Literature summary for 1.14.99.66 extracted from

Kong, X.; Ouyang, S.; Liang, Z.; Lu, J.; Chen, L.; Shen, B.; Li, D.; Zheng, M.; Li, K.K.; Luo, C.; Jiang, H.
Catalytic mechanism investigation of lysine-specific demethylase 1 (LSD1) a computational study (2011), PLoS ONE, 6, e25444 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
modeling of the complex composed of LSD1, cofactor CoREST, and histone substrate	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O60341	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the rate-limiting reductive half-reaction of LSD1 employs a direct hydride transfer mechanism. Conserved residue Tyr761 and the lysine-water-flavin motif help properly orienting FAD with respect to substrate, thereby stabilizing the catalytic environment and facilitating the demethylation reaction	Homo sapiens	?	-	?
[histone H3]-N6,N6-L-dimethyllysine4 + O2 + 2 H2O	-	Homo sapiens	[histone H3]-N6,N6-L-dimethyllysine4 + 2 formaldehyde + 2 H2O2	-	?

Cofactor

Cofactor	Comment	Organism	Structure
FAD	-	Homo sapiens

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Release 2023.1 (January 2023)