Table 1.

Kinetic Parameters of the Catalytic Activity of chKDM1AΔTower with the First 21 Amino Acids of H3 Dimethylated at K4 (H3K4me2^1–21).

Enzyme Name	$K_{\mathrm{m}}^{\text{app}}(\mathrm{\mu }\mathrm{M})$	$k_{\text{cat}}^{\text{app}}({\text{min}}^{-1})$	$k_{\text{cat}}^{\text{app}}/K_{\mathrm{m}}^{\text{app}}(\mathrm{\mu }{\mathrm{M}}^{-1}{\text{min}}^{-1})$
nΔ150 KDM1A wta,b	2.60 ± 0.2	5.97 ± 0.78	2.28 ± 0.12
nΔ25 mKDM1B wtc	11.3 ± 1.3	2.00 ± 0.60	0.18 ± 0.04
chKDM1AΔTowera	3.21 ± 0.16	0.57 ± 0.01	0.18 ± 0.01

^aIn 50 mM Tris–HCl (pH 7.85), 0.01% CHAPS (w/v), 50 µM Amplex Red & 1 U/mL HRP at 25 °C in air saturated buffer; peptide titrated from 50 µM to 0 in 2-fold dilution series (n = 3).

^bValues reported by Gaweska et al. [31].

^cValues reported by Karytinos et al. [24].