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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).