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. Author manuscript; available in PMC: 2019 Oct 2.
Published in final edited form as: Structure. 2018 Aug 16;26(10):1337–1345.e3. doi: 10.1016/j.str.2018.07.005

Table 1.

Summary of biochemical data on PGM1 loop mutants

Name Source mutation Sol. protein
(%)
MW
(kD)
Polydispersity
(%)
Rh
(nm)
T0.5
(°)
kcat
(1/s)
Km
(μM)
kcat / Km
(μM/s)
Phosphorylation before/after G16P
(%)
WTa - 90 67 20 3.7 46.3 143+/−2 80 +/−4 1.8+/−0.1 35 / 90
R503A in-house 90 63 21 3.8 n.d. n.c. n.c. n.c. 40 / 85
R503Qb patient 90 72 0 3.8 48.7 n.c. n.c. n.c. 25 / 92
G508R ExAC 80 10
2
18 4.3 - - - - 34 / 79
G511R ExAC,
Cosmic
80 22
2
0 6.0 - - - - 13 / 82
R515A in-house 90 51 19 3.3 n.d. n.c. n.c. n.c. 31 / 87
R515Lb patient 75 68 15 3.7 46.8 n.c. n.c. n.c. 33 / 49
R515Q Cosmic 90 53 19 3.3 47.6 n.c. n.c. n.c. 34 / 82
R515W ExAC, Cosmic 70 66 16 3.6 44.9 n.c. n.c. n.c. 17 / 36

Abbreviations: n.c. – not characterizable; n.d. – not done; (−) unable to assess due to aggregation;

ExAC: Exome Aggregation Consortium (Lek et al., 2016); Cosmic: Catalog of Somatic Mutations in Cancer (Forbes et al., 2017).

a

Data for WT PGM1 previous published (Lee et al., 2014) except for T (this study).

b

0.5 Kinetic data previously published (Wong et al., 2015).

Phosphorylation assessed via electrospray ionization mass spectrometry as described in Methods.