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

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

Activities were measured at 30°C at pH 7.0 in a continuous coupled enzyme assay in the presence of 50 mM P_i and 24 g/l maltodextrin (Agenamalt 19DE). The k_cat 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).

ISSN: 1471-2091