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Figure 7 | BMC Biochemistry

Figure 7

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

Figure 7

Time-courses of (GlcN) 6 hydrolysis catalyzed by wild-type, R42K and R42E chitosanases monitored by real-time mass spectrometry. The enzymatic reactions were carried out in 10 mM ammonium acetate-containing aqueous solutions pH 5.2 at 20°C. A) (GlcN)6 hydrolysis time-courses obtained for wild type endochitosanase (5.0 nM)-catalyzed reaction performed with 25.0 μM of the substrate (GlcN)6; B) (GlcN)6 hydrolysis time-courses obtained for R42K chitosanase (62.5 nM)-catalyzed reaction performed with 25.0 μM of the substrate (GlcN)6; C) (GlcN)6 hydrolysis time-courses obtained for R42E chitosanase (5.0 nM)-catalyzed reaction performed with 25.0 μM of the substrate (GlcN)6.

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BMC Biochemistry

ISSN: 1471-2091

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