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Table 5 Relative cleavage frequencies of wild type and mutated CsnN174 chitosanases from (GlcN)6 hydrolysis at 50% of substrate depletion calculated from data on Figure 7

From: A highly conserved arginine residue of the chitosanase from Streptomyces sp. N174 is involved both in catalysis and substrate binding

 

Symmetrical cleavage

Asymmetrical cleavage

Enzyme

6 → 3 + 3

4 → 2 + 2

Total

6 →4 + 2

WT

5,14 (60%)

0,28 (3%)

5,42 (63%)

3,19 (37%)

R42E

5,66 (66%)

0,65 (8%)

6,21 (74%)

2,23 (26%)

R42K

5,73 (65%)

0,53 (6%)

6,26 (71%)

2,60 (29%)