Skip to main content

Table 1 Biochemical properties of wild-type and mutated forms of Cc GlgP.

From: Orthophosphate binding at the dimer interface of Corynebacterium callunae starch phosphorylase: mutational analysis of its role for activity and stability of the enzyme

  PLP activity
  [μM/μM protein] [U/mg] kcat [s-1]
wild-type 0.7 31 47
T28A 0.6 29 44
K31A 0.6 29 44
S174A 0.7 29 44
R141A 0.7 27 40
  1. Activities were measured at 30°C at pH 7.0 in a continuous coupled enzyme assay in the presence of 50 mM Pi and 24 g/l maltodextrin (Agenamalt 19DE). The kcat value was calculated from the specific activity (U/mg) assuming a molecular mass of 90.6 kDa for the enzyme subunit. PLP values have S.D. of < 20% (N = 3) while activity values have S.D. of < 10% (N = 4).