Table 2 Phosphatase activity of PGAM5 and its oligomerization-deficient mutants

From: Functional role of PGAM5 multimeric assemblies and their polymerization into filaments

Protein

Km (µM)

Kcat (min−1)

Kcat/Km (min−1 M−1)

∆48 WT

115.2 ± 5.0

137.20 ± 2.98

1.19 (±0.06) × 106

∆48 H105A

ND

ND

ND

∆48 R288E

174.70 ± 26.99

143.30 ± 12.73

0.82 (± 0.15) × 106

∆48 F244E

ND

ND

ND

∆48 A4

ND

ND

ND

∆48 R65A

119.9 ± 15.7

23.17 ± 1.55

0.19 (±0.03) × 106

∆48 Y198E

86.17 ± 6.19

51.65 ± 1.68

0.60 (±0.05) × 106

  1. Dephosphorylation of the ASK1 phosphopeptide by WT and mutant variants of ∆48 PGAM5 was measured at 20 nM of enzyme concentration and varying concentrations of ASK1 substrate. The kinetic parameters Km, kcat, and kcat/Km were determined using GraphPad Prism software. Kinetic data for PGAM5 variants without measurable phosphatase activity are denoted ND (not determined). Data are represented as mean ± S.E.M.
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