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Literature summary extracted from

  • Yang, M.; Culhane, J.C.; Szewczuk, L.M.; Jalili, P.; Ball, H.L.; Machius, M.; Cole, P.A.; Yu, H.
    Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine (2007), Biochemistry, 46, 8058-8065 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.99.66 expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.14.99.66 structure of LSD1 in complex with cofactor CoREST and inhibitor rans-2-phenylcyclopropylamine. The inhibitor forms a covalent adduct with FAD in LSD1. The phenyl ring of the FAD-inhibitor adduct does not form extensive interactions with active-site residues Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.99.66 trans-2-phenylcyclopropylamine i.e. tranylcypromine; Parnate. Mechanism-based suicide inactivator, inactivation of LSD1 occurs with similar rates as the demethylation of substrates Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.99.66 0.05
-
 [histone H3]-N6,N6-L-dimethyllysine21 pH 7.5, 25°C Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.14.99.66 Homo sapiens O60341
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.99.66 [histone H3]-N6,N6-L-dimethyllysine21 + O2 + 2 H2O diMeK4H3-21 i.e. a dimethyl K4-containing histone H3 peptide Homo sapiens [histone H3]-L-lysine + 2 formaldehyde + 2 H2O2
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.99.66 0.051
-
 [histone H3]-N6,N6-L-dimethyllysine21 pH 7.5, 25°C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.99.66 FAD
-
 Homo sapiens