. Author manuscript; available in PMC: 2022 Jan 1.

Published in final edited form as: Eur J Drug Metab Pharmacokinet. 2021 Jan;46(1):105–118. doi: 10.1007/s13318-020-00653-1

Table 2.

Kinetic constants of the human SULT1E1 allozymes in catalyzing the sulfation of E2

SULT1E1 allozyme	V_max (nmol/min/mg)	K_m (μM)	V_max/K_m (ml/min/mg)
SULT1E1-WT¹	19.30 ± 1.2	2.07 ± 0.42	9.51 ± 1.38
SULT1E1-A43D	24.98 ±2.92^****	5.12 ± 0.9^****	4.91 ± 0.23^****
SULT1E1-A131P	22.48 ± 2.66^****	3.99 ± 0.94^****	5.74 ± 0.71^****
SULT1E1-R186L	10.31 ± 1.29^****	1.55 ± 0.42^****	6.84 ± 1.06^****
SULT1E1-P214T	7.79 ± 0.89^****	1.53 ± 0.41^****	5.24 ± 0.85^****
SULT1E1-D220V	23.15 ± 4.35^****	5.27 ± 1.4^****	4.49 ± 1.99^****

Data shown represent mean ± SD derived from 3 independent experiments. One-way ANOVA was performed followed by Tukey’s post hoc analysis.

^****

Statistical significant p<0.0001 from SULT1E1-WT.

Wild-type SULT1E1