. Author manuscript; available in PMC: 2023 Jun 9.

Published in final edited form as: Biochemistry. 2018 May 11;57(25):3480–3492. doi: 10.1021/acs.biochem.8b00223

Table 2.

The steady-state kinetic constants and inhibition dissociation constants for IMP measured for wild-type PMM1 (WT PMM1), PMM1 variants, and PMM2 for mutase activity converting Glu-1-P to Glu-6-P (see Materials and Methods). ND = no activity detected

Protein	Kinetic constants for Mutase Activity
	k_cat (s⁻¹)	K_m (μM)	k_cat/K_m (M⁻¹s⁻¹)	K_i^IMP μM

WT PMM1^a	1.3 ± 0.045	19 ± 2.1	6.8 x 10⁴	2.0 ± 0.31
R180T/R183I PMM1	1.6 ± 0.055	17 ± 2.1	9.4 x 10⁴	780 ± 47
R183I PMM1	1.0 ± 0.020	8.0 ± 0.74	1.3 x 10⁵	350 ± 25
R180T PMM1	0.9 ± 0.030	28 ± 2.8	3.2 x 10⁴	2.3 ± 0.24
M186Q PMM1	1.1 ± 0.063	10 ± 2.1	1.1 x 10⁵	2.8 ± 0.28
R108K/R183K PMM1	2.1 ± 0.19	13 ± 3.9	1.6 x 10⁵	2.0 ± 0.30
WT PMM2^a	1.0 ± 0.058	8.0 ± 1.8	1.3 x 10⁵	> 4000
T171R/I174R PMM2	ND	ND	ND

Also previously measured in ^1,2