Lysine (K)-specific demethylase 1B (KDM1B)

KDM1B, known as lysine (K)-specific demethylase 1B, is a flavin-dependent histone demethylase enzyme that catalyzes the removal of methyl groups from mono- and di-methylated lysine 4 on histone H3 (H3K4me1/2), marks typically associated with active transcription. This activity is crucial for epigenetic regulation of gene expression and the establishment of maternal DNA methylation imprints during oogenesis, which are necessary for proper development. KDM1B contains zinc finger motifs, a SWIRM domain, and shares structural similarity with other chromatin-remodeling enzymes. In addition to demethylase-dependent roles, KDM1B can mediate transcriptional repression independently of demethylase activity when tethered to DNA. Disruption of KDM1B function leads to defective imprinting, abnormal gene silencing or activation, developmental disorders, and early embryonic lethality. It is considered a therapeutic and research target in diseases involving epigenetic dysregulation, such as cancer and imprinting disorders.

Other names

LSD2AOF1BA204B7.3DJ298J15.2C6ORF193

Inhibition of histone demethylase activity, preventing removal of methyl groups from H3K4me1/2, leading to altered gene expression and chromatin state. Indirect modulation of DNA methylation and imprinting through altered histone marks. Potential induction of cell differentiation and apoptosis in cancer cells as a result of epigenetic modulation.