | LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview | Homo sapiens | ? | - |
? | |
| additional information | LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview | Arabidopsis thaliana | ? | - |
? | |
| additional information | LSD1 is specific for Lys4 of both mono- and dimethylated histone H3 using a highly specific recognition mechanism, LSD1-catalyzed reaction produces an imine intermediate that is hydrolyzed to the demethylated product and formaldehyde, Reduced flavin is reoxidized by molecular oxygen with the concomitant production of hydrogen peroxide, overview | Caenorhabditis elegans | ? | - |
? | |
| [histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 | - |
Drosophila melanogaster | [histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2 | - |
? | |
| [histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 | - |
Homo sapiens | [histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2 | - |
? | |
| [histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 | - |
Arabidopsis thaliana | [histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2 | - |
? | |
| [histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2 | - |
Caenorhabditis elegans | [histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2 | - |
? | |
| [histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2 | - |
Drosophila melanogaster | [histone H3]-L-lysine4 + succinate + formaldehyde + CO2 | - |
? | |
| [histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2 | - |
Homo sapiens | [histone H3]-L-lysine4 + succinate + formaldehyde + CO2 | - |
? | |
| [histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2 | - |
Arabidopsis thaliana | [histone H3]-L-lysine4 + succinate + formaldehyde + CO2 | - |
? | |
| [histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2 | - |
Caenorhabditis elegans | [histone H3]-L-lysine4 + succinate + formaldehyde + CO2 | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | LSD1 is a multidomain protein | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| histone demethylase | - |
Drosophila melanogaster |
| histone demethylase | - |
Homo sapiens |
| histone demethylase | - |
Arabidopsis thaliana |
| histone demethylase | - |
Caenorhabditis elegans |
| LSD1 | - |
Drosophila melanogaster |
| LSD1 | - |
Homo sapiens |
| LSD1 | - |
Arabidopsis thaliana |
| LSD1 | - |
Caenorhabditis elegans |
| More | LSD1 is a flavin-dependent amine axidase | Drosophila melanogaster |
| More | LSD1 is a flavin-dependent amine axidase | Homo sapiens |
| More | LSD1 is a flavin-dependent amine axidase | Arabidopsis thaliana |
| More | LSD1 is a flavin-dependent amine axidase | Caenorhabditis elegans |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | dependent on | Drosophila melanogaster | |
| FAD | dependent on | Homo sapiens | |
| FAD | dependent on | Arabidopsis thaliana | |
| FAD | dependent on | Caenorhabditis elegans | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | LSD1 plays a role in gene expression regulation, it is a multidomain protein and its involvement in many diverse gene-expression programs is strictly related to its domain organization | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
