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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%)