. 2021 Nov 15;60(47):3621–3632. doi: 10.1021/acs.biochem.1c00672

Table 2. Product Inhibition Patterns and Inhibition Constants^a.

variable substrate	product	type of inhibition	inhibition constant (μM)
ATP	SAM	U^b	K_ii = 230 ± 50^b^,^d
		NC^c	K_ii = 275 ± 30^c
		NC^c	K_is = 620 ± 130^c
ATP	pyrophosphate	NC^b	K_ii = 800 ± 100^b^,^e
ATP	pyrophosphate	NC^b	K_is = 210 ± 10^b^,^e
ATP	phosphate	NC^b	K_ii = 5740 ± 760^b
ATP	phosphate	NC^b	K_is = 1290 ± 170^b
l-Met	SAM	NC^b	K_ii = K_is = 190 ± 10^b
l-Met	SAM	NC^c	K_ii = K_is = 250 ± 10^c
l-Met	pyrophosphate	NC^b	K_ii = 660 ± 40^b
l-Met	pyrophosphate	NC^b	K_is = 180 ± 20^b
l-Met	phosphate	NC^b	K_ii = 4970 ± 770^b
l-Met	phosphate	NC^b	K_is = 1580 ± 360^b

At pH 7.5 and 22 °C.

Saturating concentrations of the co-substrate: 0.6 mM l-Met, 0.5 or 1 mM ATP.

Nonsaturating concentrations of the co-substrate.

Average of six independent experiments; error shows standard deviation.

Average of two independent experiments; error shows standard deviation: 0.02 mM l-Met, 0.07 mM ATP. U indicates uncompetitive inhibition and NC indicates noncompetitive inhibition.

Table 2. Product Inhibition Patterns and Inhibition Constantsa.

Table 2. Product Inhibition Patterns and Inhibition Constants^a.